Novel Aspects of Blood Coagulation Factor XIII. I. Structure, Distribution, Activation, and Function

References

• Barkan G, Gaspar A. Zur Frage der Reversibilität der Fibringerinnung II. Biochem Z 1923; 139: 291–301
   Google Scholar
• Robbins K C. A study on the conversion of fibrinogen to fibrin. Am J Physiol 1944; 142: 581–8
   Google Scholar
• Laki K, Lóránd L. On the solubility of fibrin clots. Science 1948; 108: 280
   PubMed Web of Science ®Google Scholar
• Lóránd L. A study on the solubility of fibrin clots in urea. Acta Physiol Acad Sci Hung 1948; 1: 192–6
   Google Scholar
• Lóránd L. Fibrin clots. Some properties of the “serum factor. Nature (London) 1950; 166: 694–6
   PubMedGoogle Scholar
• Loewy A G, Veneziale C Forman M. Purification of the factor involved in formation of urea-insoluble fibrin. Biochim Biophys Acta 1957; 26: 670–1
   PubMedGoogle Scholar
• Loewy A G, Dunathan K, Kriel K, Wolfinger J. Fibrinase. I. Purification of substrate and enzyme. J Biol Chem 1961; 236: 2625–33
   PubMedGoogle Scholar
• Loewy A G, Dahlberg A, Dunathan K. Fibrinase. II. Some physical properties. J Biol Chem 1961; 236: 2634–43
   PubMedGoogle Scholar
• Loewy A G, Dunathan K, Gallant J A. Fibrinase. III. Some enzymatic properties. J Biol Chem 1961; 236: 2644–7
   PubMedGoogle Scholar
• Loewy A G, Gallant J A, Dunathan K. Fibrinase. IV. Effect on fibrin solubility. J Biol Chem 1961; 236: 2648–55
   PubMedGoogle Scholar
• Duckert F, Jung E Shmerling D H. A hitherto undescribed congenital haemorrhagic diathesis probably due to fibrin stabilizing factor deficiency. Thromb Diath Haemorrh 1960; 5: 179–86
   PubMedGoogle Scholar
• Folk J A, Finlayson J S. The epsilon(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminases. Adv Protein Chem 1977; 31: 1–133
   PubMedGoogle Scholar
• Lóránd L, Losowsky M S, Miloszewski K JM. Human factor XIII: fibrin-stabilizing factor. Prog Haemost Thromb 1980; 5: 245–90
   PubMedGoogle Scholar
• Folk J E. Mechanism and basis for specifity of transglutaminase catalyzed epsilon(gamma glutamyl)lysine bond formation. Adv Enzymol 1983; 54: 1–56
   PubMedGoogle Scholar
• Muszbek L, Laki K. Interaction of thrombin with proteins other than fibrinogen (thrombin susceptible bonds). Activation of factor XIII. The thrombin, R Machovich. CRC Press, Boca Raton, FL 1984; 83–102
   Google Scholar
• Lóránd L. Activation of blood coagulation factor XIII. Ann NY Acad Sci 1986; 485: 144–58
   PubMedGoogle Scholar
• Mc Donagh J. Structure and function of factor XIII. Haemostasis and thrombosis, RW Colman, J Hirsh, VJ Marder, EW Salzman. Lippincott, Philadelphia 1982; 164–73
   Google Scholar
• Miloszewski K JA, Losowsky M S. Fibrin stabilization and factor XIII deficiency. Fibrinogen, fibrin stabilisation and fibrinolysis, JL Francis. Ellis Horwood, Chichester 1988; 175–202
   Google Scholar
• Ichinose A, Hendrickson L E, Fujikawa K. Amino acid sequence of the a subunit of human factor XIII. Biochemistry 1986; 25: 6900–6
   PubMed Web of Science ®Google Scholar
• Ichinose A, McMullen B, Fujikawa K. Amino acid sequence of the b subunit of human factor XIII, a protein composed of ten repetitive segments. Biochemistry 1986; 25: 4633–38
   PubMedGoogle Scholar
• Grundmann U, Amann E, Zettlmeissl G. Characterization of cDNA coding for human factor XIIIa. Proc Natl Acad Sci USA 1986; 83: 8024–8
   PubMed Web of Science ®Google Scholar
• Takahashi N, Takahashi Y, Putnam F W. Primary structure of blood coagulation XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci USA 1986; 83: 8019–23
   PubMed Web of Science ®Google Scholar
• Ichinose A, Davie E. Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci USA 1988; 85: 5829–33
   PubMed Web of Science ®Google Scholar
• Bohn H. The human fibrin-stabilizing factor. Mol Cell Biochem 1978; 20: 67–75
   PubMedGoogle Scholar
• Board P G, Webb G C, McKee J. Localization of the coagulation factor XIII A-subunit gene (F13A) to chromosome bands 6p24–25. Cytogenet Cell Genet 1988; 48: 25–7
   PubMedGoogle Scholar
• Korsgren C, Cohen C M. Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII. Proc Natl Acad Sci USA 1991; 88: 4840–44
   PubMedGoogle Scholar
• Aeschlimann D, Paulsson M. Transglutaminases: protein cross-linking reactions in tissues and body fluids. Thrombos Haemostas 1994; 71: 402–15
   PubMed Web of Science ®Google Scholar
• Board P G, Pierce K, Coggan M. Expression of functional coagulation factor XIII in Escherichia coli. Thromb Haemost 1990; 63: 235–40
   PubMedGoogle Scholar
• Broker M, Bäuml O. New expression vectors for the fission yeas Schizosaccharomyces pombe. FEBS Lett 1989; 248: 105–10
   PubMedGoogle Scholar
• Jagadeeswaran P, Haas P. Synthesis of human coagulation factor XIII in yeast. Gene 1990; 86: 279–83
   PubMedGoogle Scholar
• Bishop P D, Teller D C, Smith R A. Expresion, purification and characterization of human factor XIII in Saccharomyces cerevisiae. Biochemistry 1990; 29: 1861–9
   PubMed Web of Science ®Google Scholar
• Rodriguez de Cordoba S, Rey Campos S, Dykes D D. Coagulation Factor XIIIB subunit is encoded by a gene linked to the regulator of complement activation (RCA) gene cluster in man. Immunogenetics 1988; 28: 452–4
   PubMedGoogle Scholar
• Kompf J, Luckenbach C, Kloor D. Linkage analyses of human peptidase C (PEPC), human factor H (HF), and coagulation factor XIIIB (F13B). Hum Genet 1989; 83: 97–8
   PubMedGoogle Scholar
• Rey Campos J, Baeza-Sanz D Rodriguez de Cordoba S. Physical linkage of the genes coding for complement factor H and coagulation factor XIII B subunit. Genomics 1990; 7: 644–6
   PubMedGoogle Scholar
• Griffith L R, Board P G, Zwi M B. The B subunit of coagulation factor XIII is linked to renin, and the Duffy blood group to alpha-spectrin on human chromosome 1. Hum Hered 1989; 39: 107–9
   PubMedGoogle Scholar
• Webb G C, Coggan M, Ichinose A. Localization of coagulation factor XIII B subunit gene (F13B) to chromosome bands 1q31–32.1 and restriction fragment length polymorphism at the locus. Hum Genet 1989; 81: 157–60
   PubMed Web of Science ®Google Scholar
• Ichinose A, Bottenus R E, Davie E W. Structure of transglutaminases. J Biol Chem 1990; 265: 13411–14
   PubMed Web of Science ®Google Scholar
• Nonaka M, Matsuda Y, Shiroishi T. Molecular cloning of the b subunit of mouse coagulation factor XIII and assignment of the gene to chromosome 1: close evolutionary relationship to complement factor H. Genomics 1993; 15: 535–42
   PubMedGoogle Scholar
• Bottenus R, Ichinose A, Davie E. Nucleotide sequence of the gene for the b subunit of human factor XIII. Biochemistry 1990; 29: 11195–209
   PubMed Web of Science ®Google Scholar
• Patthy L. Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 1985; 41: 657–63
   PubMed Web of Science ®Google Scholar
• Patthy L. Detecting homology of distantly related proteins with consensus sequence. J Mol Biol 1987; 198: 567–77
   PubMedGoogle Scholar
• Board P G. Genetic polymorphism of the A subunit of human coagulation factor XIII. Am J Hum Genet 1979; 31: 116–24
   PubMedGoogle Scholar
• Board P G. Genetic polymorphism of the B subunit of human coagulation factor XIII. Am J Hum Genet 1980; 32: 348–53
   PubMedGoogle Scholar
• Board P G, Coggan M. Polymorphism of the A subunit of coagulation Factor XIII in the pacific region. Description of new halotypes. Hum Genet 1981; 59: 135–6
   PubMedGoogle Scholar
• Nishigaki T, Omoto K, Juji T. Genetic polymorphism of the A subunit of human coagulation factor XIII in Japanese. Jpn J Hum Genet 1981; 26: 237–41
   Google Scholar
• Castle M, Board P G. An extended survey of the genetic polymorphism at the human coagulation factor XIII A subunit structural locus. Hum Hered 1981; 35: 101–6
   Google Scholar
• Sebatan I M. A new method for FXIIIA genetic variants determination using isoelectric focusing in 1 M urea. Evidence for three structural gene loci, FXIIIA1, FXIIIA2 and FXIIIA3. Hum Genet 1988; 81: 95–7
   PubMedGoogle Scholar
• Suzuki K, Matsui K, Ito S. Polymorphism of the A subunit of coagulation factor XIII: evidence for subtypes of the FXIIIA*1 and FXIIIA*2 alleles. Am J Hum Genet 1988; 43: 170–4
   PubMedGoogle Scholar
• Prata M J, Amorim A. Formal and population genetics of F13A and FUCA1 polymorphism in northern Portugal. Hum Hered 1990; 40: 45–8
   PubMedGoogle Scholar
• Scacchi R, Corbo R M, Mulas G. Genetic polymorphism of the A and B subunits of human coagulation factor XIII in mainland Italy and Sardinia: description of a new FXIIIA variant allele. Electrophoresis 1991; 12: 667–70
   PubMedGoogle Scholar
• Nishigaki T, Omoto K. Genetic polymorphism of the B subunit of human coagulation factor XIII in Japanese. Jpn J Hum Gen 1982; 27: 265–70
   Google Scholar
• Board P G. Genetic heterogeneity of the B subunit of coagulation factor XIII: resolution of type 2. Ann Hum Genet 1984; 48: 223–8
   PubMedGoogle Scholar
• Miller S A, Dykes D D, Polesky H F. Gene frequency distribution of the B subunit of factor XIII (FXIIIB) in Minnesota whites, blacks, and amerindians. Electrophoresis 1985; 6: 399–401
   Google Scholar
• Kamboh M I, Ferrell R E. Genetic studies of low abundance human plasma proteins. II. Population genetics of coagulation factor XIIIB. Am J Hum Genet 1986; 39: 817–25
   PubMedGoogle Scholar
• Dykes D D, Polesky M F. The use of the serum protein factor XIIIB (FXIIIB) in parentage testing. Am J Clin Pathol 1987; 88: 627–30
   PubMedGoogle Scholar
• Leifheit H J, Cleve H. Analysis of the genetic polymorphism of coagulation factor XIIIB (FXIIIB) by isoelectric focusing. Electrophoresis 1988; 9: 426–9
   PubMedGoogle Scholar
• Kamboh M I, Ferrell R E. Genetic studies of low-abundance human plasma proteins. X. Coagulation factor XIIIB variants in blacks. Electrophoresis 1989; 10: 53–7
   PubMedGoogle Scholar
• Tela M, Scheffran W. Der Faktor 13 B (FSF)-Polymorphismus in schweizerischen Populationen, mit Betrachtungen über europäische Häufigkeitesgradienten. Anthropol Anz 1991; 49: 129–36
   PubMedGoogle Scholar
• Nevo S, Cleve H, Koller A. Serum protein polymorphism in Arab moslems and Druze of Israel. Hum Biol 1992; 64: 587–603
   PubMedGoogle Scholar
• Cleve H, Koller A, Patutschnick W. Genetic serum protein polymorphism in Jordanian Arabs: a pilot study of the systems AHSG, BF, F XIII B, GC, PI, PLG and TF. Gene Geogr 1992; 6: 31–40
   PubMedGoogle Scholar
• Sana N, Tay J S, Low P S. Population genetics of coagulation factor XIIIB in three ethnic groups of Singapore. Ann Hum Biol 1992; 19: 277–83
   PubMedGoogle Scholar
• Chen L Z, Easteal S, Board P G. Genetic affinities of oceanic populations based on RFLP and halotype analysis of genetic loci on three chromosomes. Hum Biol 1992; 64: 1–15
   PubMedGoogle Scholar
• Komatsu N, Kido A, Kimura Y. Polymorphism of coagulation factor XIII B subunit: further occurrence of FXIIIB 15 in Japanese and phenotyping in bloodstains. Int J Legal Med 1992; 317–9
   PubMedGoogle Scholar
• Cameselle F D, Caeiro B, Riveiro A. An alternative modality for the immunodetection of the molecular phenotypes of coagulation factor XIIIB. Hum Hered 1993; 43: 257–60
   PubMedGoogle Scholar
• Mizutani K, Nishimukai H, Yasugi T. Polymorphism of serum proteins in Japanese patients with vascular disease. I. Factor XIIIB, plasminogen and complement types in primary varicose veins. Hum Hered 1991; 41: 270–5
   PubMedGoogle Scholar
• Board P G, Chappie R, Coggan M. Halotypes of the coagulation Factor XIIIA subunit locus in normal and deficient subjects. Am J Hum Genet 1988; 42: 712–7
   PubMedGoogle Scholar
• Zoghbi H Y, Daiger S P, McCall A. Extensive DNA polymorphism at the factor XIIIa (F13A) locus and linkage to HLA. Am J Hum Genet 1988; 42: 877–83
   PubMedGoogle Scholar
• Board P G, Losowsky M S, Miloszewski K JA. Factor XIII; Inherited and acquired deficiency. Blood Rev 1993; 7: 229–42
   PubMed Web of Science ®Google Scholar
• Polymeropoulos M H, Rath D S, Xiao H. Tetranucleotide repeat polymorphism at the human coagulation factor XIII A subunit gene (F13A1). Nucleic Acids Res 1991; 19: 4306
   Google Scholar
• Nishimura D Y, Murray J C. A tetranucleotide repeat for the F13B locus. Nucleic Acids Res 1992; 20: 1167
   Google Scholar
• Carrell N A, Erickson H P, McDonagh J. Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem 1989; 264: 551–6
   PubMed Web of Science ®Google Scholar
• Bohn H, Schwick H G. Isolierung and Characterisierung eines fibrinstabilierenden Faktors aus menschlichen Plazenten. Arzneim Forsch 1971; 21: 1432–9
   PubMedGoogle Scholar
• Hilgenfeld R, Liesum A, Storm R. Crystallization of blood coagulation factor XIII by an automated procedure. FEBS Lett 1990; 265: 110–2
   PubMedGoogle Scholar
• Bishop P D, Lasser G W, LeTrong I. Human recombinant factor XIII from Saccharomyces cerevisiae. Crystallization and preliminary X-ray data. J Biol Chem 1990; 265: 13888–9
   PubMedGoogle Scholar
• Yee V C, Pedersen L, LeTrong I. Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc Natl Acad Sci USA 1994; 91: 7296–300
   PubMed Web of Science ®Google Scholar
• Pedersen L C, Yee V C, Bishop P D. Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Protein Sci 1994; 3: 1131–5
   PubMedGoogle Scholar
• Yorifuji H, Anderson K, Lynch G W. B protein of factor XIII: differentiation between free B and complexed B. Blood 1988; 72: 1645–50
   PubMed Web of Science ®Google Scholar
• Henriksson P, Hedner U, Nilsson I M. Fibrin-stabilizing factor (Factor XIII) in the fetus and the newborn infant. Pediatr Res 1974; 8: 789–91
   PubMedGoogle Scholar
• Radek J T, Jeong J M, Wilson J. Association of A subunits of recombinant placental factor XIII with the native carrier B subunits from human plasma. Biochemistry 1993; 32: 3527–34
   PubMedGoogle Scholar
• Barbui K, Rodeghiero F, Dini E. Subunit A and S inheritance in four families with congenital Factor XIII deficiency. Br J Haematol 1978; 38: 267–71
   PubMedGoogle Scholar
• Skrzynia C, Reisner H, McDonagh J. Characterization of the catalytic subunit of factor XIII by radioimmunoassay. Blood 1982; 60: 1089–95
   PubMedGoogle Scholar
• Krøll J. The subunit composition of factor XIII proteins in normal and factor XIII deficient plasma and serum analyzed by line immunoelectrophoresis. Clin Chim Acta 1989; 179: 279–84
   PubMedGoogle Scholar
• Rodeghiero F, Morbin M, Barbui T. Subunit A of factor XIII regulates subunit B plasma concentration. Thromb Haemost 1981; 46: 621–2
   PubMed Web of Science ®Google Scholar
• Miloszewski K JM, Losowsky M S. The half life of factor XII in vivo. Br J Haematol 1978; 38: 267–71
   PubMedGoogle Scholar
• Fear J D, Miloszewski K JA, Losowsky M S. The half-life of Factor XIII in the management of inherited deficiency. Thromb Haemost 1983; 49: 102–5
   PubMedGoogle Scholar
• Rodeghiero F, Tosetto A, DiBona E. Clinical pharmacokinetics of placenta-derived factor XIII concentrate in type I and type II factor XIII deficiency. Am J Hematol 1991; 36: 30–4
   PubMedGoogle Scholar
• Saito M, Asakura H, Yoshida T. A familial factor XIII subunit B deficiency. Br J Haematol 1990; 74: 290–4
   PubMed Web of Science ®Google Scholar
• Greenberg C S, Shuman M A. The zymogen form of blood coagulation factor XIII binds specifically to fibrinogen. J Biol Chem 1982; 257: 6096–101
   PubMedGoogle Scholar
• Greenberg C S, Dobson J V, Miraglia C C. Regulation of plasma factor XIII binding to fibri. in vitro. Blood 1985; 66: 1028–34
   PubMed Web of Science ®Google Scholar
• Credo R B, Curtis C G, Lóránd L. α-Chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspect. Biochemistry 1981; 20: 3770–8
   PubMedGoogle Scholar
• Lóránd L, Jeong J M, Radek J T. Human plasma factor XIII: subunit interactions and activation of zymogen. Methods Enzymol 1993; 222: 22–35
   PubMedGoogle Scholar
• Mary A, Achyuthan K E, Greenberg C S. Factor XIII binds to the Aα- and Bβ-chains in the domain of fibrinogen: an immunoblotting study. Biochem Biophys Res Commun 1987; 147: 608–14
   PubMedGoogle Scholar
• Hornyak T J, Shafer J A. Interactions of factor XIII with fibrin as substrate and cofactor. Biochemistry 1992; 31: 423–9
   PubMedGoogle Scholar
• Naski M C, Lóránd L, Shafer J A. Characterization of the kinetic pathway for fibrin promotion of α-thrombin catalyzed activation of plasma factor XIII. Biochemistry 1991; 30: 934–41
   PubMedGoogle Scholar
• Greenberg C S, Enghild J J, Mary A. Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochem J 1988; 256: 1013–9
   PubMedGoogle Scholar
• Buluk K. An unknown function of blood platelets. Pol Tyg Lek 1955; 10: 191
   Google Scholar
• Lüscher E F. Ein fibrinstabilisierender Faktor aus Thrombozyten. Schweiz Med Wochenschr 1957; 87: 1220–1
   PubMedGoogle Scholar
• Bohn H. Isolierung und Characterisierung des fibrinstabilisierenden Faktors aus menschlichen Thrombozyten. Thromb Diath Haemorrh 1970; 23: 455–68
   PubMedGoogle Scholar
• Puszkin E G, Raghuraman V. Catalytic properties of a calmodulin-regulated transglutaminase from human platelets and chicken gizzard. J Biol Chem 1985; 260: 16012–20
   PubMed Web of Science ®Google Scholar
• Muszbek L, Ádány R, Kávai M. Monocytes of patients congenially deficient in plasma factor XIII lack factor XIII subunit A antigen and transglutaminase activity. Thromb Haemost 1988; 59: 231–5
   PubMedGoogle Scholar
• Boda Z, Pfliegler G, Muszbek L. Congenital factor XIII deficiency with multiple benign breast tumors and successful pregnancy with substitutive therapy. Haemostasis 1989; 19: 348–52
   PubMedGoogle Scholar
• Kiesselbach T H, Wagner R H. Demonstration of factor XIII in human megakaryocytes by a fluorescent antibody technique. Ann NY Acad Sci 1972; 202: 318–28
   PubMedGoogle Scholar
• Ádány R, Kiss A Muszbek L. Factor XIII: a marker of mono-, and megakaryocytopoesis. Br J Haematol 1987; 67: 167–72
   PubMedGoogle Scholar
• Mc Donagh J, McDonagh R P, Delage J M. Factor XIII in human plasma and platelets. J Clin Invest 1969; 48: 940–6
   PubMedGoogle Scholar
• Marx G, Korner G, Mou X. Packaging zinc, fibrinogen and factor XIII in platelet α-granules. J Cell Physiol 1993; 156: 437–42
   PubMed Web of Science ®Google Scholar
• Lopaciuk S, Lovette K M, McDonagh J. Subcellular distribution of fibrinogen and factor XIII in human blood platelets. Thromb Res 1974; 8: 453–65
   Google Scholar
• Broekman M J, Handin R J, Cohen P. Distribution of fibrinogen and platelet factor 4 and XIII in subcellular fractions of human platelets. Br J Haematol 1975; 31: 51–5
   PubMedGoogle Scholar
• Takagi J, Kasahara K, Sekiya F. Subunit B of factor XIII is present in bovine platelets. Thromb Res 1988; 50: 767–74
   PubMedGoogle Scholar
• Muszbek L, Ádány R, Szegedi G. Factor XIII of blood coagulation in human monocytes. Thromb Res 1985; 37: 401–10
   PubMed Web of Science ®Google Scholar
• Ádány R, Belkin A, Vasilevskaya T. Identification of blood coagulation factor XIII in human peritoneal macrophages. Eur J Cell Biol 1985; 38: 171–3
   PubMedGoogle Scholar
• Henriksson P, Becker S, Lynch G. Identification of intracellular factor XIII in human monocytes and macrophages. J Clin Invest 1985; 76: 528–34
   PubMedGoogle Scholar
• Ádány R, Kappelmayer J, Muszbek L. Expression of factor XIII subunit A in different types of human macrophages. Adv Biosci 1987; 66: 323–33
   Google Scholar
• Kradin R L, Lynch G W, Kurnick J T. Factor XIII A is synthesized and expressed on the surface of U937 cells and alveolar macrophages. Blood 1987; 69: 778–85
   PubMedGoogle Scholar
• Ádány R, Nemes Z Muszbek L. Characterization of factor XIII containing macrophages in lymph nodes with Hodgkin's disease. Br J Cancer 1987; 55: 421–6
   PubMedGoogle Scholar
• Ádány R, Nemes Z, Thomázy V. Identification of factor XIII in macrophages invading lymph nodes with Hodgkin's disease. Haemostasis and cancer, L Muszbek. CRC Press, Boca Raton, FL 1987; 125–34
   Google Scholar
• Tumock K, Bulmer J N, Gray C. Phenotypic characterization of macrophage subpopulations and localization of factor XIII in the stromal cells of carcinomas. Histochem J 1990; 22: 661–6
   PubMedGoogle Scholar
• Nemes Z, Thomázy V, Ádány R. Identification of histiocytic reticulum cells by the immunohistochemical demonstration of factor XIII (F-XIIIa) in human lymph nodes. J Pathol 1986; 149: 121–32
   PubMedGoogle Scholar
• Nemes Z, Ádány R, Thomázy V. Selective visualization of human dendritic reticulum cells in reactive lymphoid follicles by immunohistochemical demonstration of the subunit A of factor XIII (F-XIIIa). Virchows Arch (Cell Pathol) 1987; 52: 453–66
   Google Scholar
• Ádány R, Muszbek L. Cells containing factor XIII subunit a in benign and soft tissue tumors. Histopathology 1987; 11: 1341–2
   PubMedGoogle Scholar
• Ádány R, Glukhova M, Kabakov A Y. Characterization of connective tissue cells containing factor XIII subunia. J Clin Pathol 1988; 41: 49–56
   PubMedGoogle Scholar
• Estrada J A, Piérard G E. Factor XIIIa-positive dendrocytes and the dermal vascular unit. Dermatologica 1990; 180: 51–3
   PubMedGoogle Scholar
• Morganroth G S, Chan L S, Weinstein G D. Proliferating cells in psoriatic dermis are comprised primarily of T cells, endothelial cells and FXIIIa+ perivascular dendritic cells. J Invest Dermatol 1991; 96: 333–40
   PubMed Web of Science ®Google Scholar
• Nemes Z. Differentiation markers in hemangiopericytoma. Cancer 1992; 69: 133–40
   PubMed Web of Science ®Google Scholar
• Cerio R, Spaull J, Wilson J E. Identification of factor XIIIa in cutaneous tissue. Histopathology 1988; 13: 362–3
   PubMedGoogle Scholar
• Ádány R. Identification of factor XIIIa in cutaneous tissue. Reply. Histopathology 1988; 13: 363–4
   Google Scholar
• Cerio R, Griffiths C E, Cooper K D. Characterisation of factor XIIIa positive dermal dendritic cells in normal and inflamed skin. Brit J Dermatol 1989; 121: 421–31
   PubMed Web of Science ®Google Scholar
• Weisberg L J, Shiu D T, Conkling P R. Identification of normal human peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII a-chain. Blood 1987; 70: 579–82
   PubMed Web of Science ®Google Scholar
• Ádány R, Polgár E Antal M. Three different cell types can synthesize factor XIII subunit A in human liver. Fourth International Conference on Transglutaminases and Protein Cross-linking Reactions. Abstract Book. 1994
   Google Scholar
• Berntorp E, Seiving B Stenberg P. Characterization of transglutaminase in normal and malignant human leucocytes. Scand J Haematol 1985; 34: 71–7
   PubMedGoogle Scholar
• Sieving B, Ohlsson K, Linder C. Transglutaminase differentiation during maturation of human blood monocytes to macrophages. Eur J Haematol 1991; 46: 263–71
   PubMedGoogle Scholar
• Conkling P R, Achyuthan K E, Greenberg C S. Human mononuclear phagocyte transglutaminase activity cross-links fibrin. Thromb Res 1989; 55: 57–68
   PubMedGoogle Scholar
• Muszbek L, Polgár J, Boda Z. Platelet factor XIII becomes active without the release of activation peptide during platelet activation. Thromb Haemost 1993; 69: 282–5
   PubMedGoogle Scholar
• Muszbek L, Haramura G, Polgár J. Transformation of cellular factor XIII into an active zymogen transglutaminase in thrombin-stimulated platelets. Thromb Haemost 1995; 74: 702–5
   Google Scholar
• Mehta K, Lopez Berenstein G, Moore W T. Interferon-gamma requires serum retinoids to promote the expression of tissue transglutaminase in cultured human blood monocytes. J Immunol 1985; 134: 2053–6
   PubMedGoogle Scholar
• Chung S I. Comparative studies on tissue transglutaminase and factor XIII. Ann NY Acad Sci 1972; 202: 240–55
   PubMedGoogle Scholar
• Kappelmayer J, Bacskó G, Kelemen E. Onset and distribution of FXIII-containing cells in the mesenchyme of chorionic villi during early phase of human placentation. Placenta 1994; 15: 613–23
   PubMedGoogle Scholar
• Ádány R, Muszbek L. Immunohistochemical detection of factor XIII subunit a in hystiocytes of human uterus. Histochemistry 1989; 91: 169–74
   PubMedGoogle Scholar
• Fear J D, Jackson P, Gray C. Localization of factor XIII in human tissues using an immunoperoxidase technique. J Clin Pathol 1984; 37: 560–3
   PubMedGoogle Scholar
• Reid M B, Gray C, Fear J D. Immunohistochemical demonstration of factors FXIIIa and XIIIs in reactive and neoplastic fibroblastic and fibrohistiocytic lesions. Histopathology 1986; 10: 1171–8
   PubMed Web of Science ®Google Scholar
• Nemeth A J, Penneys N S. Factor XIIIa is expressed by fibroblasts in fibrovascular tumors. J Cutan Pathol 1989; 16: 266–71
   PubMed Web of Science ®Google Scholar
• Nemes Z, Thomázy V. Diagnostic significance of histiocyte-related markers in malignant histiocytosis and true histiocytic lymphoma. Cancer 1988; 62: 1970–80
   PubMed Web of Science ®Google Scholar
• Nemes Z, Thomázy V. Factor XIIIa and the classic histiocytic markers in malignant fibrous histiocytoma: a comparative immunohistochemical study. Hum Pathol 1988; 19: 822–9
   PubMed Web of Science ®Google Scholar
• Cerio R, Spaull J, Jones E W. Histiocytoma cutis, a tumour of dermal dendrocytes (dermal dendrocytoma). Br J Dermatol 1989; 120: 197–206
   PubMedGoogle Scholar
• Delabie J, De Wolf-Peeters C, Morren M. Histiocytes in Sweet's syndrome. Br J Dermatol 1991; 124: 348–53
   PubMed Web of Science ®Google Scholar
• Nemeth A J, Penneys N S, Bernstein H B. Fibrous papule: a tumor of fibrohistiocytic cells that contain factor XIIIa. J Am Acad Dermatol 1988; 19: 1102–6
   PubMedGoogle Scholar
• Nickoloff B J, Griffiths C EM. Factor XIIIa-expressing dermal dendrocytes in AIDS-associated cutaneous Kaposi's sarcomas. Science 1989; 243: 1736–7
   PubMedGoogle Scholar
• Walls W D, Losowsky M S. Plasma fibrin stabilizing factor (FSF) activity in normal subjects and patients with chronic liver disease. Thromb Diath Haemorrh 1969; 21: 134–43
   PubMedGoogle Scholar
• Biland L, Duckert F, Prisender S. Quantitative estimation of coagulation factors in liver disease. The diagnostic and prognostic value of factor XIII, factor V and plasminogen. Thromb Haemost 1979; 39: 646–56
   Google Scholar
• Gybryelewicz A, Bielawiec M. Fibrin stabilization, factor XIII transamidase activity and subunits “a” and “b” concentration in plasma of patients with liver cirrhosis. Folia Haematol 1986; 113: 539–44
   Google Scholar
• Yoshioka K, Miyata H, Uraoka Y. Plasma factor XIII levels in children with renal disease. Nephron 1981; 27: 19–24
   PubMedGoogle Scholar
• Cucuianu M P, Miloszewski K, Porutiu D. Plasma factor XIII and platelet factor XIII in hyperlipaemia. Thromb Haemost 1976; 36: 542–50
   PubMedGoogle Scholar
• Ikematsu S. An approach to the metabolism of factor XIII. Acta Haematol Jpn 1981; 44: 1499–505
   PubMedGoogle Scholar
• Miloszewski K JA, Losowsky M S. Clinical consequences of inherited and acquired factor XIII deficiency. Factor XIII and fibronectin — new clinical and biological approaches, R Egbring, H D Klingemann. Medizinische Verlagsgesellschaft mbH, Marburg Lahn 1983; 31–9
   Google Scholar
• Trimble C L, Gray M H, McNutt N S. The distribution of factor XIIIa-positive cells in the human fetus and placenta. Virchows Arch A 1992; 420: 513–8
   Web of Science ®Google Scholar
• Derrick E K, Barker J N, Khan A. The tissue distribution of factor XIIIa positive cells. Histopathology 1993; 22: 157–62
   PubMed Web of Science ®Google Scholar
• Nagy J A, Henriksson P, Mc Donagh J. Biosynthesis of factor XIII B subunit by human hepatoma cell lines. Blood 1986; 68: 1272–9
   PubMedGoogle Scholar
• Wölpl A, Lattke H, Board P G. Coagulation factor XIII A and B subunits in bone marrow and liver transplantation. Transplantation 1987; 43: 151–3
   PubMedGoogle Scholar
• Poon M C, Russel JA, Low S. Hemopoietic origin of factor XIII subunits in platelets, monocytes and plasma. Evidence from bone marrow transplantation studies. J Clin Invest 1989; 84: 787–92
   PubMed Web of Science ®Google Scholar
• Janus T J, Lewis S D, Lóránd L. A promotion of thrombin-catalyzed activation of factor XIII by fibrinogen. Biochemistry 1983; 22: 6269–72
   PubMedGoogle Scholar
• Lewis S D, Janus T J, Lóránd L. Regulation of formation of factor XIIIa by its fibrin substrates. Biochemistry 1985; 24: 6772–7
   PubMedGoogle Scholar
• Greenberg C S, Miraglia C C. The effect of fibrin polymers on thrombin catalyzed plasma factor XIII formation. Blood 1985; 66: 466–9
   PubMedGoogle Scholar
• Greenberg C S, Miraglia C C, Rickles F R. Cleavage of blood coagulation factor XIII and fibrinogen by thrombin during in vitro clotting. Arch Biochem Biophys 1988; 262: 142–8
   PubMedGoogle Scholar
• Greenberg C S, Achyuthan K E, Rajagopalan S. Characterization of the fibrin polymer structure that accelerates thrombin cleavage of plasma factor XIII. J Clin Invest 1985; 75: 1463–70
   PubMedGoogle Scholar
• Chung S I, Lewis M S, Folk J E. Relationship of the catalytic properties of human plasma and platelet transglutaminases (activated blood coagulation factor XIII) to their subunit structure. J Biol Chem 1974; 249: 940–50
   PubMed Web of Science ®Google Scholar
• Greenberg C S, Achyuthan K E, Fenton J W. Factor XIIIa formation promoted by complexing of α-thrombin, fibrin and plasma factor XIII. Blood 1987; 69: 867–71
   PubMed Web of Science ®Google Scholar
• Hornyak T J, Bishop P D, Shafer J A. α-Thrombin-catalyzed activation of human platelet factor XIII: relationship between proteolysis and factor XIIIa activity. Biochemistry 1989; 28: 7326–32
   PubMedGoogle Scholar
• Homyak T J, Shafer J A. Role of calcium ion in the generation of factor XIII activity. Biochemistry 1991; 30: 6175–82
   PubMedGoogle Scholar
• Polgár J, Lénárt I, Muszbek L. Thrombomodulin inhibits the activation of factor XIII by thrombin. Thromb Res 1986; 43: 585–90
   Google Scholar
• Mary A, Achyuthan K E, Greenberg C S. b-Chains prevent the proteolytic inactivation of the a-chains of plasma factor XIII. Biochim Biophys Acta 1988; 966: 328–35
   PubMedGoogle Scholar
• Curtis C G, Brown K L, Credo R B. Calcium-dependent unmasking of active center cystein during activation of fibrin stabilizing factor. Biochemistry 1974; 13: 3774–80
   PubMed Web of Science ®Google Scholar
• Achyuthan K E, Mary A, Greenberg C S. Tb(III)-ion-binding-induced conformational changes in platelet factor XIII. Biochem J 1989; 257: 331–8
   PubMedGoogle Scholar
• De Backer-Royer C, Traoré F, Meunier J C. Purification and properties of factor XIII from human placenta. Int J Biochem 1992; 24: 91–7
   PubMedGoogle Scholar
• Credo R B, Curtis C G, Lóránd L. Ca2+-related regulatory function of fibrinogen. Proc Natl Acad Sci USA 1978; 75: 675–82
   Google Scholar
• Cook R D. Calcium-induced dissociation of human plasma factor XIII and the appearance of catalytic activity. Biochem J 1974; 141: 683–91
   PubMedGoogle Scholar
• Seelig G F, Folk J E. Half-of-the-sites and all-of-the-sites reactivity in human plasma blood coagulation factor XIIIa. J Biol Chem 1980; 255: 9589–93
   PubMedGoogle Scholar
• Barry E LR, Mosher F D. Binding and degradation of blood coagulation factor XIII by cultured fibroblasts. J Biol Chem 1990; 265: 9302–7
   PubMed Web of Science ®Google Scholar
• Greenberg C S, Shuman M A. Specific binding of blood coagulation factor XIIIa to thrombin-stimulated platelets. J Biol Chem 1984; 259: 14721–27
   PubMedGoogle Scholar
• Cox A D, Devine D V. Factor XIIIa binding to activated platelets is mediated through activation of glycoprotein IIb-IIIa. Blood, 83: 1006–16
   PubMedGoogle Scholar
• Lóránd L, Credo R B, Janus T J. Factor XIII (fibrin stabilizing factor). Methods Enzymol 1981; 80: 333–41
   PubMedGoogle Scholar
• Polgár J, Hidasi V, Muszbek L. Non-proteolytic activation of cellular protransglutaminase (placenta macrophage factor XIII). Biochem J 1990; 267: 557–60
   PubMedGoogle Scholar
• Cohen I, Glaser T, Veis A. Ca2+ dependent cross-linking process in human platelets. Biochim Biophys Acta 1981; 676: 137–47
   PubMedGoogle Scholar
• Cohen I, Lim C T, Kahn D R. Disulfide-linked and transglutaminase-catalyzed protein assemblies in platelets. Blood 1985; 66: 143–51
   PubMedGoogle Scholar
• Hársfalvi J, Fésüs L, Tarcsa E. The presence of a covalent cross-linked matrix in human platelets. Biochim Biophys Acta 1991; 1073: 268–74
   PubMedGoogle Scholar
• Ando Y, Imamura S, Yamagata Y. Platelet factor XIII is activated by calpain. Biochem Biophys Res Commun 1987; 144: 484–90
   PubMedGoogle Scholar
• Lynch G W, Pfueller S L. Thrombin-independent activation of platelet factor XIII by endogenous platelet acid protease. Thromb Haemost 1988; 59: 372–7
   PubMedGoogle Scholar
• Lóránd L, Conrad S M. Transglutaminases. Mol Cell Biochem 1984; 58: 9–35
   PubMed Web of Science ®Google Scholar
• Parameswaran K N, Lóránd L. New thioester substrates for fibrinoligase (coagulation factor XIIIa) and for transglutaminases. Transfer of fluorescently labeled acyl group to amines and alcohols. Biochemistry 1981; 20: 3703–11
   PubMedGoogle Scholar
• Micanovic R, Procyk R, Lin W. Role of histidine 373 in the catalytic activity of coagulation factor XIII. J Biol Chem 1994; 269: 9190–4
   PubMed Web of Science ®Google Scholar
• Gorman J J, Folk J E. Structural features of glutamine substrates for transglutaminases: specificities of human plasma factor XIIIa and the guinea pig liver enzyme. J Biol Chem 1981; 256: 2712–5
   PubMedGoogle Scholar
• Gorman J J, Folk J E. Structural features of glutamine substrates for transglutaminases: role of extended interactions in the specificity of human plasma factor XIIIa and the guinea pig liver enzyme. J Biol Chem 1984; 259: 9007–10
   PubMedGoogle Scholar
• Parameswaran K N, Velasco P T, Wilson J. Labeling of ε-lysine cross-linking sites in proteins with peptide substrates of factor XIIIa and transglutaminase. Proc Natl Acad Sci USA 1990; 87: 8472–5
   PubMedGoogle Scholar
• Shafer J A, Higgins D L. Human fibrinogen. CRC Crit Rev Clin Lab Sci 1988; 26: 1–41
   Google Scholar
• Mosesson M W. The assembly and structure of the fibrin clot. Nouv Rev Fr Hematol 1992; 34: 11–6
   PubMedGoogle Scholar
• Mosesson M W, Siebenblist K R, Amrani D L. Proc Natl Acad Sci USA 1989; 86: 1113–7
   PubMedGoogle Scholar
• Shainoff J R, Urbanic D A, DiBello P M. Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. J Biol Chem 1991; 266: 6429–37
   PubMedGoogle Scholar
• Grøn B, Filion Myklebust C, Bennick A. Early cross-linked fibrin in human plasma contains α-polymers with intact fibrinopeptide A. Blood Coag Fibrinol 1992; 3: 731–6
   PubMedGoogle Scholar
• Lóránd L, Ong H H. Labeling of amine-acceptor cross-linking sites of fibrin by transpeptidation. Biochemistry 1966; 5: 1747–53
   PubMedGoogle Scholar
• Lóránd L. Physiological cross-linking of fibrin. Thromb Diath Haemorrh Suppl 1970; 39: 75–102
   Google Scholar
• Kanaide D, Shainoff J R. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa). J Lab Clin Med 1975; 85: 574–97
   PubMedGoogle Scholar
• Fowler W E, Erickson H P, Hantgan R R. Cross-linked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers. Science 1981; 211: 287–9
   PubMed Web of Science ®Google Scholar
• Blombäck B, Procyk R, Adamson L. FXIII induced gelation of human fibrinogen — an alternative thiol enhanced, thrombin independent pathway. Thromb Res 1985; 37: 613–28
   PubMedGoogle Scholar
• Dardik B N, Shainoff J R. Cross-linking of monomeric fibrin by factor XIIIa. Thromb Haemost 1979; 42: 864–72
   PubMedGoogle Scholar
• Dyr J E, Blombäck B, Hessel B. Conversion of fibrinogen to fibrin by preferential release of fibrinopeptide B. Biochim Biophys Acta 1989; 990: 18–24
   PubMedGoogle Scholar
• Francis R T, McDonagh J, Mann K G. Factor V is a substrate for the transamidase factor XIIIa. J Biol Chem 1986; 261: 9787–92
   PubMedGoogle Scholar
• Huh M M, Schick B, Schick P K. Blood 1986; 66: 336a
   Google Scholar
• Huh M M, Schick B, Schick P K. Covalent cross-linking of human coagulation factor V by activated factor XIII from guinea pig megakaryocytes and human plasma. Blood 1988; 71: 1693–702
   PubMedGoogle Scholar
• Aoki N, Harpel P L. Inhibitors of the fibrinolytic enzyme system. Sem Thromb Haemost 1984; 10: 24–41
   PubMedGoogle Scholar
• Sakata Y, Aoki N. Cross-linking of α2-plasmin inhibitor to fibrin by fibrin-stabilizing factor. J Clin Invest 1980; 65: 290–7
   PubMed Web of Science ®Google Scholar
• Tamaki T, Aoki N. Cross-linking of α2-plasmin inhibitor and fibronectin to fibrin by fibrin-stabilizing factor. Biochim Blophys Acta 1981; 661: 280–6
   PubMed Web of Science ®Google Scholar
• Ichinose A, Aoki N. Reversible cross-linking of α2-plasmin inhibitor to fibrinogen by fibrin-stabilizing factor. Biochim Biophys Acta 1982; 706: 158–64
   PubMedGoogle Scholar
• Mimuro J, Kimura S, Aoki N. Release of α2-plasmin inhibitor from plasma fibrin clots by activated coagulation factor XIII. J Clin Invest 1986; 77: 1006–13
   PubMedGoogle Scholar
• Tamaki T, Aoki N. Cross-linking of α2-plasmin inhibitor to fibrin by fibrin-stabilizing factor. J Biol Chem 1982; 257: 14767–72
   PubMed Web of Science ®Google Scholar
• Kimura S, Aoki N. Cross-linking site in fibrinogen for α2-plasmin inhibitor. J Biol Chem 1986; 261: 15591–5
   PubMedGoogle Scholar
• Jansen P H, Lóránd L, Ebbesen P. Type-2 plasminogen-activator inhibitor is a substrate for trophoblast transglutaminase and factor XIIIa. Eur J Biochem 1993; 214: 141–6
   PubMedGoogle Scholar
• Borth W, Chang V, Bishop P. Lipoprotein (a) is a substrate for FXIIIa and tissue transglutaminase. J Biol Chem 1991; 266: 18149–53
   PubMed Web of Science ®Google Scholar
• Mosher D F. Cross-linking of cold-insoluble globulin by fibrin stabilizing factor. J Biol Chem 1975; 250: 6614–21
   PubMed Web of Science ®Google Scholar
• Williams E C, Janmey P A, Johnson R B. Fibronectin. Effect of disulfide bond reaction on its physical and functional properties. J Biol Chem 1983; 258: 6595–601
   PubMedGoogle Scholar
• Okada M, Blombäck B, Chang M D. Fibronectin and fibrin gel structure. J Biol Chem 1985; 260: 1811–20
   PubMed Web of Science ®Google Scholar
• Mosher D F, Johnson R B. Specificity of fibronectin-fibrin cross-linking. Ann NY Acad Sci 1983; 408: 583–94
   PubMed Web of Science ®Google Scholar
• Mc Donagh R P, McDonagh J, Petersen T E. Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectin. FEBS Lett 1981; 127: 174–8
   PubMedGoogle Scholar
• Fésüs L, Mestis M L, Muszbek L. Transglutaminase-sensitive glutamine residues of human plasma fibronectin revealed by studying its proteolytic fragments. Eur J Biochem 1986; 154: 371–4
   PubMedGoogle Scholar
• Procyk R, Adamson L, Block M. Factor XIII catalyzed formation of fibrinogen-fibronectin oligomers — a thiol enhanced process. Thromb Res 1985; 40: 833–52
   PubMed Web of Science ®Google Scholar
• Procyk R, Blombäck B. Factor XIII-induced cross-linking in solutions of fibrinogen and fibronectin. Biochim Biophys Acta 1988; 967: 304–13
   PubMedGoogle Scholar
• Mosher D F, Schad P E, Kleinman H K. Cross-linking of fibronectin to collagen by blood coagulation factor XIIIa. J Clin Invest 1979; 64: 781–7
   PubMed Web of Science ®Google Scholar
• Keski Oja J, Mosher D F, Vaheri A. Cross-linking of major fibroblast surface-associated glycoprotein (fibronectin) catalyzed by blood coagulation factor XIII. Cell 1976; 9: 29–35
   PubMedGoogle Scholar
• Barry E LR, Mosher F D. Factor XIII cross-linking of fibronectin at cellular matrix assembly sites. J Biol Chem 1988; 263: 10464–9
   PubMed Web of Science ®Google Scholar
• Barry E LR, Mosher F D. FXIIIa-mediated cross-linking of fibronectin in fibroblast cell layers. Cross-linking of cellular and plasma fibronectin and of amino-terminal fibronectin fragments. J Biol Chem 1989; 264: 4179–85
   PubMedGoogle Scholar
• Soria A, Soria C, Boulard C. Fibrin stabilizing factor (F XIII) and collagen polymerizatio. Experientia 1975; 31: 1355–7
   PubMedGoogle Scholar
• Sane D C, Moser T L, Pippen A MM. Vitronectin is a substrate for transglutaminases. Biochem Biophys Res Commun 1988; 157: 115–20
   PubMedGoogle Scholar
• Skorstengaard K, Halkier T, Højrup P. Sequence location of a putative transglutaminase cross-linking site in human vitronectin. FEBS Lett 1990; 262: 269–74
   PubMedGoogle Scholar
• Prince C W, Dickie D, Krumdieck C L. Osteopontin, a substrate for transglutaminase and factor XIII activity. Biochem Biophys Res Commun 1991; 177: 1205–10
   PubMed Web of Science ®Google Scholar
• Martin M T, Lefebvre F, Rabaud M. Biochemical study of adduct synthesis between fibrin monomers and elastin. Biomaterials 1988; 9: 519–24
   PubMed Web of Science ®Google Scholar
• Hada M, Kato M, Ikematsu S. Possible cross-linking of factor VIII related antigen to fibrin by factor XIII in delayed coagulation process. Thromb Res 1982; 25: 163–8
   PubMedGoogle Scholar
• Hada M, Kaminski M, Bockenstedt P. Covalent cross-linking of von Willebrand factor to fibrin. Blood 1986; 68: 95–101
   PubMed Web of Science ®Google Scholar
• Bockenstedt P, McDonagh J, Handin R I. Binding and covalent cross-linking of purified von Willebrand factor to native monomeric collagen. J Clin Invest 1986; 78: 551–6
   PubMedGoogle Scholar
• Bale M D, Westrick L G, Mosher D F. Incorporation of thrombospondin into fibrin clots. J Biol Chem 1985; 260: 7502–8
   PubMed Web of Science ®Google Scholar
• Bale M D, Mosher D F. Thrombospondin is a substrate for blood coagulation factor XIIIa. Biochemistry 1986; 25: 5667–73
   PubMedGoogle Scholar
• Lynch G W, Slayter H S, Miller B E. Characterization of thrombospondin as a substrate for factor XIII transglutaminase. J Biol Chem 1987; 262: 1772–8
   PubMedGoogle Scholar
• Cohen I, Young Bandala L, Blankenberg T A. Fibrinoligase-catalyzed cross-linking of myosin from platelet and skeletal muscle. Arch Biochem Biophys 1979; 192: 100–11
   PubMed Web of Science ®Google Scholar
• Cohen I, Blankenberg T A, Borden D. Factor XIIIa-catalyzed cross-linking of platelet and muscle actin. Regulation by nucleotides. Biochim Biophys Acta 1980; 628: 365–75
   PubMedGoogle Scholar
• Horváth A R, Asijee G M, Muszbek L. Cytoskeletal assembly and vinculin-cytoskeleton interaction in different phases of the activation of bovine platelets. Cell Motil Cytoskel 1992; 21: 123–31
   PubMedGoogle Scholar
• Asijee G M, Muszbek L, Kappelmayer J. Platelet vinculin: a substrate of activated factor XIII. Biochim Biophys Acta 1988; 954: 303–8
   PubMedGoogle Scholar
• Mellanby J, Pratt C LG. Calcium and blood coagulation. Proc. Roy. Soc. B. 1939; 128: 201–13
   Google Scholar
• Hartert H. Rheo-stimulation: a new method for the assay of clotting process and factor XIII. A preliminary report. Biorheology 1974; 11: 355–60
   PubMedGoogle Scholar
• Shen L L, Hermans J, McDonagh J. Effects of calcium ions and covalent cross-linking on formation and elasticity of fibrin gels. Thromb Res 1975; 6: 255–65
   PubMedGoogle Scholar
• Gelman R A, Gladner J A, Nossal R. Rigidity of fibrin gels as measured by quasielastic light scattering. Biopolymers 1980; 19: 1259–70
   PubMedGoogle Scholar
• Shen L L, Lóránd L. Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-deficient plasma with purified zymogen. J Clin Invest 1983; 71: 1336–41
   PubMedGoogle Scholar
• Gladner J A, Nossel R. Effects of cross-linking on the rigidity and proteolytic susceptibility of human fibrin clots. Thromb Res 1983; 30: 273–88
   PubMedGoogle Scholar
• Kamykowski G W, Mosher D F, Lóránd L. Modification of shear modulus and creep compliance of fibrin clots by fibronectin. Biophys Chem 1981; 13: 25–8
   PubMedGoogle Scholar
• Chou T W, McIntire L W, Petersen D M. Importance of plasma fibronectin in determining PFP and PRP clot mechanical properties. Thromb Res 1983; 29: 243–8
   PubMedGoogle Scholar
• Carr M E, Gabriel D A, McDonagh J. Influence of factor XIII and fibronectin on fiber size and density in thrombin-induced fibrin gels. J Lab Clin Med 1987; 110: 747–52
   PubMedGoogle Scholar
• Lóránd L, Jacobsen A. Accelerated lysis of blood clots. Nature (London) 1962; 195: 911–2
   PubMedGoogle Scholar
• Gormsen J, Fletcher A P, Alkjaersig N. Enzymatic lysis of plasma clots: the influence of fibrin stabilization on lysis rates. Arch Biochem Biophys 1967; 120: 654–65
   Google Scholar
• Henderson K W, Nussbaum M. The mechanism of enhanced streptokinase induced clot lysis following in vitro factor XIII inactivations. Br J Haematol 1969; 17: 445–53
   PubMedGoogle Scholar
• Mc Donagh R P, McDonagh J, Duckert F. The influence of fibrin cross-linking on the kinetics of urokinase-induced clot lysis. Br J Haematol 1971; 21: 323–32
   PubMedGoogle Scholar
• Schwartz M L, Pizzo S V, Hill R I. The effect of fibrin-stabilizing factor on the subunit structure of human fibrin. J Clin Invest 1971; 50: 1506–13
   PubMedGoogle Scholar
• Gaffney P J, Whitaker A N. Fibrin cross-links and lysis rates. Thromb Res 1979; 14: 85–94
   PubMedGoogle Scholar
• Jansen J W.C.M, Haverkate F, Koopman J. Influence of factor XIIIa activity on human whole blood clot lysi. in vitro. Thromb Haemost 1987; 57: 171–5
   PubMedGoogle Scholar
• Leidy E M, Stem A M, Friedman P A. Enhanced thrombolysis by a factor XIIIa inhibitor in a rabbit model of femoral artery thrombosis. Thromb Res 1990; 59: 15–26
   PubMedGoogle Scholar
• Shebuski R J, Sitko G R, Claremon D A. Inhibition of factor XIIIa in a canine model of coronary thrombosis: effect on reperfusion and acute reocclusion after recombinant tissue-type plasminogen activator. Blood 1990; 75: 1455–9
   PubMedGoogle Scholar
• Haverkate F. Lysis of cross-linked and non-cross-linked purified fibrin. Thromb Diath Haemorrh 1975; 34: 584–5
   PubMedGoogle Scholar
• Sakata Y, Aoki N. Significance of cross-linking of α2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest 1982; 69: 536–42
   PubMedGoogle Scholar
• Kimura S, Tamaki T, Aoki N. Acceleration of fibrinolysis by the amino-terminal peptide of α2-plasmin inhibitor. Blood 1985; 66: 157–60
   PubMed Web of Science ®Google Scholar
• van Giezen J JJ, Minkema J, Bouma B N. Cross-linking of α2-antiplasmin to fibrin is a key factor in regulating blood clot lysis: species differences. Blood Coag Fibrinolysis 1993; 4: 869–75
   PubMed Web of Science ®Google Scholar
• Francis C W, Marder V J. Increased resistance to plasmic degradation of fibrin with highly cross-linked α-polymer chains formed at high factor XIII concentrations. Blood 1988; 71: 1361–5
   PubMedGoogle Scholar
• Francis C W, Marder V J. Rapid formation of large molecular weight α-polymers in cross-linked fibrin induced by high factor XIII concentrations. Role of platelet factor XIII. J Clin Invest 1987; 80: 1459–65
   PubMedGoogle Scholar
• Sakata Y, Mimuro J, Aoki N. Differential binding of plasminogen to cross-linked and non-cross-linked fibrin: its significance in hemostatic defect in factor XIII deficiency. Blood 1984; 63: 1393–401
   PubMedGoogle Scholar
• Reed G L, Matsueda G R, Haber E. Platelet factor XIII increases the fibrinolytic resistance of platelet-rich clots by accelerating the cross-linking of α2-antiplasmin to fibrin. Thromb Haemost 1992; 68: 315–20
   PubMedGoogle Scholar
• Aoki N. Clot retraction increases clot resistance to fibrinolysis by condensing α2-plasmin inhibitor cross-linked to fibrin. Thromb Haemost 1993; 70: 376
   PubMedGoogle Scholar
• Hevessy Z, Haramura G, Boda Z. Promotion of crosslinking of fibrin and α2-antiplasmin by platelets. Thromb Haemost 1995, accepted.
   Google Scholar
• Kreager J A, Devine D V, Greenberg C S. Cytofluorometric identification of plasmin-sensitive factor XIIIa binding to platelets. Thromb Haemost 1988; 60: 88–93
   PubMedGoogle Scholar
• Devine D V, Andestad G, Nugent D. Platelet-associated factor XIII as a marker of platelet activation in patients with peripheral vascular disease. Arterioscler Thromb 1993; 13: 857–62
   PubMedGoogle Scholar
• Ádány R, Kappelmayer J, Berényi E. Factors of the extrinsic pathway of blood coagulation in tumor associated macrophages. Thrombos Haemost 1989; 62: 850–55
   PubMedGoogle Scholar
• Constantini V, Zacharski L R. Fibrin and cancer. Thromb Haemost 1993; 65: 406–14
   Google Scholar
• Dvorak H F, Senger D R, Dvorak A M. Fibrin as a component of the tumor stroma: origins and biological significance. Cancer Metast Rev 1983; 2: 41–73
   PubMed Web of Science ®Google Scholar
• Ádány R, Szegedi A, Ablin R J. Fibrinolysis resistant fibrin deposits in lymph nodes with Hodgkin's disease. Thromb Haemost 1988; 60: 293–7
   PubMedGoogle Scholar
• Muszbek L, Ádány R. Intratumoral fibrin stabilization. Lipid peroxidation and cancer, SK Nigam, DCH McBrien, TF Slater. Springer Verlag, Berlin 1988; 339–49
   Google Scholar
• Dvorak H F, Harvey S, McDonagh J. Quantitation of fibrinogen influx and fibrin deposition and turnover in line 1 and line 10 guinea pig carcinomas. Cancer Res 1984; 44: 3348–54
   PubMed Web of Science ®Google Scholar
• Zacharski L R, Brown F E, Memoli W A. Pathways of coagulation activation in situ in rheumatoid synovial tissue. Clin Immun Immunopathol 1992; 63: 155–62
   PubMedGoogle Scholar
• Chignier E, Baguet J, Dessapt B. Skin healing and fibrin stabilization factor blood levels in rabbit fetus. J Surg Res 1981; 31: 415–32
   PubMedGoogle Scholar
• Marktl W, Rundas B. The effect of factor XIII on wound granulation in the rat. Thromb Diath Haemorrh 1974; 32: 578–81
   PubMedGoogle Scholar
• Knoche H, Schmitt G. Autoradiographische Untersuchungen über den Einfluss des Factors XIII auf die Wundheilung im Tierexperiment. Arzn Forsch 1976; 26: 547–51
   PubMedGoogle Scholar
• Gierhake F W, Volkman W, Becker W. Factor XIII concentration and wound healing. German Med Month 1970; 15: 721–5
   Google Scholar
• Gierhake F W, Papastavrou N, Zimmermann K. The prophylaxis of postoperative disturbances of wound healing with factor XIII substitution (result of a double-blind study). Dtsch Med Wochenschr 1974; 99: 1004–9
   PubMed Web of Science ®Google Scholar
• Mishima Y, Nagao F, Ishibiki K. Faktor XIII in der Behandlung post-operative-theratierefrakturer Wundheilungsstörungen. Chirurg 1984; 55: 803–8
   PubMed Web of Science ®Google Scholar
• Isogai N, Ueda Y, Kurozumi N. Wound healing at the site of microvascular anastomosis: fibrin-stabilizing factor XIII administration and its effects. Microsurgery 1990; 11: 40–6
   PubMedGoogle Scholar
• Claes L, Burri C, Gerngross H. Die Beschlennigung der Frakturheilung durch Faktor XIII. Helv Chir Acta 1984; 51: 209–12
   PubMedGoogle Scholar
• Claes L, Burri C, Gerngross H. et al. Bone healing stimulated by plasma FXIII. Acta Orthop Scand 1985; 56: 57–62
   PubMedGoogle Scholar
• Gerngross H, Claes L. Successful treatment of pseudoarthrosis with human placental factor XIII concentrate. Factor XIII: second international conference, J McDonagh, R Seitz, R Egbring. Schattauer, Stuttgart 1993; 271
   Google Scholar
• Beck E, Duckert F Ernst M. The influence of fibrin stabilizing factor on the growth of fibroblasts in vitro and wound healing. Thromb Diath Haemorrh 1961; 6: 485–91
   PubMedGoogle Scholar
• Ueyama M, Urayama T. The role of factor XIII in fibroblast proliferation. Jpn J Exp Med 1978; 48: 135–42
   PubMedGoogle Scholar
• Bruhn H D, Pohl J. Growth regulation of fibroblasts by thrombin, factor XIII and fibronectin. Klin Wochenscr 1981; 59: 145–6
   PubMedGoogle Scholar
• Bruhn H D, Bemmeier R, Broers H. Regulation der Fibroblasten- und Endothelzellenproliferation durch Thrombin, Factor XIII und Fibronectin. Verhandlungsbericht der 25. Tagung der deutschen Arbeitgemeinschaft für Blutgerinnungsforschung. Schattauer, Stuttgart 1981; 257–65
   Google Scholar
• Bruhn H D. Growth regulation of vessel wall cells and of tumor cells by thrombin, factor XIII and fibronectin. Thromb Haemost 1981; 46: 762
   PubMedGoogle Scholar
• Bruhn H D, Zurborn K H. Influences of clotting factors (thrombin, factor XIII) and of fibronectin on the growth of tumor cells and leukemic cells in vitro. Blut 1983; 46: 85–8
   PubMedGoogle Scholar
• Paye M, Nusgens B V, Lapière C M. Factor XIII of blood coagulation modulates collagen biosynthesis by fibroblast. in vitro. Haemostasis 1989; 19: 274–83
   PubMedGoogle Scholar
• Ádány R, Fodor F, Molnár P. Increased density of histiocytes in uterine leiomyomas. Int J Gynecol Pathol 1990; 9: 137–44
   PubMedGoogle Scholar
• Bergsen M, Weller M, Heimann K. Nachweis von Gerinnungsfaktor XIII im Glaskörper und periretinalen Membranen bei proliferativen Netzhauterkrankungen. Forschr Opthalmol 1990; 87: 279–82
   PubMedGoogle Scholar
• Weller M, Bergsen M, Heinmann K. Blood coagulation factor XIII contributes to the development of traction retinal detachment. Acta Opthalmol 1990; 68: 246–52
   PubMedGoogle Scholar
• Kang Y, Hashimoto N, Kikuchi H. Effects of blood coagulation factor XIII on the development of experimental cerebral aneurysms in rats. J Neurosurg 1990; 73: 242–7
   PubMedGoogle Scholar
• Kasai S, Kunimoto T, Nitta K. Cross-linking of fibrin by activated factor XIII stimulates attachment, morphological changes and proliferation of fibroblasts. Biomed Res 1983; 4: 155–60
   Google Scholar
• Herter T, Anaguostopoulos-Svchleep J, Windman D. The influence of factor XIII on the fibrosing of a nerve anastomosis in the rat. Res Exp Med 1989; 189: 25–32
   PubMedGoogle Scholar
• Toida M, Watanabe F, Tsai C S. Factor XIIIa-containing cells and fibrosis in oral and maxillofacial lesions: an immunohistochemical study. Oral Surg Oral Med Oral Pathol 1989; 68: 293–9
   PubMedGoogle Scholar
• Grinnel F, Feld M, Minter D. Fibroblast adhesion to fibrinogen and fibrin substrates: requirement for cold insoluble globulin (plasma fibronectin). Cell 1980; 19: 517–25
   PubMed Web of Science ®Google Scholar
• Lanir N, Ciano P S, Van de Water L. Macrophage migration in fibrin gel matrices. II. Effects of clotting factor XIII, fibronectin, and glycosaminoglycan content on cell migration. J Immunol 1988; 140: 2340–9
   PubMed Web of Science ®Google Scholar
• Paye M, Lapière C M. The lack of attachment of transformed embryonic lung epithelial cells to collagen I is corrected by fibronectin and factor XIII. J Cell Sci 1986; 86: 95–107
   PubMed Web of Science ®Google Scholar
• Leibovich S J, Ross R. The role of macrophages in wound repair. A study with hydrocortisone and antimacrophage serum. Amer J Pathol 1975; 78: 71–100
   PubMed Web of Science ®Google Scholar
• Glynn L E. Tissue repair and regeneration. Raven Press, New York 1985
   Google Scholar
• Okamoto M, Yamamoto T, Matsubara S. Factor XIII-dependent generation of 5th complement component (C5)-derived monocyte chemotactic factor coinciding with plasma clotting. Biochim Biophys Acta 1992; 1138: 53–61
   PubMedGoogle Scholar
• Tidrick R T, Warner E D. Fibrin fixation of skin transplants. Surgery 1944; 15: 90–5
   Google Scholar
• Fisher S, Rikover M, Naor S. Factor 13 deficiency with severe hemorrhagic diathesis. Blood 1966; 28: 34–9
   PubMedGoogle Scholar
• Rodeghiero F, Castaman G C, DiBona E. Successful pregnancy in women with congenital factor XIII deficiency. Blut 1987; 55: 45–8
   PubMedGoogle Scholar
• Kobayashi T, Terao T, Kojima T. Congenital factor XIII deficiency with treatment of factor XIII concentrate and normal vaginal delivery. Gynecol Obstet Invest 1990; 29: 235–8
   PubMedGoogle Scholar
• Halkiel T, Magnusson S. Contact activation of blood coagulation is inhibited by plasma factor XIII b-chain. Thromb Res 1988; 51: 313–24
   PubMedGoogle Scholar
• Sixma J J, Van den Berg A, Schiphorst M. Immunocytochemical localization of albumin and factor XIII in thin cryo sections of human blood platelets. Thromb Haemost 1984; 51: 388–91
   PubMedGoogle Scholar
• Joist J H, Niewiarowski S. Retention of platelet fibrin stabilizing factor during the platelet release reaction and clot retraction. Thromb Diath Haemorrh 1973; 29: 679–83
   PubMedGoogle Scholar
• Holme P A, Brosstadt F, Solum N O. The difference between platelet and plasma FXIII used to study the mechanism of platelet microvesicle formation. Thromb Haemost 1993; 70: 681–6
   PubMed Web of Science ®Google Scholar
• Kasahara K, Takagi J, Sekiya F. “A” subunit of factor XIII is present on bovine platelet membrane and mediates collagen-induced platelet activation. Thromb Res 1988; 50: 25363
   Google Scholar
• Saito Y, Imada T, Takagi J. Platelet factor XIII. The collagen receptor. J Biol Chem 1986; 261: 1355–58
   PubMedGoogle Scholar
• Aihara M, Sawada Y, Takami H. Factor XIII is not involved in human platelet-collagen interaction. Tohoku J Exp Med 1989; 159: 37–44
   PubMedGoogle Scholar
• Ozsoylu S, Hicsonmez G. Platelet aggregation in congenital factor XIII deficiency. Acta Haematol 1976; 56: 314–7
   PubMedGoogle Scholar
• Rao K MK, Newcomb T F. Clot retraction in a factor XIII free system. Scand J Haematol 1980; 24: 142–48
   PubMedGoogle Scholar
• Zhu Y, Tass L, Lane W. Specific binding of the transglutaminase, platelet factor XIII, to HSP27. J Biol Chem 1994; 269: 22379–84
   PubMed Web of Science ®Google Scholar
• Mendelsohn M E, Zhu Y, O'Neill S. The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor related 27-kDa heat shock protein. Proc Natl Acad Sci USA 1991; 88: 11212–16
   PubMed Web of Science ®Google Scholar
• Zhu Y, O'Neill S, Mendelsohn M E. HSP27, a thrombin-activated phosphoprotein, translocates to the cytoskeleton following human platelet activation. Circulation 1992; 86(Suppl I)739a
   Google Scholar
• Muszbek L, Ádány R, Lopaciuk S. Possible role of factor XIII subunit a in phagocytosis by monocytes. Haematol Rev 1986; 1: 120a
   Google Scholar
• Kávai M, Ádány R, Pásti G. Marker profile, enzyme activity, and function of a human myelomonocytic leukemia cell line. Cell Immunol 1992; 139: 531–40
   PubMedGoogle Scholar
• Yee V C, Pedersen L C, Bishop P D. Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res 1995; 78: 389–97
   PubMed Web of Science ®Google Scholar