Overview: Therapeutic Uses of Cell-Matrix Adhesive Proteins

References to primary literature

• BURRIDGE K, FATH K: Focal contacts: Trans-membrane links between the extracellu-lar matrix and the cytoskeleton. BioEssays (1989) 10(4):104–108.
   PubMed Web of Science ®Google Scholar
• LUNA EJ, Hrrr AL: Cytoskeleton-plasma membrane interactions. Science (1992) 258:955–963.
   PubMed Web of Science ®Google Scholar
• JAKEN S, LEACH K, KLAUCK T: Association of type 3 protein kinase C with focal contacts in rat embryo fibroblasts. J. Cell. Biol. (1989) 109:697–704.
   PubMed Web of Science ®Google Scholar
• HANKS S, CALALB M, HARPER M, PATEL S: Focal adhesion protein-tyrosine kinase phos-phorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. (1992) 89:8487–8491.
   Google Scholar
• cDNA cloning used to identify a non-membrane-spanning focal adhesion kinase (FadK) which is phosphorylated on tyrosine within minutes of exposure of cells to immobi-lized Fn.
   Google Scholar
• KORNBERG L, EARP H, PARSONS J, SCHALLER M, JULIANO R: Cell adhesion or integrin clus-tering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. (1992) 267:23439–23442.
   PubMed Web of Science ®Google Scholar
• KLEuSS C, HESCHELER J, EWEL C, ROSENTHAL W, SCHULTS G, Wrrno B: Assignment of G-protein subtypes to specific receptors induc-ing inhibition of calcium currents. Nature (1991) 353:43–48.
   PubMed Web of Science ®Google Scholar
• SCHWARTZ M, INGBER D, LAWRENCE M, SPRINGER T, LECHENE C: Multiple integrins share the ability to induce elevation of intracellular pH. Exp. Cell Res. (1991) 195:533–535.
   PubMed Web of Science ®Google Scholar
• YAMADA KM: Adhesive recognition sequences.J. Biol. Chem. (1991) 266:12809–12812.
   PubMed Web of Science ®Google Scholar
• RUOSLAHTI E, PIERSCHBACHER M: New Per-spectives in Cell Adhesion: RGD and Inte-grins. Science (1987) 238:491–497.
   PubMed Web of Science ®Google Scholar
• THIERY J-P, DUBAND J-L, DUFOUR S, SAVAGNER P, IMHOF B: Roles of Fibronectin in embryo-genesis in Biology of Extracellular Matrix: A Series: Fibronectin (1989) Mosher D (Ed), Academic Press, San Diego.
   Google Scholar
• McCowin( BA, ZETTER BR: Adhesive inter-actions in angiogenesis and metastasis. Phar-mac. Ther. (1992) 53:239–260.
   Google Scholar
• Review of neovascularization and endothelial cell biology from the standpoint of CMAPs.
   Google Scholar
• FAWCETT J, HARRIS A: Cell adhesion molecules and cancer. Curt: Opin. Oncol. (1992) 4(1):142–148.
   PubMedGoogle Scholar
• PREISSNER K, JENNE D: Vitronectin: a new molecular connection in haemostasis. Thromb. Haemostasis (1991) 66(2): 189–194.
   PubMed Web of Science ®Google Scholar
• COLVIN R: Fibronectin in wound healing. In: Biology of Extracellular Matrix: A Series: Fi-bronectin (1989) Mosher D (Ed), Academic Press, San Diego.
   Google Scholar
• SABA TM: Kinetics of plasma fibronectin: Relationship to phagocytic function and lung vascular integrit. In: Biology of Extra-cellular Matrix: A Series: Fibronectin (1989) Mosher D (Ed), Academic Press, San Diego.
   Google Scholar
• TAMKUN J, DESimoNE D, FONDA D, PATEL R, BUCK C, HoRwrrz A, HYNES R: Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell (1986) 46:271–282.
   PubMed Web of Science ®Google Scholar
• HYNES R: Integrins: A family of cell surface receptors. Cell (1987) 48:549–554.
   Google Scholar
• First classification of the integrin family and a thorough contemporary review.
   Google Scholar
• HYNES R: Integrins: Versatility, modulation and signaling in cell adhesion. Cell (1992)69: 11–25.
   Google Scholar
• Classic update of the 1987 review by a leading researcher.
   Google Scholar
• ALBELDA S, BUCK C: Integrins and other cell adhesion molecules. FASEB J. (1990) 4:2868–2880.
   PubMed Web of Science ®Google Scholar
• BRIESEWITZ R, EPSTEIN M, MARCANTONIO E: Expression of Native and Truncated Formsof the Human Integrin alpha-1 Subunit. J. Biol. Chem. (1993) 268(4):2989–2996.
   Google Scholar
• Cloning of cDNAs encoding the human a integrin subunit showed that secretion of a soluble truncated a-1 subunit required dimerization with soluble 131. Native and soluble c43 dimers appeared to be formed independently, suggest-ing the involvement of transmembrane or cytoplasmic do-mains in native heterodimer asembly.
   Google Scholar
• LEAVESLEY D, SCHWARTZ M, ROSENFELD M, CHERESH D: Integrin P-1-mediated and 13-3-mediated endothelial cell migration is triggered through distinct signaling mecha-nisms. J. Cell Biol. (1993) 120(6):1519–1527.
   Google Scholar
• Cell migration on collagen did not require the presence of extracellular calcium, whereas it was an absolute require-ment for vitronectin-mediated migration. Contact with Vn stimulated a rise in intracellular Ca2+ which required an extracellular calcium source, whereas there was no such effect of collagen.
   Google Scholar
• YAMADA Y, KLEINIVIAN H: Functional do-mains of cell adhesion molecules. Curr. Opin. Cell Biol. (1992) 4:819–823.
   PubMedGoogle Scholar
• DAmsKY CH, WERE Z: Signal transduction by integin receptors for extracellular ma-trix: cooperative processing of extracellu-lar information. Curr. Opin. Cell Biol. (1992) 4:772–781.
   PubMed Web of Science ®Google Scholar
• INGBER D: Integrins as mechanochemical transducers. Curr Opin. Cell Biol. (1991) 3:841–848.
   PubMed Web of Science ®Google Scholar
• GINSBERG M, DU X, PLOW E: Inside-out inte-grin signalling. Curr Opin. Cell Biol. (1992) 4:766–771.
   Google Scholar
• BLOBEL C, WHITE J: Structure, function and evolutionary relationship of protein contain-ing a disintegrin domain. Curr Opin. Cell Biol. (1992) 4:760–765.
   PubMedGoogle Scholar
• SCARBOROUGH R. ROSE J, NAUGHTON M, PHILLIPS D, NANNIZZI L, ARFSTEN A, CAMPBELL A, CHARO I: Characterization of the Integrin Specificities of Disintegrins Isolated from American Pit Viper Venoms. J. Biol. Chem. (1993) 268(2):1058–1065.
   Google Scholar
• A series of homologous disintegrins was isolated and used to demonstrate that amino acid sequences immediately ad-jacent to the RGD site can create an extended RGD locus. The nature of this locus and the presentation of the RGD sequence may be involved in determining integrin selec-tivity and affinity. Read in conjunction with patent [113].
   Google Scholar
• MORRISON P, EDSALL J, MILLER S: Prepara-tion and properties of serum and plasma proteins XVIII. The separation of purified fibrinogen from fraction I of human plasma. J. Am. Chem. Soc. (1948) 70:3103–3108.
   Google Scholar
• VAHERI A, MOSHER D: High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant tranforma-tion. Biochim. Biophys. Acta. (1978) 516:1–25.
   PubMed Web of Science ®Google Scholar
• HYNES R: Fibronectins. (1990) Springer-Verlag, New York.
   Google Scholar
• Essential reference tool for CMAP researchers: well-ref-erenced, informative, intelligent and thought-provoking.
   Google Scholar
• SCHWARZBAUER J: Alternative splicing of fi-bronectin: three variants, three functions. BioEssays (1991) 13(10):527–533.
   PubMed Web of Science ®Google Scholar
• GRINNELL F: Cellular adhesiveness and ex-tracellular substrata. Int. Rev. CytoL (1978) 53:65–144.
   PubMedGoogle Scholar
• PIERSCHBACHER M, Ruosuum E: The cell attachment activity of fibronectin can be du-plicated by small synthetic fragments of the molecule. Nature (1984) 309:30–33.
   Google Scholar
• Classic paper identifying the RGDS cell adhesion motif in fibronectin.
   Google Scholar
• D'SOUZA S, GINSBERG M, PLOW E: Arginyl-glycyl-aspartic acid (RGD): a cell adhesion TIBS (1991) 16:246–249.
   Google Scholar
• FAULL R, KOVACH N, HARLAN J, GINSBERG M: Affinity modulation of integrin alpha-5-0-1 - regulation of the functional response by soluble fibronectin. J. Cell Bid. (1993) 121(0:155–162.
   Google Scholar
• Use of an anti-131 monoclonal antibody suggests that the a5131 Fn integrin can exist in different affinity states. Phy-siological concentrations of soluble Fn occupy the high affinity receptors thereby inhibiting adhesion to immobi-lized Fn, whereas low affinity receptors remain unoccu-pied and are still able to mediate adhesion.
   Google Scholar
• GRINNELL F: Fibronectin Adsorption on Ma-terial Surfaces in Blood in contact with Nat-ural and Artificial Surfaces. (1987) Leonard E, Turitto E, Vroman L (Eds), The New York Academy of Sciences, New York.
   Google Scholar
• GuRRATE M, MULLER G, KEssLER H, AUMAILLEY M, TIMPL R: Conformation/activity stud-ies of rationally designed potent anti-adhe-sive RGD peptides. Ear. J. Biochem. (1992) 210:911–921.
   Google Scholar
• Used two-dimensional NMR and molecular modelling in the systematic design of cyclic RGD-based penta- and hexapeptides. A range of specificities and potencies (up to 100 times the inhibitory capacity of the linear GRGDS peptide) were obtained, demonstrating the potential for generating lead structures.
   Google Scholar
• GREENSPOON N, HERSHKOVIZ R, AWN R VARON D, SKENKMAN B, MARX G, FEDERMANS, ICAPUSTINA G, LITER O: Structural Anal-ysis of Integrin Recognition and the In-hibition of Integrin-Mediated Cell Func-tions by Novel Nonpeptidic Surrogates of the Arg-Gly-Asp Sequence. Biochemistry (1993) 32:1001–1008.
   Google Scholar
• Construction of structural RGD mimetics demonstrated active structures containing guanidinium and carboxylic groups separated by an 11-carbon atom backbone. The RGD surrogates inhibited platelet and cell adhesion in vitro, and CD4+ T-cell mediated hypersensitivity in vivo.
   Google Scholar
• TOMASIN1 B, MOSHER D: Vitronectin. Prog. Haem. Thromb. (1990) 10:269–305.
   Google Scholar
• CHARO I, NANNIZZI L, SMITH J, CHERESH D: The vitronectin Receptor av133 Binds Fi-bronectin and Acts in Concert with agil in Promoting Cellular Attachment and Cel-lular Attachment and Spreading on Fi-bronectin. J. Cell Biol. (1990) 1116(1)):2795–2800.
   Google Scholar
• Demonstration of the ability of the ability of different in-tegrins to act in concert: the av-03 Vn receptor, as well as the a5-131 Fn integrin, was shown to bind Fin in bio-chemical and cell assays.
   Google Scholar
• HORTON M: Current Status Review Vit-ronectin receptor: tissue specific expression or adaptation to culture? InL J. Exp. PathoL (1990) 71:741–759.
   Google Scholar
• UNDERWOOD P, BENNETT F: A comparison of the biological activities of the cell-adhesive proteins vitronectin and fibronectin. J. Cell Sci. (1989) 93:641–649.
   Google Scholar
• Paper in a series from this group using serum specifically depleted of Fn, Vn or both to study cell attachment mech-anisms in vitro in the presence of all other serum compo-nents. Particular attention is paid to the influence of the substrate on CMAP adsorption.
   Google Scholar
• BALE M, WOHLFAHRT L, MOSHER D, TOMASINI B, SUTTON R: Identification of Vitronectin as a Major Plasma Protein Adsorbed on Poly-mer Surfaces of Different Copolymer Com-position. Blood (1989) 74(8):2698–2706.
   Google Scholar
• Key paper identifying Vn as a major potential contributor to cell adhesion, due to its adsorption onto surfaces in the face of competition from other serum proteins.
   Google Scholar
• STEELE J, JOHNSON G, MCFARLAND C, DALTONB, GENGENBACH T, CHATELIER R, UNDERWOOD P, GREISER H: Roles of serum vitronectin, and fibronectin in initial attachment of hu-man vein endothelial cells, and dermal fi-broblasts on oxygen- and nitrogen-contain-ing surfaces made by radiofrequency plas-mas. J. Biomater. Sci. (Polymer Ed) (1993) In press.
   Google Scholar
• GECHTMAN Z, SHARMA R, KREIZMAN T FRIDKIN T, SHALTIEL S: Synthetic peptides derived from the sequence around the plas-min cleavage site in vitro nectin. Use in mapping the PAI-1 binding site. FEBS Lett. (1993) 315(3):293–297.
   Google Scholar
• Study using a series of 8 peptides derived from the plas-min cleavage site in Vn to map its binding site for plas-minogen activator inhibitor. Plasmin splits this site in two, thereby reducing the affinity of Vn for PAT, with haemo-static implications.
   Google Scholar
• ENGEL J: Laminins and Other Strange Proteins. Biochemistry (1992) 31(44):10643–10651.
   PubMed Web of Science ®Google Scholar
• SONNENBERG A: Laminin receptors in the in-tegrin family. Path. Biol. (1992) 40(8):773–778.
   PubMedGoogle Scholar
• TAWIL N, WILSON P, CARBororro S: Inte-grins in Point Contacts Mediate Cell Spread-ing: Factors that Regulate Integrins Accu-mulation in Point Contacts vs. Focal Con-tacts. J. Cell Biol. (1993) 120(1):261–271.
   PubMed Web of Science ®Google Scholar
• MECHAM R: Receptors for laminin on mam-malian cells. FASEB J. (1991) 5:2538–2546.
   PubMed Web of Science ®Google Scholar
• HUGHES R: Role of glycosylation in cell inter-actions with extracellular matrix. Biochem. Soc. Trans. (1992) 20:279–284.
   PubMed Web of Science ®Google Scholar
• WAGNER D: Cell Biology of von Willebrand factor. Anna. Rev. Cell Biol. (1990) 6:217–246.
   Web of Science ®Google Scholar
• KAuFivIAN R: Biological regulation of factor VIII activity. Annu. Rev. Med. (1992) 43:325–339.
   PubMed Web of Science ®Google Scholar
• PEERSCHKE E: Platelet Membrane Glyco-proteins. (Functional Characterization and Clinical Applications.). Clin. Pathol. (1992) 98(4):455–463.
   Google Scholar
• HAWIGER J, TIMMONS S: Binding of Fibrinogen and von Willebrand Factor to Platelet Glycoprotein Ilb-Illa Complex. Meth. Enzy-moL (1992) 215:228–243.
   Google Scholar
• Good practical guide for those venturing into the field of vWf and fibrinogen binding to platelets.
   Google Scholar
• ROTH GJ: Platelets and blood vessels: the adhesion event. Immunology Today (1992) 13(3):100–105.
   PubMedGoogle Scholar
• ERBAN J, WAGNER D: A 130-kDa Protein on Endothelial Cells Binds to Amino Acids 15-42 of the BB chain of fibrinogen. J. Biol. Chem. (1992) 267:2451–2458.
   PubMed Web of Science ®Google Scholar
• PARISE L, STEINER B, NANNIZZI L, CRISS A, PHILLIPS D: Evidence for novel binding sites on the platelet glycoprotein lib and 111a sub-units and immobilized fibrinogen. Biochem. J. (1993) 289:445–451.
   Google Scholar
• Study showing that although RODS-mediated fibrinogen attachment to the GP(a1113/133 integrin) requiresthe intact complex, another RGD-independant mechanism also operates. The second mechanism appears to be non-covalent, irreversible, calcium independant, and may de-pend on the conformation of fibrinogen: a good example of the complexity of adhesive mechanisms.
   Google Scholar
• RUGGERI Z: Von Willebrand factor as a tar-get for antithrombotic interventon. Circula-tion (1992) 86(Suppl 6):26–29.
   Google Scholar
• WILLIAMS J, RUCINSKI B, HOLT J, NIEWIAROW-SKI S: Elegantin and Albolabrin purified peptides from viper venoms; homologied with the RGDS domain of fibrinogen and von Willebrand factor. Biochim. Biophys. Acta (1990) 1039:81–89.
   PubMed Web of Science ®Google Scholar
• HOOK M, WOODS A, JOHANSSON S, KJELLEN L, COUCHMAN JR: Functions of proteogly-cans at the cell surface. In: Functions of the proteoglycans Ciba Foundation Symposium 124, John Wiley, Chichester. (1986) 143–157.
   Google Scholar
• GALLAGHER JT, TURNBULL JE: Heparan sul-phate in the binding and activation of ba-sic fibroblast growth factor. GlycobioL (1992) 2:523–528.
   PubMed Web of Science ®Google Scholar
• COSTER L, MALMSTROM A, CARLSTEDT I, FRANSSON L-A: The core protein of pro-teoheparan sulphate consists of disulphide-bonded subunits. Biochem. J. (1983) 215:417–419.
   PubMed Web of Science ®Google Scholar
• FRANSSON L-A, CARLSTEDT I, COSTER L, MALMSTROM A: Binding of transferrin to the core protein of fibroblast proheparan sulphate. Proc. Natl. Acad. Sci. USA (1984) 81:5657–5661.
   PubMed Web of Science ®Google Scholar
• MALI M, JAAKKOLA P, ARVILOMMI A-M, JALKANEN M: Sequence of human synde-can indecates a novel gene family of inte-gral membrane proetoglycans. J. Biol. Chem. (1990) 265:6884–6889.
   PubMed Web of Science ®Google Scholar
• RAPRAEGER A: Transformation growth fac-tor (type-beta) promotes the addition of chondroitin sulphate chains to the cell surface proteoglycan (syndecan) of mouse mammary epithelia. J. Cell Biol. (1989) 109:2509–2518.
   PubMed Web of Science ®Google Scholar
• CULTY M, MIYAKE K, KINCADE PW, SILORSKIE, BUTCHER EC, UNDERHILL C: The hyaluro-nate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins../. Cell Biol. (1990) 111:2765–2774.
   PubMed Web of Science ®Google Scholar
• HARDINGHAM TE, FOSANG AJ: Proteoglycans: many forms and may functions. FASEB .1. (1992) 6:861-870.
   Google Scholar
• Comprehensible overview of proteoglycans basic forms.
   Google Scholar
• UNDERHILL C: CD44: The hyaluronan re-ceptor. J. Cell Sci. (1992) 103:293–298.
   PubMed Web of Science ®Google Scholar
• NOONAN DM, FULLE A, VELEN'TE P et al.: The complete sequence of perlecan, a membrane heparan sulphate proteoglycan, reveals ex-tensive similarity with laminin A chain, low density lipoprotein-receptor and the neural cell adhesion molecule. J. Biol. Chem. (1991) 266:22939–22947.
   Google Scholar
• CHIQUET-EHRISMANN R: Anti-adhesive mole-cules of the extracellular matrix. Curr Opin. Cell Biol. (1991) 3:800–804.
   PubMed Web of Science ®Google Scholar
• BORNSTEIN P: Thrombospondins: structure and regulation of expression. FASEB J. (1992) 6:3290–3299.
   PubMed Web of Science ®Google Scholar
• RIOu J, UMBHAUER M, SHI D, BOUCAUT J: Tenascin: a potential modulator of cell-ex-tracellular matrix interactions during verte-brate embryogenesis. Biol. Cell. (1992) 75:1–9.
   PubMed Web of Science ®Google Scholar
• SAGE E, BORNSTEIN P: Extracellular Proteins That Modulate Cell-Matrix Interactions. J. Biol. Chem. (1991) 266(23):14831–14834.
   PubMed Web of Science ®Google Scholar
• BUTLER W: The Nature and Significance of Osteopontin. Conn. Tiss. Res. (1989) 23:123–136.
   PubMed Web of Science ®Google Scholar
• VAN DER REST M, GARRONE R: Collagen family of proteins. FASEB J. (1991) 5:2814–2823.
   Google Scholar
• Excellent summary of current structural classification of the collagens.
   Google Scholar
• JUST M, HERBST H, HUMMEL M et al.: Un-dulin is a novel member of the fibronectin-tenascin family of extracellular matrix gly-coproteins. J. Biol. Chem. (1991) 266:17326–17332.
   PubMed Web of Science ®Google Scholar
• TRUEB J, TRUEB B: Type IV collagen is a variant of undulin. Eur. J. Biochem. (1992) 207:549–557.
   PubMedGoogle Scholar
• LEGAN P, COLLINS J, GARROD D: The Molecu-lar Biology of Desmosomes and Hemidesmo-somes: "What's in a name?" BioEssays (1992) 14:385–393.
   PubMed Web of Science ®Google Scholar
• GEIGER B, AYALON O: Cadherins. Annu. Rev. Cell. Biol. (1992) 8:307–32.
   PubMedGoogle Scholar
• KEELAN E, HASICARD D: CAMS and anti-CAMS: the clinical potential of cell adhesion molecules. J. R. Coll. Physicians Lond. (1992) 26(1):17–24.
   PubMedGoogle Scholar
• SABA TM: Fibronectin: role in phagocytic host defence and lung vascular injury. In: Fi-bronectin in health and disease. (1989) Carsons SE (Ed) CRC Press, Boca Raton, Florida pp49–68.
   Google Scholar
• HUMPHRIES MJ, OLDEN K, YAMADA KM: Fibronectin and cancer: Implications of cell adhesion to fibronectin for metastasis. In: Fi-bronectin in health and disease (1989) Car-sons SE (Ed) CRC Press, Boca Raton, Florida, pp161–199.
   Google Scholar
• A detailed review and huge bibliography.
   Google Scholar
• GRINNELL F: Fibronectin and wound healing (1984) 26:107–116.
   Google Scholar
• GROSSMAN JE: Plasma fibronectin and fi-bronectin therpay in sepsis and critical ill-ness. Rev. Infect. Dis. (1987) 9 (Suppl 4):S420–430.
   Google Scholar
• BROWN RA: Failure of fibronectin as an op-sonin in the host defence system. A case of competitive self inhibition? Lancet (1983) II:1058–60.
   Google Scholar
• NISHIDA T, NAKAGAWA S, NISHIBAYASHI C, TANAKA H, MANABE R: Fibronectin enhance-ment of corneal epithelial wound healing of rabbits in vivo. Arch. Ophthalmol. (1984) 102:455–456.
   Google Scholar
• NISHIDA T, °BASHI Y, AWATA T, MANABE R: Fibronectin a new therapy for trophic corneal ulcer. Arch. Ophthalmol. (1983) 101: 1046–1048.
   PubMedGoogle Scholar
• KONO I et al.: Beneficial effect of topical fi-bronectin in patients with keratoconjunctivi-tis Sicca of Sjogren's syndrome. J. Rheuma-tol. (1985) 12:487–489.
   PubMed Web of Science ®Google Scholar
• LioTTA LA: Tumor invasion and metasta-sis: role of the basement membrane. Am. .1. Pathol. (1984) 117:339–348.
   Google Scholar
• IWAMOTO Y, ROBEY FA, GRAF J et al.: YIGSR, A synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science (1987) 238:1132–1134.
   PubMed Web of Science ®Google Scholar
• KANEMOTO T, REICH R, ROYCE L et al.: Iden-tification of an amino acid sequence from the laminin A chain that stimulates metastasis and collagenase IV production. Proc. Natl. Acad. Sci. USA (1990) 87:2279–2283.
   PubMed Web of Science ®Google Scholar
• ROYCE LS, MARTIN GR, KLEINMAN HK: Induction of an invasive phenotype in benign tumor cells with a laminin A-chain synthetic peptide. Invasion Metastasis (1992) 12:149–155.
   Google Scholar
• Murine melanoma cell lines stimulated to produce type VI collagen degrading protease and to invade a matrigel sub-strate by peptide PA22–2, containing laminin sequence.
   Google Scholar
• GRANT DS, KINSELLA JL, FRIDMAN R et al.: Interaction of endothelial cells with a laminin A-chain peptide (SIKVAV) in vitro and induction of angiogenic behaviour in vivo. J. Cell Physiol. (1992) 153:614–625.
   PubMed Web of Science ®Google Scholar
• WEST DC, HAMPSON IN, ARNOLD F, KUMAR S: Angiogenesis induced by degradation products of hyaluronic acid. Science (1985) 228:1324–1326.
   Google Scholar
• First identification of this source of angiogenic activity with its implications for the importance of hyaluronan breakdown.
   Google Scholar
• VAHERI A, STEPHENS RW, SALONEN E-M, POLLANEN J, TAPIOVAARA H: Plasminogen activation at the cell surface-matrix inter-face. Cell Differentiation and Development (1990) 32:255–262.
   PubMedGoogle Scholar
• BERMAN M, MONSEAU E, LAW M, AIKEN D: Ulceration is correlated with degradation of fibrin and fibronectin at the corneal surface. Invest. Ophthal. Vis. Sci. (1983) 24:1358–1366.
   PubMed Web of Science ®Google Scholar
• NIMNI ME, CHEUNG DT, STRATES B, KODAMA M, SHEIK K: Bioprosthesis derived from crosslinked and chemically modified collage-nous tissues. In: Collagen (1988) Nimni ME (Ed) CRC Press, Boca Raton, Florida, Volume ppl -38.
   Google Scholar
• Good introductory overview.
   Google Scholar
• YANNAS IV: Regeneration of skin and nerve by use of collagen templates. In: Collagen vol III Biotechnology (1988) Nimni ME (Ed) CRC press, Florida, pp87–115.
   Google Scholar
• An important summary of influential concepts and obser-vations in the field.
   Google Scholar
• DOILLON CJ, SILVER FH: Collagen-based wound dressing: effects of hyaluronic acid and fibronectin on wound healing. Biomate-rials (1986) 7:3–7.
   PubMed Web of Science ®Google Scholar
• Darr VM, HAVERSTICK DM, O'RouRKE K et al.: Inhibition of platelet aggregation by a monoclonal antibody to human fibronectin. Proc. NatI Acad. Sci. USA (1985) 82:3844–3849.
   PubMed Web of Science ®Google Scholar
• JILEK F, HORMANN H: Cold insoluble globu-lin III. Cyanogen bromide and plasminoly-sis fragments containing a label introduced by transamidation. Hoppe-Seyler's Z Physiol. Chem. (1977) 358:1165–1173.
   Google Scholar
• GAUSS-MULLER V, KLEINMAN HK, MARTIN GR, SCH1FFMANN E: Role of attachment fac-tors and attractants in fibroblast chemo-taxis. J. Lab. Clin. Med. (1980) 96:1071–1080.
   PubMed Web of Science ®Google Scholar
• KURKINEN M, VAHERI A, ROBERTS PJ, STENMAN S: Sequential appearance of fibronectin and collagen in experimental granulation tissue. Lab. Invest. (1980) 43:47–53.
   PubMed Web of Science ®Google Scholar
• HYNES RO: Wound healing, inflammation and fibrosis. In: Fibronectins (1988) Springer-Verlag, New York, pp349–364.
   Google Scholar
• FALCONE PA, BONAVENTURA M, TURNER DC, FROMM D: The effect of exogenous fi-bronectin on wound breaking strength. Plas-tic Reconstructive Surg. (1984) 74:809–812.
   PubMed Web of Science ®Google Scholar
• BROWN RA, BLUNN GW, EJIM OS: Prepa-ration of orientated fibrous mats from fi-bronectin: composition and stability. Sub-mitted.
   Google Scholar
• HYNES RO: Biosynthesis and fibrillogenesis. In: Fibronectins. (1988) Springer-Verlag, New York, pp176–199.
   Google Scholar
• EJIM OS, BLUNN GW, BROWN RA: Produc-tion of artificial orientated mats and strands from plasma fibronectin: a morphological study. Biomaterials In press.
   Google Scholar
• JACKSON DS: The Dermal Scar. In: Collagen in Health and Disease (1982) Weiss JB, Jayson MIV (Eds), Churchill-Livingstone, Edinburgh, pp466–473.
   Google Scholar
• CARDARELLI PM, YAMAGATA S. IKUHIKO T, GORCSAN S. CHIANG SL, LOBI T: The collagen receptor a2-131, from MG-63 and HT 1080 cells interacts with cyclic RGD peptides. J. Biol. Chem. (1992) 267:23159–23164.
   PubMed Web of Science ®Google Scholar
• NISHIYAMA T, TOMIGAWA N, NAKAJMA K, HAYASHI T: Quantitative evaluation of the factors affecting the process of fibroblast-mediated collagen gel contraction by sepa-rating the process into three phases. Colla-gen Relat. Res. (1988) 8:259–273.
   PubMedGoogle Scholar
• TIOLLIER J, DUMAS H, TARDY M, TAYOT J-L: Fibroblast behaviour on gels of type LIII and IV human placental collagens. Exp. Cell Res. (1990) 191:95–104.
   PubMed Web of Science ®Google Scholar
• Trvois E, TOILLIER J, GAUCHERAND M, DUMAS H, TARDY M, THIVOLET J: In vitro and post transplantation differentiation of hu-man keratinocytes grown on the human type IV collagen film of a bilayered dermal sub-stitute. Exp. Cell Res. (1991) 193:310–319.
   PubMed Web of Science ®Google Scholar
• THOMPSON ICP, HANNA KD, GIPSON IK, GRAVAGNA P, WARING GO, JOHNSON-WINT B: Synthetic Epikeratoplasty in Rhesus mon-keys with human type IV collagen. Cornea (1993) 12:35–45.
   PubMed Web of Science ®Google Scholar
• LAQUERRIERE A, YUN J, TOILLIER J, HEMET J, TADM M: Experimental evaluation of bilay-ered human collagen as a dural substitute. .1. Neurosurg. (1993) 78:487–491.
   PubMed Web of Science ®Google Scholar
• MORGON A, DISANT F, TRUY E: Experimental study of collagen as eardrum graft support in dogs. Acta Otolaryngol. (1989) 107:450–455.
   PubMed Web of Science ®Google Scholar
• LUNDBORG G: Nerve Injury and Repair. (1988) Churchill Livingstone, Edinburgh, pp 1–31.
   Google Scholar
• YUN J, TIOLLIER I, TARDY M etal.: Nerve re-generation using a human placental collagen type IV/IVox tube. Proceedings of the Eur-popean 7issue Repair Society (1992) 46.
   Google Scholar
• GRANT DS, TASHIRO K-I, SEGUI-REAL B, YAMADA Y, MARTIN GR, KLEINMAN HK: Two laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro. Cell (1989) 58:933–943.
   Google Scholar
• GRANT DS, KINSELLA J, CID MC, KLEINMAN HK: Specific Lamjnin domains mediate en-dothelial cell adhesionand angiogenesis. In: Angiogenesis in health and disease (1992) Maragoudalcis ME et al. (Eds) Plenum Press, New York pp99–110.
   Google Scholar
• MADRI JA, WILLIAMS SK: Capillary endo-thelial cell culutres: phenotypic modulation by matrix components. J. Cell Biol. (1983) 97:153–165.
   PubMed Web of Science ®Google Scholar
• INGBER DE: Fibronectin controls endothelial cell gowth by modulating cell shape. Proc. Natl. Acad. Sci. USA (1990) 87:3579–83.
   Google Scholar
• Pivotal observations linking CMAP function with growth factor action.
   Google Scholar
• BREM SS, ZAGZAG D, TSANACLIS AMC, GATLEY S, ELKOUBY M-P, BREIN SE: In-hibition of angiogenesis and tumour growth in the brain: suppression of endothelial cell turnover by penicillamine and the depletion of copper: an angiogenic co-factor. Am. J. Pathol. (1990) 137:1121–1142.
   PubMed Web of Science ®Google Scholar
• AuERBAcH R: Patterns of tumour metasta-sis: organ selectivity in the spread of cancer cells. Lab. Invest. (1988) 58:361–364.
   PubMed Web of Science ®Google Scholar
• Cox DA, KiNz S. CERLETTI N, MCMAS'TER GK, BuRic RR: Wound healing in aged an-imals - effects of locally appled TGF-B2 in different model systems. In: Angiogenesis (1992) Steiner R et al. (Eds) Birkhauser-Ver-lag, Basel, pp287–295.
   Google Scholar
• BROWN RA, WEISS JB: Neovascularisation and its role in the osteoarthritic process. Ann. Rheum. Dis. (1988) 47:881–885.
   PubMed Web of Science ®Google Scholar
• STEVENS CR, WILLIAMS RB, FARRELL AJ, BLAKE DR: Hypoxia and inflammatory syn-ovitis: observations and speculations. Ann. Rheum. Dis. (1991) 50:124.
   PubMed Web of Science ®Google Scholar
• FRIDMAN R, GIACCONE G, KANEmoro T, MARTIN GR, GAZDAR AF, MULSHINE JL: Re-constituted basement membrane (matrigel) and laminin can enhance the tumorigenic-ity and the drug resistance of small cell lung cancer cell lines. Proc. Natl. Acad. Sci. USA (1990) 87:6698–6702.
   PubMed Web of Science ®Google Scholar
• MAST BA, FLOOD LC, HAYNES JH et al.: Hyaluronic acid is a major component of the matrix of foetal rabbit skin and wounds: im-plications for healing and regeneration. Ma-trix (1991) 11:63–68.
   Google Scholar
• FAVARO G, SCHIAVINATO A, LANGONE F, SPIN' S, LINT E, GOVONI E: Peripheral nerve re-generation through resorbable and perma-nent nerve guides: A comparison in long term pathologic alterations. Proceedings of the Eurpopean Tissue Repair Society (1992) 47.
   Google Scholar
• BROWN RA, MORE J, EJIM OS: Preparation of a gold-binding conjugate containing gold thiomalate. Artzenmietel Forcsh. (1993) 43: 682–685.
   Google Scholar
• BROWN RA, WELLS TM: Interaction and aggregation of gold thiomalate (myocrysin) and poly L-lysine. J. Phann. Pharmacol. (1992) 44:467–471.
   PubMed Web of Science ®Google Scholar
• PESSA ME, BLAND KI, COPELAND EM: Growth factors and determinants of wound repair. J. Surg. Res. (1987) 142:201–217.
   Google Scholar
• BURGESS WH, MACIAG T: The heparin bind ing growth factor family of proteins. Ann. Rev. Biochem. (1989) 58:575–606.
   Google Scholar
• Review of FGF-like growth factor family with classifica-tion based on ability to bind to heparin.
   Google Scholar
• ANDRADE JD, HLADY V: Protein Adsorp-tion and Materials Biocompatibility: A Tuto-rial Review and Suggested Hypotheses. Adv. Polym. Sci. (1986) 79:1–63.
   Web of Science ®Google Scholar
• BRASH JL: The fate of Fibrinogen following adsorption at the blood biomaterial inter-face. In: Blood in contact with Natural and Ar-tificial Surfaces. (1987) Leonard E, Turitto E, Vroman L (Eds), The New York Academy of Sciences, New York.
   Google Scholar
• OKADA T, IKADA Y: In vitro and in vivo diges-tion of collagen covalently immobilized onto the silicone surface. J. Biomed. Mater Res. (1992) 26:1569–1581.
   PubMed Web of Science ®Google Scholar
• GRINNELL F: Focal adhesion sites and the re-moval of substratum-bound fibronectin. J. Cell. Biol. (1986) 103:2697–2706.
   PubMed Web of Science ®Google Scholar
• WILLIAMS DF: A model for biocompatibil-ity and its evaluation. J. Biomed. Eng. (1989) 11:185–191.
   PubMedGoogle Scholar
• CHENG S-S, CHITTUR K, SUKENIK C, CULP L, LEWANDOWSKA K: The conformation of fibronectin on self-assembled monolayers with different surface composition: an FT-IR/ATR study. Nineteenth Annual Meeting of the Society for Biomaterials (1993) Birming-ham, AL, USA, 308.
   Google Scholar
• UNDERWOOD P, STEELE J, DALTON B: Effects of polystyrene surface chemistry on the bio-logical activity of solid phase fibronectin and vitronectin, analysed with monoclonal anti-bodies. J. Cell Sci. (1993) 104(3):793.
   PubMed Web of Science ®Google Scholar
• BRUNSTEDT M, ZIATS N, ROSE-CAPRARA V HILTNER P. ANDERSON J, LODOEN G, PAYET C: Attachment and proliferation of bovine aortic endothelial cells onto additive modi-fied poly(ether urethane ureas). J. Biomed. Mater Res. (1993) 27:483–492.
   Google Scholar
• Typical study of in vitro cell/CMAP/surface interactions from a leading biomaterials group, well-referenced and discussed in context of current literature.
   Google Scholar
• HERBERT C, DRUMHELLER P, ELBERT D, PATHAK C, HUBBELL J: Cell-Nonadhesiveness of pHEMA hydrogel copolymerized with bi-functional PEG diacrylate and EMA is de-pendent on PEG concentration and molecu-lar weight. Nineteenth Annual Meeting of the Society for Biomaterials (1993) Birmingham, AL, USA, 177.
   Google Scholar
• MERRILL EW: Distinctions and Correspondences among Surfaces Contacting Blood in Blood in contact with Natural and Artificial Surfaces. (1987) Leonard E, Turitto E, Vroman L (Eds), The New York Academy of Sciences, New York.
   Google Scholar
• Brief review of surface properties in relation to adsorption of blood proteins onto biomaterials.
   Google Scholar
• ANDERSON J, KOTTKE-MARCHANT K: Platelet Interactions with Biomaterials and Artificial Devices. CRC Crit. Rev. Biocompat. (1985) 1(2): 111–204 .
   Google Scholar
• LIN HB, GARCIAECHEVERRIA C, ASAKURA S. SUN W, MOSHER DF, COOPER SL: Endothelial Cell Adhesion on Polyurethanes Containing Covalently Attached RGD-Peptides. Bioma-terials (1992) 13(13):905–914.
   Google Scholar
• HUBBELL J, MASSIA S, DESAI N, DRUMHELLER P: Endothelial cell-Selective materials for tis-sue engineering in the vascular graft via a new receptor. BioffechnoL (1991) 9:568–572.
   Google Scholar
• Good study identifying REDV as an adhesive sequence for endothelial cells but not platelets and subsequently grafting it to substrates for vascular applications. Read in conjunction with reference [1481.
   Google Scholar
• MASSIA S, HUBBELL J: Vascular Endothelial Cell Adhesion and Spreading Promoted by the Peptide REDV of the IIICS Region of Plasma Fibronectin Is Mediated by Integrin a4[31. J. Biol. Chem. (1992) 267(20):14019–14026.
   Google Scholar
• Elegant study showing that endothelial cell binding to the REDV peptide is mediated via the ct4131 integrin which is not found on platelets. Potential mechanism for enhancing endothelialization without platelet adhesion.
   Google Scholar
• RATNER B: Plasma deposition for biomedical applications: A brief review. J. Biomater. Sci. Polymer Ed. (1992) 4(1):3–11.
   PubMed Web of Science ®Google Scholar
• GOMBOTZ WR, HOFFMAN AS: Gas-discharge techniques for biomaterial modification. CRC Crit. Rev. Biocompat. (1987) 4(1):1–42.
   Google Scholar
• Excellent thorough review of plasma modification and its medical applications. Recommended as a starting point for any newcomer to the field.
   Google Scholar
• CHEHROUDI B, GOULD T, BRUNEI 1E, D: Ef-fects of a grooved titanium-coated implant surface on epithelial cell behavior in vitro and in vivo. .1. Biomat Mater Res. (1989) 23:1067–1085.
   Google Scholar
• MEYLE J, GULTIG K: Focal adhesion sites of human fibroblasts grown on microstruc-tured surfaces. Nineteenth Annual Meeting of the Society for Biomaterials. (1993) Birming-ham, AL, USA, 283.
   Google Scholar
• PULE° D, PRESTON K, SHAFFER J, BIZIOs R: Examination of osteoblast/orthopaedic bio-material interactions using molecular tech-niques. Biomaterials (1993) 14(2): 111–114 .
   PubMed Web of Science ®Google Scholar
• KLINKMANN H, IVANOVITCH P: Biocompati- bility: The need for a systems approach. J. Lab. Clin. Med. (1993) 121:203–204.
   Google Scholar
• Commentary on the problems besetting biomaterials re-search and the need to consider the compound/material/-device/procedure/patient as a system for evaluation.
   Google Scholar
• WEAVER D, Prrr W: Molecular dynam-ics simulations of protein interactions with polymer surfaces. Nineteenth Annual Meeting of the Society for Biomaterials. (1993) Birm-ingham, AL, USA, 179.
   Google Scholar
• ALON R, BAYER E, WILCHEK M: Cell Adhe- sion to Streptavidin via RGD Dependent In-tegrins. Eur J. Cell. Biol. (1993) 60(1):1–11.
   Google Scholar
• Interesting discovery that streptavidin undergoes confor-mational change following biotin binding, leading to the exposure of an RYD sequence which has high RGD homology and therefore binds cells via integrin receptors.
   Google Scholar
• HANEIN D, SABANAY H, ADDADI L, GEIGER B: Selective interactions of cells with crystal surfaces. Implications for the mechanism of cell adhesion. J. Cell Sci. (1993) 104:275–288.
   Google Scholar
• Novel use of calcium (R,R)-tartrate tetrahydrate crystals with two chemically equivalent but structurally distinct faces. One face was directly adhesive for cells, leading to protein-independant attachment and cell death, whilst the other showed slower cell adhesion mediated by CMAPs.
   Google Scholar
• TRAVIS J: Biotech gets a grip on cell adhe-sion. Science (1993) 260:906–908.
   PubMed Web of Science ®Google Scholar