Alkaline Phosphatase, Defensin Gene Expression and Effect of Myeloid Cell Growth Factors in Normal and Leukemic Cells

References

• Borregaard N. The human neutrophil. Function and dysfunction. European Journal of Haematology 1988; 41: 401–413
   PubMed Web of Science ®Google Scholar
• Bainton D. F., Ullyot J. L., Farquhar M. G. The development of neutrophilic polymorphonuclear leukocytes in human bone marrow. Journal of Experimental Medicine 1971; 134: 907–934
   PubMed Web of Science ®Google Scholar
• Lehrer R. I., Ganz T. Antimicrobial polypeptides of human neutrophils. Blood 1990; 76: 2169–2181
   PubMed Web of Science ®Google Scholar
• Bainton D. F., Farquhar M. G. Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells. Journal of Cell Biology 1968; 39: 299–317
   PubMed Web of Science ®Google Scholar
• Ganz T., Selsted M. E., Szklarek D., Harwig S. S., Daher K., Bainton D. F., Lehrer R. I. Defensins. Natural peptide antibiotics of human neutrophils. Journal of Clinical Investigation 1985; 76: 1427–1435
   PubMed Web of Science ®Google Scholar
• Starkey P. M., Barrett A. J. Human cathepsin G. Catalytic and immunological properties. Biochemical Journal 1976; 155: 273–278
   PubMed Web of Science ®Google Scholar
• Campanelli D., Detmers P. A., Nathan C. F., Gabay J. E. Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties. Journal of Clinical Investigation 1990; 85: 904–915
   PubMed Web of Science ®Google Scholar
• Weiss J., Olsson I. Cellular and subcellular localization of the bactericidal/permeability-increasing protein of neutrophils. Blood 1987; 69: 652–659
   PubMed Web of Science ®Google Scholar
• Spitznagel J. K., Dalldorf F. G., Leffell M. S., Folds J. D., Welsh I. R., Cooney M. H., Martin L. E. Character of azurophil and specific granules purified from human polymorphonuclear leukocytes. Laboratory Investigation 1974; 30: 774–785
   PubMed Web of Science ®Google Scholar
• Bretz U., Baggiolini M. Biochemical and morphological characterization of azurophil and specific granules of human neutrophilic polymorphonuclear leukocytes. Journal of Cell Biology 1974; 63: 251–269
   PubMed Web of Science ®Google Scholar
• Damiano V. V., Kucich U., Murer E., Laudenslager N., Weinbaum G. Ultrastructural quantitation of peroxidase- and elastase-containing granules in human neutrophils. American Journal of Pathology 1988; 131: 235–245
   PubMed Web of Science ®Google Scholar
• West B. C., Rosenthal A. S., Gelb N. A., Kimball H. R. Separation and characterization of human neutrophil granules. American Journal of Pathology 1974; 77: 41–66
   PubMed Web of Science ®Google Scholar
• Cramer E., Pryzwansky K. B., Villeval J. L., Testa U., Breton-Gorius J. Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold. Blood 1985; 65: 423–432
   PubMed Web of Science ®Google Scholar
• Ringel E. W., Soter N. A., Austen K. F. Localization of histaminase to the specific granule of the human neutrophil. Immunology 1984; 52: 649–658
   PubMed Web of Science ®Google Scholar
• Kjeldsen L., Bainton D. F., Sengelov H., Borregaard N. Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation. Blood 1993; 82: 3183–3191
   PubMed Web of Science ®Google Scholar
• Kjeldsen L., Bainton D. F., Sengelov H., Borregaard N. Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils. Blood 1994; 83: 799–807
   PubMed Web of Science ®Google Scholar
• Murphy G., Reynolds J. J., Bretz U., Baggiolini M. Collagenase is a component of the specific granules of human neutrophil leucocytes. Biochemical Journal 1977; 162: 195–197
   PubMed Web of Science ®Google Scholar
• Segal A. W., Jones O. T. The subcellular distribution and some properties of the cytochrome b component of the microbicidal oxidase system of human neutrophils. Biochemical Journal 1979; 182: 181–188
   PubMed Web of Science ®Google Scholar
• Borregaard N., Heiple J. M., Simons E. R., Clark R. A. Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: translocation during activation. Journal of Cell Biology 1983; 97: 52–61
   PubMed Web of Science ®Google Scholar
• Borregaard N., Tauber A. I. Subcellular localization of the human neutrophil NADPH oxidase. b-Cytochrome and associated flavoprotein. Journal of Biological Chemistry 1984; 259: 47–52
   PubMed Web of Science ®Google Scholar
• Jesaitis A. J., Buescher E. S., Harrison D., Quinn M. T., Parkos C. A., Livesey S., Linner J. Ultrastructural localization of cytochrome b in the membranes of resting and phagocytosing human granulocytes. Journal of Clinical Investigation 1990; 85: 821–835
   PubMed Web of Science ®Google Scholar
• Fletcher M. P., Gallin J. I. Human neutrophils contain an intracellular pool of putative receptors for the chemoattractant N-formyl-methionyl-leucyl-phenylalanine. Blood 1983; 62: 792–799
   PubMed Web of Science ®Google Scholar
• Yoon P. S., Boxer L. A., Mayo L. A., Yang A. Y., Wicha M. S. Human neutrophil laminin receptors: activation-dependent receptor expression. Journal of Immunology 1987; 138: 259–265
   PubMed Web of Science ®Google Scholar
• Bainton D. F., Miller L. J., Kishimoto T. K., Springer T. A. Leukocyte adhesion receptors are stored in peroxidase-negative granules of human neutrophils. Journal of Experimental Medicine 1987; 166: 1641–1653
   PubMed Web of Science ®Google Scholar
• Singer I. I., Scott S., Kawka D. W., Kazazis D. M. Adhesomes: specific granules containing receptors for laminin, C3bi/fibrinogen, fibronectin, and vitronectin in human polymorphonuclear leukocytes and monocytes. Journal of Cell Biology 1989; 109: 3169–3182
   PubMed Web of Science ®Google Scholar
• Sengelov H., Kjeldsen L., Diamond M. S., Springer T. A., Borregaard N. Subcellular localization and dynamics of Mac-1 (alpha m beta 2) in human neutrophils. Journal of Clinical Investigation 1993; 92: 1467–1476
   PubMed Web of Science ®Google Scholar
• Dewald B., Bretz U., Baggiolini M. Release of gelatinase from a novel secretory compartment of human neutrophils. Journal of Clinical Investigation 1982; 70: 518–525
   PubMed Web of Science ®Google Scholar
• Kjeldsen L., Bjerrum O. W., Askaa J., Borregaard N. Subcellular localization and release of human neutrophil gelatinase, confirming the existence of separate gelatinase-containing granules. Biochemical Journal 1992; 287: 603–610
   PubMed Web of Science ®Google Scholar
• Morel F., Dewald B., Berthier S., Zaoui P., Dianoux A. C., Vignais P. V., Baggiolini M. Further characterization of the gelatinase-containing particles of human neutrophils. Biochimica et Biophysica Acta 1994; 1201: 373–380
   PubMed Web of Science ®Google Scholar
• Mollinedo F., Schneider D. L. Subcellular localization of cytochrome b and ubiquinone in a tertiary granule of resting human neutrophils and evidence for a proton pump ATPase. Journal of Biological Chemistry 1984; 259: 7143–7150
   PubMed Web of Science ®Google Scholar
• Lacal P., Pulido R., Sanchez-Madrid F., Mollinedo F. Intracellular location of T200 and Mo1 glycoproteins in human neutrophils. Journal of Biological Chemistry 1988; 263: 9946–9951
   PubMed Web of Science ®Google Scholar
• Mollinedo F., Gomez-Cambronero J., Cano E., Sanchez-Crespo M. Intracellular localization of platelet-activating factor synthesis in human neutrophils. Biochemical & Biophysical Research Communications 1988; 154: 1232–1239
   PubMed Web of Science ®Google Scholar
• Hibbs M. S., Bainton D. F. Human neutrophil gelatinase is a component of specific granules. Journal of Clinical Investigation 1989; 84: 1395–1402
   PubMed Web of Science ®Google Scholar
• Borregaard N., Miller L. J., Springer T. A. Chemoattractant-regulated mobilization of a novel intracellular compartment in human neutrophils. Science 1987; 237: 1204–1206
   PubMed Web of Science ®Google Scholar
• Borregaard N., Christensen L., Bejerrum O. W., Birgens H. S., Clemmensen I. Identification of a highly mobilizable subset of human neutrophil intracellular vesicles that contains tetranectin and latent alkaline phosphatase. Journal of Clinical Investigation 1990; 85: 408–416
   PubMed Web of Science ®Google Scholar
• Kobayashi T., Robinson J. M. A novel intracellular compartment with unusual secretory properties in human neutrophils. Journal of Cell Biology 1991; 113: 743–756
   PubMed Web of Science ®Google Scholar
• Sengelov H., Nielsen M. H., Borregaard N. Separation of human neutrophil plasma membrane from intracellular vesicles containing alkaline phosphatase and NADPH oxidase activity by free flow electrophoresis. Journal of Biological Chemistry 1992; 267: 14912–14917
   PubMed Web of Science ®Google Scholar
• Bjerrum O. W., Borregaard N. Dual granule localization of the dormant NADPH oxidase and cytochrome b559 in human neutrophils. European Journal of Haematology 1989; 43: 67–77
   PubMed Web of Science ®Google Scholar
• Calafat J., Kuijpers T. W., Janssen H., Borregaard N., Verhoeven A. J., Roos D. Evidence for small intracellular vesicles in human blood phagocytes containing cytochrome b558 and the adhesion molecule CD11b/CD18. Blood 1993; 81: 3122–3129
   PubMed Web of Science ®Google Scholar
• Rice W. G., Ganz T., Kinkade J., Jr., Selsted M. E., Lehrer R. I., Parmley R. T. Defensin-rich dense granules of human neutrophils. Blood 1987; 70: 757–765
   PubMed Web of Science ®Google Scholar
• Borregaard N., Cowland J. B. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 1997; 89: 3503–3521
   PubMed Web of Science ®Google Scholar
• Tsuruta T., Tani K., Hoshika A. Myeloperoxidase gene expression and regulation by myeloid cell growth factors in normal and leukemic cells, Leukemia and Lymphoma, (in press)
   Google Scholar
• Low M. G. Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors. Biochemical Journal 1987; 244: 1–13
   PubMed Web of Science ®Google Scholar
• Kam W., Clauser E., Kim Y. S., Kan Y. W., Rutter W. J. Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proceedings of the National Academy of Sciences of the United States of America 1985; 82: 8715–8719
   PubMed Web of Science ®Google Scholar
• Millan J. L. Molecular cloning and sequence analysis of human placental alkaline phosphatase. Journal of Biological Chemistry 1986; 261: 3112–3115
   PubMed Web of Science ®Google Scholar
• Henthorn P. S., Knoll B. J., Raducha M., Rothblum K. N., Slaughter C., Weiss M., Lafferty M. A., Fischer T., Harris H. Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proceedings of the National Academy of Sciences of the United States of America 1986; 83: 5597–5601
   PubMed Web of Science ®Google Scholar
• Weiss M. J., Henthorn P. S., Lafferty M. A., Slaughter C., Raducha M., Harris H. Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proceedings of the National Academy of Sciences of the United States of America 1986; 83: 7182–7186
   PubMed Web of Science ®Google Scholar
• Berger J., Garattini E., Hua J. C., Udenfriend S. Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proceedings of the National Academy of Sciences of the United States of America 1987; 84: 695–698
   PubMed Web of Science ®Google Scholar
• Henthorn P. S., Raducha M., Edwards Y. H., Weiss M. J., Slaughter C., Lafferty M. A., Harris H. Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proceedings of the National Academy of Sciences of the United States of America 1987; 84: 1234–1238
   PubMed Web of Science ®Google Scholar
• Millan J. L., Manes T. Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proceedings of the National Academy of Sciences of the United States of America 1988; 85: 3024–3028
   PubMed Web of Science ®Google Scholar
• Watanabe S., Watanabe T., Li W. B., Soong B. W., Chou J. Y. Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. Journal of Biological Chemistry 1989; 264: 12611–12619
   PubMed Web of Science ®Google Scholar
• Smith M., Weiss M. J., Griffin C. A., Murray J. C., Buetow K. H., Emanuel B. S., Henthorn P. S., Harris H. Regional assignment of the gene for human liver/bone/kidney alkaline phosphatase to chromosome 1p36.1-p34. Genomics 1988; 2: 139–143
   PubMedGoogle Scholar
• Wachstein M. Alkaline phosphatase activity in normal and abnormal human blood and bone marrow cells. The Journal of Laboratory and Clinical Medicine 1946; 31: 1–17
   PubMed Web of Science ®Google Scholar
• Hayhoe F. G. J., Quaglino D. Cytochemical demonstration and measurement of leucocyte alkaline phosphatase activity in normal and pathological states by a modified azo-dye coupling technique. British Journal of Haematology 1958; 4: 375–389
   PubMed Web of Science ®Google Scholar
• Smith G. P., Harris H., Peters T. J. Studies of the biochemical and immunological properties of human neutrophil alkaline phosphatase with comparison to the established alkaline phosphatase isoenzymes. Clinica Chimica Acta 1984; 142: 221–230
   PubMed Web of Science ®Google Scholar
• Weiss M. J., Ray K., Henthorn P. S., Lamb B., Kadesch T., Harris H. Structure of the human liver/bone/kidney alkaline phosphatase gene. Journal of Biological Chemistry 1988; 263: 12002–12010
   PubMed Web of Science ®Google Scholar
• Henthorn P. S., Raducha M., Kadesch T., Weiss M. J., Harris H. Sequence and characterization of the human intestinal alkaline phosphatase gene. Journal of Biological Chemistry 1988; 263: 12011–12019
   PubMed Web of Science ®Google Scholar
• Stewart C. A. Leucocyte alkaline phosphatase in myeloid maturation. Pathology 1974; 6: 287–293
   PubMed Web of Science ®Google Scholar
• Rosenblum D., Petzold S. J. Granulocyte alkaline phosphatase. Studies of purified enzymes from normal subjects and patients with polycythemia vera. Journal of Clinical Investigation 1973; 52: 1665–1672
   PubMed Web of Science ®Google Scholar
• Rosenblum D., Petzold S. J. Neutrophil alkaline phosphatase: comparison of enzymes from normal subjects and patients with polycythemia vera and chronic myelogenous leukemia. Blood 1975; 45: 335–343
   PubMed Web of Science ®Google Scholar
• Lewis S. M., Dacie J. V. Neutrophil leucocyte) alkaline phosphatase in paroxysmal nocturnal haemoglobinuria. British Journal of Haematology 1965; 11: 549–556
   PubMed Web of Science ®Google Scholar
• Trubowitz S., Feldman D., Benante C., Hunt V. M. The alkaline phosphatase content of the human polymorphonuclear leukocyte in blood and marrow. American Journal of Clinical Pathology 1959; 31: 481–486
   Web of Science ®Google Scholar
• Pedersen B. Functional and biochemical phenotype in relation to cellular age of differentiated neutrophils in chronic myeloid leukaemia. British Journal of Haematology 1982; 51: 339–344
   PubMed Web of Science ®Google Scholar
• Bendix-Hansen K., Kerndrup G. Myeloperoxidase-deficient polymorphonuclear leucocytes. (V): Relation to FAB-classification and neutrophil alkaline phosphatase activity in primary myelodysplastic syndromes. Scandinavian Journal of Haematology 1985; 35: 197–200
   PubMedGoogle Scholar
• Hook E. B., Engel R. R. Leucocyte life-span, leucocyte alkaline phosphatase, and the 21st chromosome. The Lancet 1964; 1: 112
   Web of Science ®Google Scholar
• Galbraith P. R. Studies on the longevity, sequestration and release of the leukocytes in chronic myelogenous leukemia. Canadian Medical Association Journal 1966; 95: 511–521
   PubMed Web of Science ®Google Scholar
• Spiers A., Liew A., Baikie A. G. Neutrophil alkaline phosphatase score in chronic granulocytic leukaemia: effects of splenectomy and antileukaemic drugs. Journal of Clinical Pathology 1975; 28: 517–523
   PubMed Web of Science ®Google Scholar
• Bondue H., Machin D., Stryckmans P. A. The leucocyte alkaline phosphatase activity in mature neutrophils of different ages. Scandinavian Journal of Haematology 1980; 24: 51–56
   PubMedGoogle Scholar
• Pedersen B., Hayhoe F. G. Cellular changes in chronic myeloid leukaemia. British Journal of Haematology 1971; 21: 251–256
   PubMed Web of Science ®Google Scholar
• Pedersen B., Hayhoe F. G. Relation between phagocytic activity and alkaline phosphatase content of neutrophils in chronic myeloid leukaemia. British Journal of Haematology 1971; 21: 257–260
   PubMed Web of Science ®Google Scholar
• Athens J. W., Raab S. O., Haab O. P., Boggs D. R., Ashenbrucker H., Cartwright G. E., Wintrobe M. M. Leukokinetic studies. X. Blood granulocyte kinetics in chronic myelocytic leukemia. Journal of Clinical Investigation 1965; 44: 765–777
   PubMed Web of Science ®Google Scholar
• Galbraith P. R., Abu-Zahra H. T. Granulopoiesis in chronic granulocytic leukaemia. British Journal of Haematology 1972; 22: 135–143
   PubMed Web of Science ®Google Scholar
• Rambaldi A., Terao M., Bettoni S., Bassan R., Battista R., Barbui T., Garattini E. Differences in the expression of alkaline phosphatase mRNA in chronic myelogenous leukemia and paroxysmal nocturnal hemoglobinuria polymorphonuclear leukocytes. Blood 1989; 73: 1113–1115
   PubMed Web of Science ®Google Scholar
• Nicholson-Weller A., March J. P., Rosenfeld S. I., Austen K. F. Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor. Proceedings of the National Academy of Sciences of the United States of America 1983; 80: 5066–5070
   PubMed Web of Science ®Google Scholar
• Chow F. L., Telen M. J., Rosse W. F. The acetylcholinesterase defect in paroxysmal nocturnal hemoglobinuria: evidence that the enzyme is absent from the cell membrane. Blood 1985; 66: 940–945
   PubMed Web of Science ®Google Scholar
• Davitz M. A., Low M. G., Nussenzweig V. Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PIPLC). Selective modification of a complement regulatory protein. Journal of Experimental Medicine 1986; 163: 1150–1161
   PubMed Web of Science ®Google Scholar
• Selvaraj P., Rosse W. F., Silber R., Springer T. A. The major Fc receptor in blood has a phosphatidylinositol anchor and is deficient in paroxysmal nocturnal haemoglobinuria. Nature 1988; 333: 565–567
   PubMed Web of Science ®Google Scholar
• Tsuruta T., Tani K., Shimane M., Ozawa K, Takahashi S., Tsuchimoto D., Takahashi K., Nagata S., Sato N., Asano S. Effects of myeloid cell growth factors on alkaline phosphatase, myeloperoxidase, defensin and granulocyte colony-stimulating factor receptor mRNA expression in haemopoietic cells of normal individuals and myeloid disorders. British Journal of Haematology 1996; 92: 9–22
   PubMed Web of Science ®Google Scholar
• Rambaldi A., Terao M., Bettoni S., Tini M. L., Bassan R., Barbui T., Garattini E. Expression of leukocyte alkaline phosphatase gene in normal and leukemic cells: regulation of the transcript by granulocyte colony-stimulating factor. Blood 1990; 76: 2565–2571
   PubMed Web of Science ®Google Scholar
• Valentine W. N., Beck W. S. Biochemical studies on leucocyte: I. Phosphatase activity in health, leucocytosis, and myelocytic leukemia. Journal of Laboratory & Clinical Medicine 1951; 38: 39–55
   PubMed Web of Science ®Google Scholar
• Valentine W. N., Follette J. H., Hardin E. B., Beck W. S., Lawrence J. S. Studies on leukocyte alkaline phosphatase activity: Relation to “stress” and pituitary-adrenal activity. Journal of Laboratory & Clinical Medicine 1954; 44: 219–228
   PubMed Web of Science ®Google Scholar
• Valentine W. N., Follette J. H., Solomon D. H., Reynolds J. The relationship of leukocyte alkaline phosphatase to “stress,” to ACTH, and to adrenal 17-OH-corticosteroids. Journal of Laboratory & Clinical Medicine 1957; 49: 723–737
   PubMed Web of Science ®Google Scholar
• Kenny J. J., Moloney W. C. Leukocytic alkaline phosphatase: Behavior during prolonged incubation and infection in normal and leukemic leukocytes. Blood 1957; 12: 295–302
   PubMed Web of Science ®Google Scholar
• Rosen R. B., Teplitz R. L. Chronic granulocytic leukemia complicated by ulcerative colitis: Elevated leukocyte alkaline phosphatase and possible modifier gene deletion. Blood 1965; 26: 148–156
   PubMed Web of Science ®Google Scholar
• Perillie P. E. Studies of the changes in leukocyte alkaline phosphatase following pyrogen stimulation in chronic granulocytic leukemia. Blood 1967; 29: 401–406
   PubMed Web of Science ®Google Scholar
• Schiffer C. A., Aisner J., Daly P. A., Wiernik P. H. Increased leukocyte alkaline phosphatase activity following transfusion of leukocytes from a patient with chronic myelogenous leukemia. American Journal of Medicine 1979; 66: 519–522
   PubMed Web of Science ®Google Scholar
• Rustin G. J., Goldman J. M., McCarthy D., Mees S., Peters T. J. An extrinsic factor controls neutrophil alkaline phosphatase synthesis in chronic granulocytic leukaemia. British Journal of Haematology 1980; 45: 381–387
   PubMed Web of Science ®Google Scholar
• Sato N., Asano S., Urabe A., Ohsawa N., Takaku F. Induction of alkaline phosphatase in neutrophilic granulocytes, a marker of cell maturity, from bone marrow of normal individuals by retinoic acid. Biochemical & Biophysical Research Communications 1985; 131: 1181–1186
   PubMed Web of Science ®Google Scholar
• Sato N., Asano S., Ueyama Y., Mori M., Okabe T., Kondo Y., Ohsawa N., Kosaka K. Granulocytosis and colony-stimulating activity (CSA) produced by a human squamous cell carcinoma. Cancer 1979; 43: 605–610
   PubMed Web of Science ®Google Scholar
• Sato N., Asano S., Mori M., Ueyama Y., Sugano K., Ohsawa N., Takaku F. Characterization of neutrophil alkaline phosphatase-inducing factor (NAP-IF). Journal of Cellular Physiology 1985; 124: 255–260
   PubMed Web of Science ®Google Scholar
• Matsuo T. In vitro modulation of alkaline phosphatase activity in neutrophils from patients with chronic myelogenous leukemia by monocyte-derived activity. Blood 1986; 67: 492–497
   PubMed Web of Science ®Google Scholar
• Sato N., Asano S., Koelfler H. P., Yoshida S., Takaku F., Takatani O. Identification of neutrophil alkaline phosphatase-inducing factor in cystic fluid of a human squamous cell carcinoma as granulocyte colony-stimulating factor. Journal of Cellular Physiology 1988; 137: 272–276
   PubMed Web of Science ®Google Scholar
• Sato N., Mori M., Oshimura M., Ueyama Y., Miwa T., Ohsawa N., Kosaka K., Asano S. Factor(s) responsible for the increase in alkaline phosphatase activity of postmitotic granulocytes from normal individuals and patients with chronic myeloid leukemia. Blood 1982; 59: 141–147
   PubMed Web of Science ®Google Scholar
• Yuo A., Kitagawa S., Okabe T., Urabe A., Komatsu Y., Itoh S., Takaku F. Recombinant human granulocyte colony-stimulating factor repairs the abnormalities of neutrophils in patients with myelodysplastic syndromes and chronic myelogenous leukemia. Blood 1987; 70: 404–411
   PubMed Web of Science ®Google Scholar
• Sato N., Takatani O., Koeffler H. P., Sato H., Asano S., Takaku F. Modulation by retinoids and interferons of alkaline phosphatase activity in granulocytes induced by granulocyte colony-stimulating factor. Experimental Hematology 1989; 17: 258–262
   PubMed Web of Science ®Google Scholar
• Teshima T., Shibuya T., Harada M., Akashi K., Taniguchi S., Okamura T., Niho Y. Granulocyte-macrophage colony-stimulating factor suppresses induction of neutrophil alkaline phosphatase synthesis by granulocyte colony-stimulating factor. Experimental Hematology 1990; 18: 316–21
   PubMed Web of Science ®Google Scholar
• Mizukami H., Sato N. Retinoic acid acts to neutralize the inhibitory effect of granulocyte-macrophage colony-stimulating factor (GM-CSF) on alkaline phosphatase activity of neutrophils that is induced by granulocyte colony-stimulating factor (G-CSF). Experimental Hematology 1992; 20: 482–485
   PubMed Web of Science ®Google Scholar
• Sato N., Mizukami H., Tani K., Asano S., Takaku F. Regulation of alkaline phosphatase activity in neutrophilic granulocyte. Acta Haematologica Japonica 1990; 53: 1569–1576
   Web of Science ®Google Scholar
• Sato N., Mizukami H., Tani K., Asano S. Regulation of mRNA levels of alkaline phosphatase gene in neutrophilic granulocytes by granulocyte colony-stimulating factor and retinoic acid. European Journal of Haematology 1991; 46: 107–111
   PubMed Web of Science ®Google Scholar
• Taoka T., Yamaoka G., Arai T., Kiuchi H., Tanaka T., Takahara J., Kawanishi K., Irino S. Alkaline phosphatase activity in the human promyelocytic leukemia cell line, HL-60, induced by retinoic acid and recombinant human granulocyte colony-stimulating factor. Leukemia Research 1993; 17: 695–698
   PubMed Web of Science ®Google Scholar
• Gianni M., Terao M., Zanotta S., Barbui T., Rambaldi A., Garattini E. Retinoic acid and granulocyte colony-stimulating factor synergistically induce leukocyte alkaline phosphatase in acute promyelocytic leukemia cells. Blood 1909; 83, 1921
   Google Scholar
• Steinman R. A., Tweardy D. J. Granulocyte colony-stimulating factor receptor mRNA upregulation is an immediate early marker of myeloid differentiation and exhibits dysfunctional regulation in leukemic cells. Blood 1994; 83: 119–127
   PubMed Web of Science ®Google Scholar
• Tsurumi H., Tojo A., Takahashi T., Moriwaki H., Asano S., Muto Y. The combined effects of all-trans retinoic acid and granulocyte colony-stimulating factor as a differentiation induction therapy for acute promyelocytic leukemia. Internal Medicine 1993; 32: 648–650
   PubMed Web of Science ®Google Scholar
• Imaizumi M., Sato A., Koizumi Y., Inoue S., Suzuki H., Suwabe N., Yoshinari M., Ichinohasama R., Endo K., Sawai T., et al. Potentiated maturation with a high proliferating activity of acute promyelocytic leukemia induced in vitro by granulocyte or granulocyte/macrophage colony-stimulating factors in combination with all-trans retinoic acid. Leukemia 1994; 8: 1301–1308
   PubMed Web of Science ®Google Scholar
• Gianni M., Li Calzi M., Terao M., Rambaldi A., Garattini E. Tyrosine kinases but not cAMP-dependent protein kinase mediate the induction of leukocyte alkaline phosphatase by granulocyte-colony-stimulating factor and retinoic acid in acute promyelocytic leukemia cells. Biochemical & Biophysical Research Communications 1995; 208: 846–854
   PubMed Web of Science ®Google Scholar
• Garattini E., Gianni M. Leukocyte alkaline phosphatase a specific marker for the post-mitotic neutrophilic granulocyte: regulation in acute promyelocytic leukemia. Leukemia & Lymphoma 1996; 23: 493–503
   PubMed Web of Science ®Google Scholar
• Usuki K., Nishizawa Y., Endo M., Osawa M., Kitazume K., Iki S., Watanabe M., Urabe A. Administration of granulocyte colony-stimulating factor during remission induction therapy with all-trans retinoic acid for acute promyelocytic leukemia. International Journal of Hematology 1996; 64: 213–219
   PubMed Web of Science ®Google Scholar
• Selsted M. E., Harwig S. S., Ganz T., Schilling J. W., Lehrer R. I. Primary structures of three human neutrophil defensins. Journal of Clinical Investigation 1985; 76: 1436–1439
   PubMed Web of Science ®Google Scholar
• Selsted M. E., Szklarek D., Lehrer R.I. Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes. Infection & Immunity 1984; 45: 150–154
   PubMed Web of Science ®Google Scholar
• Lehrer R. I., Szklarek D., Ganz T., Selsted M. E. Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity. Infection & Immunity 1985; 49: 207–211
   PubMed Web of Science ®Google Scholar
• Lehrer R. I., Daher K., Ganz T., Selsted M. E. Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes. Journal of Virology 1985; 54: 467–472
   PubMed Web of Science ®Google Scholar
• Lichtenstein A., Ganz T., Selsted M. E., Lehrer R. I. In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes. Blood 1986; 68: 1407–1410
   PubMed Web of Science ®Google Scholar
• Territo M. C., Ganz T., Selsted M. E., Lehrer R. Monocyte-chemotactic activity of defensins from human neutrophils. Journal of Clinical Investigation 1989; 84: 2017–2020
   PubMed Web of Science ®Google Scholar
• Daher K. A., Lehrer R. I., Ganz T., Kronenberg M. Isolation and characterization of human defensin cDNA clones. Proceedings of the National Academy of Sciences of the United States of America 1988; 85: 7327–7331
   PubMed Web of Science ®Google Scholar
• Shiomi K., Nakazato M., Ihi T., Kangawa K, Matsuo H., Matsukura S. Establishment of radioimmunoassay for human neutrophil peptides and their increases in plasma and neutrophil in infection. Biochemical & Biophysical Research Communications 1993; 195: 1336–1344
   PubMed Web of Science ®Google Scholar