Macrophage-dependent regulation of syndecan gene expression

Circulation Research

Volumn 81, Issue 5, 1997, Pages 785-796

  Li, Jian ^a   Brown, Lawrence F ^a   Laham, Roger J ^a   Volk, Rudiger ^a   Simons, Michael ^a,b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

Author keywords

Angiogenesis; Extracellular matrix; Heparan sulfate; Macrophage; Syndecan

Indexed keywords

SYNDECAN;

ANGIOGENESIS; ANIMAL MODEL; ARTICLE; EXTRACELLULAR MATRIX; GENE EXPRESSION; HEART INFARCTION; MACROPHAGE; MOUSE; NONHUMAN; PRIORITY JOURNAL; RAT; WOUND HEALING;

EID: 0030670074     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.81.5.785     Document Type: Article

References (49)

1. Bernfield M, Kokenyesi R, Kato M, Hinkes MT, Spring J, Gallo RL, Lose EJ. Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans. Annu Rev Cell Biol. 1992;8:365-393.
2. Jalkanen M, Elenius K, Salmivitra M. Syndecan - a cell surface proteoglycan that selectively binds extracellular effector molecules. In: Lane DA, ed. Heparin and Related Polysaccharides. New York, NY: Plenum Publishing Corp; 1992:79-85.
3. Rosenbere RD, Slworak NW, Liu J, Schwartz JJ, Zhang L. Heparan sulfate proteoglycans of the cardiovascular system. J Clin Invest. 1997;99:2062-2070.
4. Shworak NW, Kojima T, Rosenberg RD. Isolation and characterization of ryudocan and syndecan heparan sulfate proteoglycans. core proteins, and cDNAs from a rat entlothetial eell line. Haemostasis. 1993;23(suppl 1):161-176.
5. Nikkari ST, Jarvelainen HT, Wight TN, Ferguson M, Clowes AW. Smooth muscle cell expression of extracellular matrix genes after arterial injury. Am J Pathol. 1994;144:1348-1356.
6. Elenius K, Vainio S, Laato M, Salmivitra M, Thesleff I, Jalkanen M. Induced expression of syndecan in healing wounds. J Cell Biol. 1991;114:585-595.
7. Basson CT, Kocher O, Basson MD, Asis A, Madri JA. Differential modulation of vascular cell integrin and extracellular matrix expression in vitro by TGF-beta 1 correlates with reciprocal effects on cell migration. J Cell Physiol. 1992;153:118-128.
8. Edwards IJ, Wagner WD, Owens RT. Macrophage secretory products selectively stimulate dermatan sulfate proteoglycan production in cultured arterial smooth muscle cells. Am J Pathol. 1990;136: 609-621.
9. Gallo RL, Ono M, Povsic T, Pape C, Eriksson E, Klagsbrun M, Bernfield M. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc Natl Acad Sci U S A. 1994;91:11035-11039.
10. Li J, Brown LF, Hibberd MG, Grossman JD, Morgan JP, Simons M. VEGF, flk-1, and flt-1 expression in a rat myocardial infarction model of angiogenesis. Am J Physiol. 1996;270:H1803-H1811.
11. Litwin SE, Katz SE, Morgan JP, Douglas PS. Serial echocardiographic assessment of left ventricular geometry and function after large myocardial infarction in the rat. Circulation. 1994;89:345-354.
12. Harada K, Friedman M, Lopez JJ, Wang SY, Li J, Prasad PV, Pearlman JD, Edelnian ER, Sellke FW, Simons M. Vascular endothelial growth factor administration in chronic myocardial ischemia. Am J Physiol. 1996:270(pt 2):H1791-H1802.
13. Wiktor-Jedrzejczak W, Urbanowska E, Szperl M. Granulocytemacrophage colony-stimulating factor corrects macrophage deficiencies, but not osteopetrosis, in the colony-stimulating factor-1-deficient op/op mouse. Endocrinology. 1994;134:1932-1935.
14. Agerberth B, Lee JY, Bergman T, et al. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur J Biochem. 1991;202:849-854.
15. Storici P, Zanetti M. A cDNA derived from pig bone marrow cells predicts a sequence identical to the intestinal antibacterial peptide PR-39. Biochem Biophys Res Commun. 1993;196:1058-1065.
16. Simons M, Morgan KG, Parker C, Collins E, Rosenberg RD. The prolo-oncogenc c-myb mediates an intracellular calcium rise during the late G1 phase of the cell cycle. J Biol Chem. 1993;268:627-632.
17. Shworak NW, Shirakawa M, Mulligan RC, Rosenberg RD. Characterization of ryudocan glycosaminoglycan acceptor sites. J Biol Chem. 1994;269:21204-21214.
18. Witmer-Pack MD, Hughes DA, Schuler G, et al. Identification of macrophages and dendritic cells in the osteopetrotic (op/op) mouse. J Cell Sci. 1993;104:1021-1029.
19. Saunders S, Jalkanen M, O'Farrell S, Bernfield M. Molecular cloning of syndecan, an integral membrane proteoglycan. J Cell Biol. 1989;108:1547-1556.
20. Cizmeci-Smith G, Asundi V, Stahl RC, et al. Regulated expression of syndecan in vascular smooth muscle cells and cloning of rat syndecan core protein cDNA. J Biol Chem. 1992;267:15729-15736.
21. Cizmeci-Smith G, Stahl RC, Showalter LJ, Carey DJ. Differential expression of transmembrane proteoglycans in vascular smooth muscle cells. J Biol Chem. 1993;268:18740-18747.
22. Kato M, Wang H, Bernfield M, Gallagher JT, Turnbull JE. Cell surface syndecan-1 on distinct cell types differs in fine structure and ligand binding of its heparan sulfate chains. J Biol Chem. 1994;269: 18881-18890.
23. David G. Structure and functional diversity of the heparan sulfate proteoglycans. In: Lane DA, ed. Heparin and Related Polysaccharides. New York, NY: Plenum Publishing Corp; 1992:69-78.
24. Kim CW, Goldberger OA, Gallo RL, Bernfield M. Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns. Mol Biol Cell. 1994;5:797-805.
25. Carey DJ, Evans DM, Stahl RC, et al. Molecular cloning and characterization of N-syndecan, a novel transmembrane heparan sulfate proteoglycan. J Cell Biol. 1992;117:191-201.
26. Elenius K, Salmivirta M, Inki P, Mali M, Jalkanen M. Binding of human syndecan to extracellular matrix proteins. J Biol Chem. 1990;265:17837-17843.
27. Mali M, Elenius K, Miettinen HM, Jalkanen M. Inhibition of basic fibroblast growth factor-induced growth promotion by overexpression of syndecan-1. J Biol Chem. 1993;268:24215-24222.
28. Sanderson RD, Turnbull JE, Gallagher JT, Lander AD. Fine structure of heparan sulfate regulates syndecan-1 function and cell behavior. J Biol Chem. 1994;269:13100-13106.
29. Ruoslahti E, Yamaguchi Y. Proteoglycans as modulators of growth factor activities. Cell. 1991;64:867-869.
30. Yayon A, Klagsbrun M, Esko JD, Leder P, Ornitz DM. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell. 1991;64: 841-848.
31. Vainio S, Jalkanen M, Vaahtokari A, et al. Expression of syndecan gene is induced early, is transient, and correlates with changes in mesenchymal cell proliferation during tooth organogenesis. Dev Biol., 1991;147:322-333.
32. Brown LF, Dubin D, Lavigne L, Logan B, Dvorak HF, Van deWater L. Macrophages and fibroblasts express embryonic fibronectins during cutaneous wound healing. Am J Pathol. 1943;142:793-801.
33. DiPietro LA, Nissen NN, Gamelli RL, Koch AE, Pyle JM, Polverini PJ. Thrombospondin 1 synthesis and function in wound repair. Am J Pathol. 1996;148:1851-1860.
34. Yeaman C, Rapraeger AC. Post-transcriptional regulation of syndecan-1 expression by cAMP in peritoneal macrophages. J Cell Biol. 1993;122:941-950.
35. Yeaman C, Rapraeger AC. Membrane-anchored proteoglycans of mouse macrophages: P388D1 cells express a syndecan-4-like heparan sulfate protcoglycan and a distinct chondroitin sulfate form. J Cell Physiol. 1993;157:413-425.
36. Uhlin-Hansen L, Eskeland T, Kolset SO. Modulation of expression of chondroitin sulfate proteoglycan in stimulated human macrophages. J Biol chem. 1989;264:14916-14922.
37. Laskin JD, Dokidis A, Gardner CR, Laskin DL. Changes in sulfated proteoglycan production after activation of rat liver macrophages. Hepatology. 1991;14:306-312.
38. Edwards IJ, Xu H, Obunike JC, Goldherg IJ, Wagner WD. Differentiated macrophages synthesize a heparan sulfate protcoglycan and an oversulfated chondroitin sulfate proteoglycan that bind lipoprotein lipase. Arterioscler Thromb Vasc Biol. 1995;15:400-409.
39. Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor, Proc Natl Acad Sci U S A. 1987;84:5449-5453.
40. Holak TA, Engstrom A, Kraulis PJ, et al. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry. 1988;27:7620-7629.
41. Selsted ME, Tang YQ, Morris WL, et al. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J Biol Chem. 1993;268:6641-6648.
42. Gudmundsson GH, Magnusson KP, Chowdhary BP, Johansson M, Andersson L, Boman HG. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39, Proc Natl Acad Sci U S A. 1995;92:7085-7089.
43. Shi J, Ross CR, Chengappa MM, Blecha F. Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine. J Leukoc Biol. 1994;56:807-811.
44. Lee SH, Starkey PM, Gordon S. Quantitative analysis of total macrophage content in adult mouse tissues: immunochemical studies with monoclonal antibody F4/80. J Exp Med. 1985;161: 475-489.
45. Cross M, Mangelsdorf I, Wedel A, Renkawitz R. Mouse lysozyme M gene: isolation, characterization, and expression studies. Proc Natl Acad Sci U S A. 1988;85:6232-6236.
46. Gordon S, Clarke S, Greaves D, Doyle A. Molecular immunobiology of macrophages: recent progress. Curr Opin Immunol. 1995;7:24-33.
47. Lieschke GJ, Grail D, Hodgson G, et al. Mice lacking granulocyte colony-stimulating factor have chronic neutropenia, granulocyte and macrophage progenitor cell deficiency, and impaired neutrophil mobilization. Blood. 1994;84:1737-1746.
48. Pungercar J, Strukelj B, Kopitar G, et al. Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow. FEBS Lett. 1993;336:284-288.
49. Storici P, Scocchi M, Tossi A, Gennaro R, Zanetti M. Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA. FEBS Lett. 1994;337:303-307.