PDF herunterladen
Thromb Haemost 2001; 85(05): 793-799
DOI: 10.1055/s-0037-1615720
Review Article
Schattauer GmbH

Plasma Levels of Syndecan-4 (Ryudocan) Are Elevated in Patients with Acute Myocardial Infarction

Tetsuhito Kojima
1   Department of Medical Technology, Nagoya University School of Health Sciences
2   First Department of Internal Medicine, Nagoya University School of Medicine, Nagoya
,
Akira Takagi
1   Department of Medical Technology, Nagoya University School of Health Sciences
,
Masahiro Maeda
3   Immuno-Biological Laboratories, Co. Ltd., Fujioka
,
Tatsuya Segawa
3   Immuno-Biological Laboratories, Co. Ltd., Fujioka
,
Atsuya Shimizu
2   First Department of Internal Medicine, Nagoya University School of Medicine, Nagoya
,
Koji Yamamoto
2   First Department of Internal Medicine, Nagoya University School of Medicine, Nagoya
,
Tadashi Matsushita
2   First Department of Internal Medicine, Nagoya University School of Medicine, Nagoya
,
Hidehiko Saito
2   First Department of Internal Medicine, Nagoya University School of Medicine, Nagoya
4   Aichi Juridical Foundation for Blood Disease Research, Nagoya, Japan
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Received 06. Juni 2000

Accepted after resubmission 02. Januar 2001

Publikationsdatum:
11. Dezember 2017 (online)

Auch verfügbar auf
    Lizenzen und Reprints

Summary

Syndecan-4 (ryudocan) is a cell-surface heparan sulfate proteoglycan, which plays an important role in a variety of biological functions including regulation of blood coagulation, cell adhesion, and cell growth. In this study, we measured plasma levels of syndecan-4 in patients with acute myocardial infarction using an enzyme-immunoassay, and found that they were extremely high, with a peak of average (10.5 ± 5.6 ng/ml, 2 weeks after onset), as compared with those in normal subjects (0.078 ± 0.030 ng/ml) (p < 0.001). We also observed a distinct expression of syndecan-4 in the repair region of the damaged cardiac tissues with infarction, but not in intact region, by immunohistochemical analysis. To clarify the mechanism of syndecan-4 induction, we investigated the hypoxia effect on its expression, and found that hypoxia treatment up-regulated the gene expression of syndecan-4 in various types of cells. Taken together, it is suggested that syndecan-4 is induced by hypoxia stimuli in ischemic heart tissues, and may function as a tissue-repair molecule via biological mediators such as heparin-binding growth factors.

Keywords

Syndecan-4 (ryudocan) - enzyme-linked immuno-sorbent assay (ELISA) - acute myocardial infarction - hypoxia - tissue repair
 

  • References

  • 1 Kojima T, Leone CW, Marchildon GA, Marcum JA, Rosenberg RD. Isolation and characterization of heparan sulfate proteoglycans produced by cloned rat microvascular endothelial cells. J Biol Chem 1992; 267: 4859-69.
    PubMedGoogle Scholar
  • 2 Kojima T, Shworak NS, Rosenberg RD. Molecular cloning and expression of two distinct cDNA encoding heparan sulfate proteoglycan core proteins from a rat endothelial cell line. J Biol Chem 1992; 267: 4870-7.
    PubMedGoogle Scholar
  • 3 Bernfield M, Kokenyesi R, Kato M, Hinkes M, Spring J, Gallo RL, Lose EJ. Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans. Annu Rev Cell Biol 1992; 8: 365-93.
    CrossrefPubMedGoogle Scholar
  • 4 Carey DJ. Syndecans: multifunctional cell-surface co-receptors. Biochem J 1997; 327: 1-16.
    CrossrefPubMedGoogle Scholar
  • 5 Woods A, Couchman JR. Syndecan 4 Heparan Sulfate Proteoglycan Is a Selectively enriched and widespread focal adhesion component. Mol Biol Cell 1994; 5: 183-92.
    CrossrefPubMedGoogle Scholar
  • 6 Baciu PC, Goetinck PF. Protein kinase C regulates the recruitment of syndecan-4 into focal contacts. Mol Biol Cell 1995; 6: 1503-13.
    CrossrefPubMedGoogle Scholar
  • 7 Ishiguro K, Kadomatsu K, Kojima T, Muramatsu H, Tsuzuki S, Nakamura E, Kusugami K, Saito H, Muramatsu T. Syndecan-4 deficiency impairs focal adhesion formation only under restricted conditions. J Biol Chem 2000; 275: 5249-52.
    CrossrefPubMedGoogle Scholar
  • 8 Kim CW, Goldberger OA, Gallo RI, 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.
    CrossrefPubMedGoogle Scholar
  • 9 Kojima T, Katsumi A, Yamazaki T, Muramatsu T, Nagasaka K, Ohsumi K, Saito H. Human ryudocan from endothelium-like cells binds basic fibroblast growth factor, midkine, and tissue factor pathway inhibitor. J Biol Chem 1996; 271: 5914-20.
    CrossrefPubMedGoogle Scholar
  • 10 Shworak NW, Shirakawa M, Mulligan RC, Rosenberg RD. Characterization of ryudocan glycosaminoglycan acceptor sites. J Biol Chem 1994; 269: 21204-14.
    PubMedGoogle Scholar
  • 11 Horowitz A, Simons M. Phosphorylation of the cytoplasmic tail of syndecan-4 regulates activation of protein kinase Ca. J Biol Chem 1998; 273: 10914-8.
    CrossrefPubMedGoogle Scholar
  • 12 Oh E-S, Woods A, Couchman JR. Mulimerization of the cytoplasmic domain of syndecan-4 Is required for its ability to activate protein kinase C. J Biol Chem 1997; 272: 11805-11.
    CrossrefPubMedGoogle Scholar
  • 13 Oh E-S, Woods A, Lim S-T, Theibert AW, Couchman JR. Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinattely regulate protein kinase C activity. J Biol Chem 1998; 273: 10624-9.
    CrossrefPubMedGoogle Scholar
  • 14 Gallo RL, Ono M, Povsic T, Page C, Eriksson E, Klagsbrun M, Bernfield M. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a prorine-rich antimicrobial peptide from wounds. Proc Natl Acad Sci USA 1994; 91: 11035-9.
    CrossrefPubMedGoogle Scholar
  • 15 Cizmeci-Smith G, Eugene L, Youkey J, Showalter LJ, Carey DJ. Syndecan-4 is a primary-response gene induced by basic fibroblast growth factor and arterial injury in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 1997; 17: 172-80.
    CrossrefPubMedGoogle Scholar
  • 16 Li J, Brown LF, Laham RJ, Volk R, Simons M. Macrophage-dependent regulation of syndecan gene expression. Circ Res 1997; 81: 785-96.
    CrossrefPubMedGoogle Scholar
  • 17 Shweiki D, Itin A, Soffer D, Keshet E. Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis. Nature 1992; 359: 843-5.
    CrossrefPubMedGoogle Scholar
  • 18 Plate KH, Breier G, Weich HA, Risau W. Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo. Nature 1992; 359: 845-8.
    CrossrefPubMedGoogle Scholar
  • 19 Levy AP, Levy NS, Wegner S, Goldberg MA. Transcriptional regulation of the rat vascular endothelial growth factor gene by hypoxia. J Biol Chem 1995; 270: 13333-40.
    CrossrefPubMedGoogle Scholar
  • 20 Levy AP, Levy NS, Goldberg MA. Post-transcriptional regulation of vascular endothelial growth factor by hypoxia. J Biol Chem 1996; 271: 2746-53.
    CrossrefPubMedGoogle Scholar
  • 21 Matsushita T, Kojima T, Emi N, Takahashi I, Saito H.. Impaired Human Tissue Factor-mediated Activity in Blood Clotting factor VII Nagoya (Arg304Trp); Evidence that a region in the catalytic domain of factor VII is important for the association with tissue factor. J Biol Chem 1994; 269: 7355-63.
    PubMedGoogle Scholar
  • 22 Kojima T, Inazawa J, Takamatsu J, Rosenberg RD, and Saito H. Human ryudocan core protein: molecular cloning and characterization of the cDNA, and chromosomal localization of the gene. Biochem Biophys Res Commun 1993; 190: 814-22.
    CrossrefPubMedGoogle Scholar
  • 23 Kon S, Maeda M, Segawa T, Hagiwara Y, Horikoshi Y, Chikuma S, Tanaka K, Rashid MM, Inobe M, Chambers AF, Uede T. Antibodies to different peptides in osteopontin reveal complexities in the various secreted forms. J Cell Biochem 2000; 77: 487-98.
    CrossrefPubMedGoogle Scholar
  • 24 Shworak NW, Fritze LMS, Liu J, Butler LD, Rosenberg RD. Cell-free synthesis of anticoagulant heparan sulfate reveals a limiting converting activity that modifies an excess precursor pool. J Biol Chem 1996; 271: 27063-71.
    CrossrefPubMedGoogle Scholar
  • 25 Claycomb WC, Lanson Jr NA, Stallworth BS, Egeland DB, Delcarpio JB, Bahinski A, Izzo Jr NJ. HL-1 cells: A cardiac muscle cell line that contracts and retains phenotypic characteristics of the adult cardiomyocyte. Proc Natl Acad Sci USA 1998; 95: 2979-84.
    CrossrefPubMedGoogle Scholar
  • 26 Tsuzuki S, Kojima T, Katsumi A, Yamazaki T, Sugiura I, Saito H. Molecular cloning, genomic organization, promoter activity, and tissue-specific expression of the mouse ryudocan gene. J Biochem 1997; 122: 17-24.
    CrossrefPubMedGoogle Scholar
  • 27 Saunders S, Jalkanen M, O’Farrell S, and Bernfield M. Molecular cloning of syndecan, an integral membrane proteoglycan. J Cell Biol 1989; 108: 1547-56.
    CrossrefPubMedGoogle Scholar
  • 28 David G, Bai XM, Van der Schueren B, Marynen P, Cassiman JJ, Van den Berghe H. Spatial and temporal changes in the expression of fibroglycan (syndecan-2) during mouse embryonic development. Development 1993; 119: 841-54.
    PubMedGoogle Scholar
  • 29 Shima DT, Kuroki M, Deutsch U, Ng YS, Adamis AP, D’Amore PA. The mouse gene for vascular endothelial growth factor. Genomic structure, definition of the transcriptional unit, and characterization of transcriptional and post-transcriptional regulatory sequences. J Biol Chem 1996; 271: 3877-83.
    CrossrefPubMedGoogle Scholar
  • 30 Tokunaga K, Taniguchi H, Yoda K, Shimizu M, Sakiyama S. Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-actin mRNA. Nucleic Acids Res 1986; 14: 2829.
    CrossrefPubMedGoogle Scholar
  • 31 Toyozumi H, Kojima K, Matsushita T, Hamaguchi M, Tanimoto M, Saito H. Diagnosis of hemophilia B carriers using two novel dinucleotide polymorphisms and Hha I RFLP of the factor IX gene in Japanese subjects. Thromb Haemost 1995; 74: 1009-14.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 32 Volk R, Schwartz JJ, Li J, Rosenberg RD, Simons M. The role of syndecan cytoplasmic domain in basic fibroblast growth factor-dependent signal transduction. J Biol Chem 1999; 274: 24417-24.
    CrossrefPubMedGoogle Scholar
  • 33 Subramanian SV, Fitzgerald ML, Bernfield M. Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor Activation. J Biol Chem 1997; 272: 14713-20.
    CrossrefPubMedGoogle Scholar
  • 34 Walgenbach KJ, Gratas C, Shestak KC, Becker D. Ischaemia-induced expression of FGF in normal skeletal muscle: a potential paracrine mechanism for mediating angiogenesis in ischaemic skeletal muscle. Nat Med 1995; 1: 453-9.
    CrossrefPubMedGoogle Scholar
  • 35 Obama H, Biro S, Tashiro T, Tsutsui J, Ozawa M, Yoshida H, Tanaka H, Muramatsu T. Myocardial infarction induces expression of midkine, a heparin-binding growth factor with reparative activity. Anticancer Res 1998; 18: 145-52.
    PubMedGoogle Scholar
  • 36 Banai S, Shweiki D, Pinson A, Chandra M, Lazarovici G, Keshet E. Upregulation of vascular endothelial growth factor expression induced by myocardial ischaemia: implications for coronary angiogenesis. Cardiovasc Res 1994; 28: 1176-9.
    CrossrefPubMedGoogle Scholar
  • 37 Zhang Y, Pasparakis M, Kollias G, Simons M. Myocyte-dependent regulation of endothelial cell syndecan-4 expression. J Biol Chem 1999; 274: 14786-90.
    CrossrefPubMedGoogle Scholar
  • 38 Ishiguro K, Kojima T, Taguchi O, Saito H, Muramatsu T, Kadomatsu K. Syndecan-4 expression is associated with follicular atresia in mouse ovary. Histochem Cell Biol 1999; 112: 25-33.
    CrossrefPubMedGoogle Scholar