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2003 | 08 | 2 |
Tytuł artykułu

Syndecan-4 distribution during the differentiation of satellite cells isolated from soleus muscle treated by phorbol ester and calphostin C

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
It was shown that syndecans have a potential role in muscle development. We focused this study on the role of syndecan-4 distribution and phosphorylation during the differentiation of satellite cells isolated from Soleus muscle. Syndecans are cell surface heparan sulfate proteoglycans (HSPGs) that bind numerous ligands through their HS glycosaminoglycan chains (GAG). They play a role in cell-extracellular matrix and cell-cell adhesion, signal transduction and the targeting of growth factors and other molecules to the cell surface. Syndecan-4 acts as a co-receptor or, along with integrins, is localized to the cell membrane of focal contacts. Syndecan-4 participates in the organization of the structure of focal contacts reacting with extracellular matrix molecules. The interaction of syndecan-4 with protein kinase C (PKC) isoforms is the main mechanism regulating its distribution in cells. Our current study focused on the role of the distribution of syndecan-4, and its interactions with PKC isoforms during the differentiation of activated satellite cells. We used the PKC activator TPA (12-O-tetradecanoyl phorbol 13-acetate) and the PKC inhibitor Calphostin C (Cal C). We concluded that syndecan-4 was important not only in the activation of satellite cells, but also in myoblast differentiation. During our research, we observed the presence of syndecan-4 and changes in its location over the course of that process. We also showed that TPA and Cal C treatment had an influence on the subcellular distribution of syndecan-4, but there was no influence on myoblast differentiation. We speculated that the reason for changes after TPA treatment was the interactions with activated PKCα, which provoked syndecan-4/PKCα complex translocation to integrins. We also supposed that Cal C treatment inhibited PKCδ activity and probably induced PKCα association to syndecan-4, and syndecan-4 translocation to integrins.
Wydawca
-
Rocznik
Tom
08
Numer
2
Opis fizyczny
p.269-278,fig.
Twórcy
autor
  • Warsaw University, Miecznikowa 1, 02-096 Warsaw, Poland
autor
autor
Bibliografia
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  • 7.Fuentealba, L., Carey, D.J. and Brandan, E. Antisense inhibition of syndecan-3 expression during skeletal muscle differentiation accelerates myogenesis through a basic fibroblast growth factor-dependent mechanism. J. Biol. Chem. 274 (1999) 37876-37884.
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  • 12.Carey, D.J. Syndecans: multifunctional cell-surface co-receptors. Bioch. J. 327 (1997) 1-16.
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  • 15.Ron, D. and Kazanietz, M.G. New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J. 13 (1999) 1658- 1672.
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  • 19.Bogi, K., Lorenzo, P.S., Szallasi, Z., Aes, P., Wagner, G.S. and Blumberg, P.M. Differential selectivity of ligands for C1a and C1b phorbol ester binding domains of protein kinase Cδ: possible correlation with tumor-promoting activity. Cancer Res. 58 (1998) 1423-1428.
  • 20.Slater, S.J., Ho, C., Kelly, M.B., Larkin, J.D., Taddeo, F.J., Yeager, M.D. and Stubbs, C.D. Protein kinase Cα contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities. J. Biol. Chem. 271 (1996) 4627-4631.
  • 21.Budworth, J. and Gescher, A. Differential inhibition of cytosolic and membrane-derived protein kinase C activity by staurosporine and other kinase inhibitors. FEBS Lett. 362 (1995) 139-142.
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  • 23.Alterio, J., Courtois, Y., Robelin, J., Bechet, D. and Martelly, I. Acidic and basic fibroblast growth factor mRNAs are expressed by skeletal muscle satellite cells. Biochem. Biophys. Res. Commun. 166 (1990) 1205-1212.
  • 24.Laemli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriphage T4. Nature 227 (1970) 680-685.
  • 25.Couchman, J.R. and Woods, A. Syndecan-4 and integrins: combinatorial signalling in cell adhesion. J. Cell Sci. 112 (1999) 3415-3420.
  • 26.Baciu, P.C. and Goetinck, P.F. Protein kinase C regulates the recuitment of syndecan-4 into focal contacts. Mol. Biol. Cell 6 (1995) 1503-1513.
  • 27.Ssang-Taek, L., Longley, R.L., Couchman, J.R. and Woods, A. Direct binding of syndecan-4 cytoplasmic domain to the catalyctic domain of PKCα increases focal adhesion localization of PKCα. J. Biol. Chem. (2003) in press.
  • 28.Pears, C.J. and Goode, N.T. PKC downregulation: signal or adaptation? in: Protein kinase C, (Parker, J.P., Dekker, L.V.), Springer-Verlag, Heidelberg, 1997, 45-55.
  • 29.Ron, D. and Kazanietz, M.G. New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J. 13 (1999) 1658- 1676.
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  • 31.Rapraeger, A.C. Molecular interactions of syndecans during development. Cell Dev. Biol. 12 (2001) 107-116.
Typ dokumentu
Bibliografia
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Identyfikator YADDA
bwmeta1.element.agro-article-d06a6bd9-6b98-42bc-8685-97ba21dfe879
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