The Role of Biglycan in the Heart

REFERENCES

• Fisher L.W., Termine J.D., Young M.F. Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species. J. Biol. Chem. 1989; 264: 4571–4576
   PubMed Web of Science ®Google Scholar
• Ameye L., Young M.F. Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases. Glycobiology 2002; 12: 107R–116R
   PubMed Web of Science ®Google Scholar
• Ruoslahti E., Yamaguchi Y. Proteoglycans as modulators of growth factor activities. Cell 1991; 64: 867–869
   PubMed Web of Science ®Google Scholar
• Iozzo R.V. Matrix proteoglycans: from molecular design to cellular function. Annu. Rev. Biochem. 1998; 67: 609–652
   PubMed Web of Science ®Google Scholar
• Latif N., Sarathchandra P., Taylor P.M., et al. Localization and pattern of expression of extracellular matrix components in human heart valves. J. Heart Valve Dis. 2005; 14: 542–548
   Google Scholar
• Wight T.N., Kinsella M.G., Qwarnstrom E.E. The role of proteoglycans in cell adhesion, migration and proliferation. Curr. Op. Cell. Biol. 1992; 4: 793–801
   PubMedGoogle Scholar
• Camejo G., Hurt-Camejo E., Wiklund O., et al. Association of apo B lipoproteins with arterial proteoglycans: pathological significance and molecular basis. Atherosclerosis 1998; 139: 205–222
   PubMed Web of Science ®Google Scholar
• Williams K.J. Arterial wall chondroitin sulfate proteoglycans: diverse molecules with distinct roles in lipoprotein retention and atherogenesis. Cur. Opin. Lipidol. 2001; 12: 477–487
   PubMed Web of Science ®Google Scholar
• Dreher K.L., Asundi V., Matzura D., et al. Vascular smooth muscle biglycan represents a highly conserved proteoglycan within the arterial wall. Eur. J. Cell. Biol. 1990; 53: 296–304
   PubMed Web of Science ®Google Scholar
• Riessen R., Isner J.M., Blessing E., et al. Regional differences in the distribution of the proteoglycans biglycan and decorin in the extracellular matrix of atherosclerotic and restenotic human coronary arteries. Am. J. Pathol. 1994; 144: 962–974
   PubMed Web of Science ®Google Scholar
• O’Brien K.D., Olin K.L., Alpers C.E. Comparison of apolipoprotein and proteoglycan deposits in human coronary atherosclerotic plaques: colocalization of biglycan with apolipoproteins. Circulation 1998; 519–527
   PubMed Web of Science ®Google Scholar
• Sambadam T., Baker J.R., Christner J.E., et al. Specificity of the low-density lipoprotein glycosaminoglycan interaction. Arteriosc. Throm. 1991; 11: 561–568
   PubMedGoogle Scholar
• Santiago-Garcia J., Kodama T., Pitas R.E. The class A scavenger receptor binds to proteoglycans and mediates adhesion of macrophages to the extracellular matrix. J. Biol. Chem. 2003; 278: 6942–6946
   PubMed Web of Science ®Google Scholar
• Chang M.Y., Tsoi C., Wight T.N., et al. Lysophosphatidylcholine regulates synthesis of biglycan and the proteoglycan form of macrophage colony stimulating factor. Arterioscler. Thromb. Vasc. Biol. 2003; 23: 809–815
   PubMed Web of Science ®Google Scholar
• Schönherr E., Jarvelainen H.T., Kinsella M.G., et al. Platelet-derived growth factor and transforming growth factor-beta 1 differentially affect the synthesis of biglycan and decorin by monkey arterial smooth muscle cells. Arterioscler. Thromb. 1993; 13: 1026–1036
   PubMedGoogle Scholar
• Lijnen P.J., Petrov V.V., Fagard R.H. Induction of cardiac fibrosis by transforming growth factor-[beta]1. Mol. Gen. Metabol. 2000; 71: 418–435
   PubMed Web of Science ®Google Scholar
• Bereczki E., Gonda S., Csont T., Korpos E., Zvara A., Ferdinandy P., Santha M. Overexpression of biglycan in the heart of transgenic mice: an antibody microarray study. J. Proteome. Res. 2007; 6: 854–61
   PubMed Web of Science ®Google Scholar
• Breuer B., Schmidt G., Kresse H. Non-uniform influence of transforming growth factor-beta on the biosynthesis of different forms of small chondroitin sulphate/dermatan sulphate proteoglycan. Biochem. J. 1990; 269: 551–554
   PubMed Web of Science ®Google Scholar
• Ungefroren H., Krull N.B. Transcriptional regulation of the human biglycan gene. J. Biol. Chem. 1996; 271: 15787–15795
   PubMed Web of Science ®Google Scholar
• Ahmed M.S., Oie E., Vinge L.E. Induction of myocardial biglycan in heart failure in rats–an extracellular matrix component targeted by AT1 receptor antagonism. Cardiovasc. Res. 2003; 60: 557–568
   PubMed Web of Science ®Google Scholar
• Murakami M., Kusachi S., Nakahama M., et al. Expression of the alpha 1 and alpha 2 chains of type IV collagen in the infarct zone of rat myocardial infarction. J. Mol. Cell. Cardiol. 1998; 30: 1191–202
   PubMed Web of Science ®Google Scholar
• Melendez J., Turner C., Avraham H., et al. Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via src kinase is antagonized by paxillin. J. Biol. Chem. 2004; 279: 53516–53523
   PubMed Web of Science ®Google Scholar
• Weis S.M, Zimmermann S.D., Shah M., Covell J.W., Omens J.H., Ross J., Jr, Dalton N, Jones Y, Reed C.C., Iozzo R.V., McCulloch A.D. A role for decorin in the remodeling of myocardial infarction. Matrix Biol. 2005; 24: 313–324
   PubMed Web of Science ®Google Scholar
• Xu T.S., Bianco P., Fisher L.W., et al. Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice. Nat Genet. 1998; 20: 78–82
   PubMed Web of Science ®Google Scholar
• Ferdinandy P., Schulz R. Nitric oxide, superoxide, and peroxynitrite in myocardial ischaemia-reperfusion injury and preconditioning. Br. J. Pharmacol. 2003; 138: 532–543
   PubMed Web of Science ®Google Scholar
• Janssens S., Pokreisz P., Schoonjans L., Pellens M., Vermeersch P., Tjwa M., Jans P., Scherrer-Crosbie M., Picard M. H., Szelid Z., Gillijns H., Van de Werf F., Collen D., Bloch K. D. Cardiomyocyte-specific overexpression of nitric oxide synthase 3 improves left ventricular performance and reduces compensatory hypertrophy after myocardial infarction. Circ. Res. 2004; 94: 1256–1262
   PubMed Web of Science ®Google Scholar
• Yamamoto K., Kusachi S., Ninomiya Y., et al. Increase in the expression of biglycan mRNA expression co-localized closely with that of type I collagen mRNA in the infarct zone after experimentally-induced myocardial infarction in rats. J. Mol. Cell. Card. 1998; 30: 1749–1756
   PubMed Web of Science ®Google Scholar
• Tufvesson E., Westergren-Thorsson G. Tumour necrosis factor-alpha interacts with biglycan and decorin. Febs Lett. 2002; 530: 124–128
   PubMed Web of Science ®Google Scholar
• Hocking A.M., Strugnell R.A., Ramamurthy P., et al. Eukaryotic expression of recombinant biglycan—post-translational processing and the importance of secondary structure for biological activity. J. Biol. Chem. 1996; 271: 19571–19577
   PubMed Web of Science ®Google Scholar
• Schönherr E., Hausser H., Beavan L., et al. Decorin-type I collagen interaction. Presence of separate core proteinbinding domains. J. Biol. Chem. 1995; 270: 8877–83
   PubMed Web of Science ®Google Scholar
• Wiberg C., Klatt A.R., Wagener R., et al. Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan. J. Biol. Chem. 2003; 278: 37698–37704
   PubMed Web of Science ®Google Scholar
• Bowe M.A., Mendis D.B., Fallon J.R. The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle. J. Cell. Biol. 2000; 148: 801–810
   PubMed Web of Science ®Google Scholar
• Schaefer L., Babelova A, Kiss E., et al. The matrix component biglycan is proinflammatory and signals through Toll-like receptors 4 and 2 in macrophages. J. Clin. Invest. 2005; 115: 2223–2233
   PubMed Web of Science ®Google Scholar
• Michels J., Johnson P.W.M., Packham G. Mcl-1. Inter. J. Biochem. Cell Biol. 2005; 37(2)267–271
   PubMed Web of Science ®Google Scholar
• Shimizu-Hirota R., Sasamura H., Kuroda M., et al. Extracellular matrix glycoprotein biglycan enhances vascular smooth muscle cell proliferation and migration. Circ. Res. 2004; 94: 1067–1074
   PubMed Web of Science ®Google Scholar
• Kikuchi A., Tomoyasu H., Kido I., et al. Haemopoietic biglycan produced by brain cells stimulates growth of microglial cells. J. Neuroimmunol. 2000; 106: 78–86
   Google Scholar
• Schaefer L., Beck K.F., Raslik I., et al. Biglycan, a nitric oxide-regulated gene, affects adhesion, growth, and survival of mesangial cells. J. Biol. Chem. 2003; 278: 26227–26237
   Google Scholar
• Weber C.K., Sommer G., Michl P., et al. Biglycan is overexpressed in pancreatic cancer and induces G1-arrest in pancreatic cancer cell lines. Gastroenterology 2001; 121: 657–667
   PubMed Web of Science ®Google Scholar
• Strehler E. E., Zacharias D. A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol.Rev. 2001; 81: 21–50
   PubMed Web of Science ®Google Scholar
• Williams J. C., Armesilla A. L., Mohamed T. M. A., Hagarty C. L., McIntyre F. H., Schomburg S., Zaki A. O., Oceandy D., Cartwright E. J., Buch M. H., Emerson M., Neyses L. The sarcolemmal calcium pump, alpha-1 syntrophin, and neuronal nitric-oxide synthase are parts of a macromolecular protein complex. J.Biol.Chem. 2006; 281: 23341–23348
   PubMed Web of Science ®Google Scholar
• Geppert M., Goda Y., Hammer R.E., Li C., Rosahl T.W., Stevens C.F., Sudhof T.C. Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse. Cell 1994; 79: 717–727
   PubMed Web of Science ®Google Scholar