N-Terminal Sequence of a Core Protein from a Biglycan Isolated from Bovine Aorta

References

• Berenson G. S., Radhakrishnamurthy B., Dalferes E. R., Jr., Srinivasan S. R. Carbohydrate macromolecules and atherosclerosis. Hum. Pathol. 1971; 2: 57–59
   PubMed Web of Science ®Google Scholar
• Wight T. N. Progress in Hemostasis and Thrombosis. Vessel Proteoglycans and Thrombosis. T. H. Spaet, Grune and Stratton, New York 1980; Vol. 5: 1–39
   Google Scholar
• Camejo G. Interaction of lipids, lipoproteins with intercellular matrix of arterial tissues: Its possible role in atherogenesis. Adv. Lipid Res. 1982; 19: 1–53
   PubMedGoogle Scholar
• Berenson G. S., Radhakrishnamurthy B., Srinivasan S. R., Vijayagopal P., Dalferes E. R., Jr., Sharma C. Recent advances in molecular pathology: Carbohydrates-protein macro-molecules and arterial wall integrity—A role in atherogenesis. Exp. Mol. Pathol. 1984; 41: 267–287
   PubMed Web of Science ®Google Scholar
• Wagner W. D. Proteoglycan structure and function as related to atherosclerosis. Ann. N.Y. Acad. Sci. 1985; 454: 52–68
   PubMed Web of Science ®Google Scholar
• Ruoslahti E. Proteoglycans in cell regulation. J. Biol. Chem. 1989; 264: 13369–13372
   PubMed Web of Science ®Google Scholar
• Sage E. H., Bornstein P. Extracellular proteins that modulate cell-matrix interactions. SPARC, tenasein and thrombospondin. J. Biol. Chem. 1991; 266: 14831–14834
   PubMed Web of Science ®Google Scholar
• Ehrlich K., Radhakrishnamurthy B., Berenson G. S. Isolation of a chondroitin sulfate-dermatan sulfate proteoglycan from bovine aorta. Arch. Biochem. Biophys. 1975; 171: 361–369
   PubMed Web of Science ®Google Scholar
• Vijayagopal R., Srinivasan S. R., Radhakrishnamurthy B., Berenson G. S. Hemostatic properties and serum lipoprotein binding of a heparan sulfate proteoglycan from bovine aorta. Biochem. Biophys. Acta 1983; 758: 70–83
   PubMed Web of Science ®Google Scholar
• Oegema T. R., Jr., Hascall V. C., Eisenstein R. Characterization of bovine aorta proteoglycan extracted with guanidine hydrochloride in the presence of protease inhibitors. J. Biol. Chem. 1979; 254: 1312–1318
   PubMed Web of Science ®Google Scholar
• McMurtrey J., Radhakrishnamurthy B., Dalferes E. R., Jr., Berenson G. S., Gregory J. R. Isolation of proteoglycanhyaluronate complexes from bovine aorta. J. Biol. Chem. 1979; 254: 1621–1626
   PubMed Web of Science ®Google Scholar
• Vijayagopal P., Radhakrishnamurthy B., Srinivasan S. R., Berenson G. S. Isolation and characterization of a link protein from bovine aorta. Proteoglycan aggregate. Biochem. Biophys. Acta 1985; 839: 110–118
   PubMed Web of Science ®Google Scholar
• Vogel K. G., Heinegard D. Characterization of proteoglycans from adult bovine tendon. J. Biol. Chem. 1985; 260: 9298–9306
   PubMed Web of Science ®Google Scholar
• Pearson C. H., Winterbottom N., Fachse D. S., Scott P. P. The NH2-terminal amino acid sequence of bovine skin proteoglycan sulfate. J. Biol. Chem. 1983; 258: 15101–15104
   PubMedGoogle Scholar
• Chang Y., Yanagishita M., Hascall V. C., Wight T. N. Proteoglycans synthesis by smooth muscle cells derived from monkey (Macaca nemestrina) aorta. J. Biol. Chem. 1983; 258: 5679–5688
   PubMed Web of Science ®Google Scholar
• Kinsella M. G., Wight T. N. Isolation and characterization of dermatan sulfate proteoglycans synthesized by bovine aortic endothelial cells. J. Biol. Chem. 1988; 263: 19222–19231
   PubMed Web of Science ®Google Scholar
• Marcum J. A., Thompson M. A. The amino-terminal region of a proteochondroitin core protein secreted by aortic smooth muscle cells share sequence homology with the prepeptide region of the biglycan core protein from human bone. Biochem. Biophys. Res. Commun. 1991; 175: 706–712
   PubMed Web of Science ®Google Scholar
• Neame R. J., Choi H. U., Rosenberg L. C. The primary structure of the core protein of the small leucine-rich proteoglycan (PGI) from bovine articular cartilage. J. Biol. Chem. 1989; 264: 8653–8661
   PubMed Web of Science ®Google Scholar
• Stöcker G., Meyer H. E., Wagener C., Greiling H. Purification and N-terminal amino acid sequence of a chondroitin sulphate/dermatan sulphate proteoglycan isolated from intima/media preparation of human aorta. Biochem. J. 1991; 274: 415–420
   PubMed Web of Science ®Google Scholar
• Heinegard D., Björne-Persson A., Cöster L., Franzen A., Gardell S., Malström A., Paulsson M., Sandfalk R., Vogel K. The core proteins of large and small interstitial proteoglycans from various connective tissues form distinct subgroups. Biochem. J. 1985; 230: 181–194
   PubMed Web of Science ®Google Scholar
• Fisher L. W., Hawkins G. R., Tuross N., Termine J. D. Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from mineral compartment of developing human bone. J. Biol. Chem. 1987; 262: 9702–9708
   PubMed Web of Science ®Google Scholar
• 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 non-connective tissue proteins in variety species. J. Biol. Chem. 1989; 264: 4571–4576
   PubMed Web of Science ®Google Scholar
• Dreher K. L., Asundi V., Matzura D., Cowan K. Vascular smooth muscle biglycan represents a high conserved proteoglycan within the arterial wall. Eur. J. Cell. Biol. 1990; 53: 296–304
   PubMed Web of Science ®Google Scholar
• Radhakrishnamurthy B., Jeansonne N., Berenson G. S. Organization of glycosaminoglycan chains in a chondroitin sulfate-dermatan sulfate proteoglycan from bovine aorta. Biochim. Biophys. Acta 1986; 882: 85–96
   PubMed Web of Science ®Google Scholar
• Iwata M., Carlson S. S. A large chondroitin sulfate basement membrane associated proteoglycan exists as disulfide-stabilized complex of several proteins. J. Biol. Chem. 1991; 266: 323–333
   PubMed Web of Science ®Google Scholar
• Blumenkrantz N., Asboe-Hansen G. New method for quantitative determination of uronic acid. Anal. Biochem. 1973; 54: 484–489
   PubMed Web of Science ®Google Scholar
• Rosenberg L. C., Choi H. U., Tang L-H., Johnson T. L., Pal S., Webber C., Reiner A., Pool A. R. Isolation of dermatan sulfate proteoglycans from mature bovine articular cartilages. J. Biol. Chem. 1985; 260: 6304–6313
   PubMed Web of Science ®Google Scholar
• Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987; 166: 368–379
   PubMed Web of Science ®Google Scholar
• Hunkapiller M. W., Ostrander E. L. F., Hord L. E. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Meth. Enzymol. 1983; 91: 227–236
   PubMed Web of Science ®Google Scholar
• Moos M., Jr., Nguyen N. Y., Liu T. Y. Reproducible high yield sequencing of proteins electrophoretically separated and transferred to an inert support. J. Biol. Chem. 1988; 263: 6005–6008
   PubMed Web of Science ®Google Scholar
• Kyhse-Anderson J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. Biochem. Biophys. Method 1984; 10: 203–209
   PubMedGoogle Scholar
• Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 1987; 262: 10035–10038
   PubMed Web of Science ®Google Scholar
• Reig J. A., Klein D. C. Submicrogram quantities of unstained proteins are visualized on polyvinylidene difluoride membrane by transillumination. Appl. Theoret. Electrophoresis 1988; 1: 59–60
   PubMedGoogle Scholar
• Coull J. M., Pappin D. J. C. A rapid fluorescent staining procedure for proteins electroblotted onto PVDF membrane. J. Protein Chem. 1990; 9: 259–260
   Google Scholar
• Radhakrishnamurthy B., Jeansonne N., Tracy R. E., Berenson G. S. A monoclonal antibody that recognizes hyaluronic acid binding region of aorta proteoglycans. Atherosclerosis 1993; 98: 179–192
   PubMed Web of Science ®Google Scholar
• Blake M. S., Johnston K. H., Russell-Jones G. J., Gotschlich E. C. A rapid sensitive method for detection of alkaline phosphatase conjugated antibody on western blots. Anal. Biochem. 1984; 136: 175–179
   PubMed Web of Science ®Google Scholar
• Simpson R. J., Moritz R. L., Begg G. S., Rubira M. R., Nice E. C. Micropreparative procedures for high sensitivity sequencing of peptides and proteins. Anal. Biochem. 1989; 177: 221–236
   PubMed Web of Science ®Google Scholar
• Moore S., Stein W. H. Determination of amino acids. Methods in Enzymology 1963; 6: 819
   Web of Science ®Google Scholar
• Nakazawa M., Manabe K. The direct hydrolysis of proteins containing tryptophan on polyvinylidene difluoride membrane by mercaptoethane-sulfonic acid in the vapor phase. Anal. Biochem. 1992; 206: 105–108
   PubMed Web of Science ®Google Scholar
• Brown R. E., Jarvis K. L., Hyland K. J. Protein measurement using bicinchoninic acid elimination of interfering substances. Anal. Biochem. 1989; 180: 136–139
   PubMed Web of Science ®Google Scholar
• Lee G. J-L., Tieckelmann H. High performance liquid chromatographic determinations of disaccharides resulting from enzymatic degradation of isomeric chondroitin sulfates. Anal. Biochem. 1979; 94: 231–236
   PubMed Web of Science ®Google Scholar
• Register T., Wagner W. D., Robbins R. A., Lively M. O. Structural properties of and partial protein sequence analysis of the major dermatan sulfate proteoglycan of pigeon aorta. Atherosclerosis 1993; 98: 99–111
   PubMed Web of Science ®Google Scholar
• Torok M. A., Evans S. A. S., Marcum J. A. cDNA sequence for bovine biglycan (PGI) protein core. Biochim. Biophys. Acta 1993; 1173: 81–84
   PubMed Web of Science ®Google Scholar
• Fransson L. A. Interactions between dermatan sulfate chains:I. Affinity chromatography of copolymeric galactosamino-glycans on dermatan sulfate substituted agarose. Biochim. Biophys. Acta 1976; 473: 106–115
   Google Scholar
• Fransson L. A., Cöster L. Interactions between dermatan sulfate chain: II. Structural studies on aggregating glycan chains and oligosaccharides with affinity for dermatan sulfate-sub-stituted agarose. Biochim. Biophys. Acta 1979; 582: 132–144
   PubMed Web of Science ®Google Scholar
• Cöster L., Fransson L. A., Seehan J., Nieduszynski I. A., Phelps C. R. Self association of dermatan sulfate proteoglycans from bovine sclera. Biochem. J. 1981; 197: 483–490
   PubMed Web of Science ®Google Scholar
• Poole A. B., Webber C., Pidoux I., Choi H., Rosenberg L. C. Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues. J. Histochem. Cytochem. 1986; 34: 619–624
   PubMed Web of Science ®Google Scholar
• Sobue M., Nakashima N., Fukatsu T., Nagasaka T., Katoh T., Ogura T., Takeuchi J. Production and characterization of monoclonal antibody to dermatan sulfate proteoglycan. J. Histochem. Cytochem. 1988; 36: 479–485
   PubMed Web of Science ®Google Scholar
• Riessen R., Isner J. M., Blessing E., Loushin C., Nikol S., Wight T. 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
• Yamaguchi Y., Mamm D. M., Ruoslahti E. Negative regulation of transforming growth factor-B by the proteoglycan decorin. Nature 1990; 346: 281–284
   PubMed Web of Science ®Google Scholar