Gene Expression of the Chondroitin Sulfate Proteoglycan Core Protein PG19

LITERATURE CITED

• Alfonso-Pizarro, A., D. P. Carlson, and J. Ross. 1984. Subcellular localization of RNAs in transfected cells: role of sequences at the 5′ terminus. Nucleic Acids Res. 12:8363–8380.
   PubMedGoogle Scholar
• Allan, M., W. G. Lanyon, and J. Paul. 1983. Multiple origins of transcription in the 4.5 Kb upstream of the epsilon-globin gene. Cell 35:187–197.
   PubMedGoogle Scholar
• Axelsson, I., and D. K. Heinegård. 1980. Characterization of chondroitin sulfate-rich proteoglycans from bovine corneal stroma. Exp. Eye Res. 31:57–66.
   PubMed Web of Science ®Google Scholar
• Benyajati, C., N. Spoerel, H. Haymerle, and M. Ashburner. 1983. The messenger RNA for alcohol dehydrogenase in Drosophila melanogaster differs in its 5′ end in different developmental stages. Cell 33:125–133.
   PubMed Web of Science ®Google Scholar
• Bos, J. L., M. Verlaan-de Vries, A. M. Jansen, G. H. Veeneman, J. M. van Boom, and A. J. ver der Erb. 1984. Three different mutations in codon 61 of the human N-ras gene detected by synthetic oligonucleotide hybridization. Nucleic Acids Res. 12:9155–9163.
   PubMed Web of Science ®Google Scholar
• Bourdon, M. A., Å. Oldberg, M. Pierschbacher, and E. Ruoslahti. 1985. Molecular cloning and sequence analysis of a chondroitin sulfate proteoglycan cDNA. Proc. Natl. Acad. Sci. USA 82:1321–1325.
   PubMedGoogle Scholar
• Bourdon, M. A., M. Shiga, and E. Ruoslahti. 1986. Identification from cDNA of the precursor form of a chondroitin sulfate proteoglycen core protein. J. Biol. Chem. 261:12534–12537.
   PubMedGoogle Scholar
• Brennan, M. J., Å. Oldberg, E. G. Hayman, and E. Ruoslahti. 1983. Effect of a proteoglycan produced by rat tumor cells on their adhesion to fibronectin-collagen substrata. Cancer Res. 43:4302–4307.
   PubMed Web of Science ®Google Scholar
• Brennan, M. J., Å. Oldberg, M. D. Pierschbacher, and E. Ruoslahti. 1984. Chondroitin/dermatan sulfate proteoglycan in human fetal membranes. J. Biol. Chem. 259:13742–13750.
   PubMedGoogle Scholar
• Couchman, J. R., A. Woods, M. Höök, and J. E. Christner. 1985. Characterization of a dermatan sulfate proteoglycan synthesized by murine parietal yolk sac (PYS-2). J. Biol. Chem. 260:13755–13762.
   PubMedGoogle Scholar
• Culp, L. A., B. A. Murray, and B. J. Rollins. 1979. Fibronection and proteoglycans as determinants of cell-substratum adhesion. J. Supramol. Struct. 11:401–427.
   PubMedGoogle Scholar
• Didsbury, J. R., E. C. Theil, R. E. Kaufman, and L. F. Dickey. 1986. Multiple red cell ferritin mRNAs, which code for an abundant protein in the embryonic cell type, analyzed by cDNA sequence and by primer extension of the 5′-untranslated regions. J. Biol. Chem. 261:949–955.
   PubMedGoogle Scholar
• Doege, K., P. Fernandez, J. R. Hassell, M. Sasaki, and Y. Yamada. 1986. Partial cDNA sequence encoding a globular domain at the C terminus of the rat cartilage proteoglycan. J. Biol. Chem. 261:8108–8111.
   PubMedGoogle Scholar
• Efstratiadis, A., J. W. Posakony, T. Maniatis, R. M. Lawn, C. O'Connell, R. A. Spritz, J. K. De Riel, B. G. Forget, S. M. Weissman, J. L. Slightom, A. E. Blechl, O. Smithies, F. E. Baralle, C. C. Shoulders, and N. J. Proudfoot. 1980. The structure and evolution of the human β-globin gene family. Cell 21:653–668.
   PubMed Web of Science ®Google Scholar
• Fransson, L.-A., I. Carlstedt, L. Cöster, and A. Malmström. 1984. Binding of transferrin to the core protein of fibroblast proteoheparan sulfate. Proc. Natl. Acad. Sci. USA 81:5657–5661.
   PubMed Web of Science ®Google Scholar
• Goldberg, D. A. 1980. Isolation and partial characterization of the Drosophila alcohol dehydrogenase gene. Proc. Natl. Acad. Sci. USA 77:5794–5798.
   PubMedGoogle Scholar
• Grindlay, G. J., W. G. Lanyon, M. Allan, and J. Paul. 1984. Alternative sites of transcription initiation upstream of the canonical cap site in human γ-globin and β-globin genes. Nucleic Acids Res. 12:1811–1820.
   PubMedGoogle Scholar
• Hascall, V. C., and G. K. Hascall. 1981. Proteoglycans, p. 39–63. In E. D. Hay (ed.), Cell biology of extracellular matrix. Plenum Publishing Corp., New York.
   Google Scholar
• Hultmark, D., R. Klemenz, and W. J. Gehring. 1986. Translational and transcriptional control elements in the untranslated leader of the heat-shock gene hsp22. Cell 44:429–438.
   PubMedGoogle Scholar
• Jackson, F. R., T. A. Bargiello, S.-H. Yun, and M. W. Young. 1986. Product of per locus of Drosophila shares homology with proteoglycans. Nature (London) 320:185–188.
   PubMed Web of Science ®Google Scholar
• Kanwar, Y. S., and M. G. Farquhar. 1979. Isolation of glycosaminoglycans (heparan sulfate) from glomerular basement membranes. Proc. Natl. Acad. Sci. USA 76:1303–1307.
   PubMed Web of Science ®Google Scholar
• Koda, J. E., and M. Bernfield. 1984. Heparan sulfate proteoglycans from mouse mammary epithelial cells. Basal extracellular proteoglycan binds specifically to native type I collagen fibrils. J. Biol. Chem. 259:11763–11770.
   PubMedGoogle Scholar
• Krusius, T., and E. Ruoslahti. 1986. Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA. Proc. Natl. Acad. Sci. USA 83:7683–7687.
   PubMed Web of Science ®Google Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual, p. 280. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• McGrogan, M., C. C. Simonsen, D. T. Smouse, P. J. Farnham, and R. T. Schimke. 1985. Heterogeneity at the 5′ end termini of mouse dihydrofolate reductase mRNAs. J. Biol. Chem. 260:2307–2314.
   PubMedGoogle Scholar
• McKnight, S. L., E. R. Gavis, R. Kingsbury, and R. Axel. 1981. Analysis of transcriptional regulatory signals of the HSV thymidine kinase gene: identification of an upstream control region. Cell 25:385–398.
   PubMed Web of Science ®Google Scholar
• Melton, D. A., P. A. Krieg, M. R. Rebagliati, T. Maniatis, K. Zinn, and M. R. Green. 1984. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 12:7035–7056.
   PubMed Web of Science ®Google Scholar
• Oegema, T. R., Jr., V. C. Hascall, and R. Eigenstem. 1979. Characterization of bovine aorta proteoglycan extracted with guanidine hydrochloride in the presence of protease inhibitors. J. Biol. Chem. 254:1312–1318.
   PubMed Web of Science ®Google Scholar
• Oldberg, Å., E. G. Hayman, and E. Ruoslahti. 1981. Isolation of a chondroitin sulfate proteoglycan from a rat yolk sac tumor and immunochemical demonstration of its cell surface localization. J. Biol. Chem. 256:10847–10852.
   PubMed Web of Science ®Google Scholar
• Oldberg, Å., E. Linney, and E. Ruoslahti. 1983. Molecular cloning and nucleotide sequence of a cDNA clone coding for the cell attachment domain in human fibronectin. J. Biol. Chem. 258:10193–10196.
   PubMedGoogle Scholar
• Oldberg, Å., E. Ruoslahti. 1982. Interactions between chondroitin sulfate proteoglycan, fibronectin, and collagen. J. Biol. Chem. 257:4859–4863.
   PubMedGoogle Scholar
• Parthasarathy, N., and E. G. Spiro. 1981. Characterization of the glycosaminoglycan component of the renal glomerular basement membrane and its relationship to the peptide portion. J. Biol. Chem. 256:507–513.
   PubMed Web of Science ®Google Scholar
• Radhakrishnamurthy, B., E. Smart, E. R. Dalferes, Jr., and G. S. Berenson. 1980. Isolation and characterization of proteoglycans from bovine lung. J. Biol. Chem. 255:7575–7582.
   PubMed Web of Science ®Google Scholar
• Reddy, P., A. C. Jacquier, N. Abovich, G. Petersen, and M. Rosbash. 1986. The period clock locus of D. melanogaster codes for a proteoglycan. Cell 46:53–61.
   PubMed Web of Science ®Google Scholar
• Robinson, H. M., A. A. Horner, M. Höök, S. Ögren, and U. Lindahl. 1978. A proteoglycan form of heparin and its degradation to single-chain molecules. J. Biol. Chem. 253:6687–6693.
   PubMed Web of Science ®Google Scholar
• Robinson, J., M. Viti, and M. Höök. 1984. Structure and properties of an under-sulfated heparan sulfate proteoglycan synthesized by a rat hepatoma cell line. J. Cell Biol. 98:946–953.
   PubMed Web of Science ®Google Scholar
• Sai, S., T. Tanaka, R. A. Kosher, and M. L. Tanzer. 1986. Cloning and sequence analysis of a partial cDNA for chicken cartilage proteoglycan core protein. Proc. Natl. Acad. Sci. USA 83:5081–5085.
   PubMed Web of Science ®Google Scholar
• Sakashita, S., E. Engvall, and E. Ruoslahti. 1980. Basement membrane glycoprotein laminin binds to heparin. FEBS Lett. 116:243–246.
   PubMed Web of Science ®Google Scholar
• Sant, A. J., S. E. Cullen, K. S. Giacoletto, and B. D. Schwartz. 1985. Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan. J. Exp. Med. 162:1916–1934.
   PubMedGoogle Scholar
• Seldin, D. C., K. F. Austen, and R. L. Stevens. 1985. Purification and characterization of protease-resistant secretory granule proteoglycans containing chondroitin sulfate Di-B and heparin- like glycosaminoglycans from rat basophilic leukemia cells. J. Biol. Chem. 260:11131–11139.
   PubMedGoogle Scholar
• Shin, H.-S., T. A. Bargiello, B. T. Clark, F. R. Jackson, and M. W. Young. 1985. An unusual coding sequence from a Drosophila clock gene is conserved in vertebrates. Nature (London) 317:445–448.
   PubMed Web of Science ®Google Scholar
• Singer, R. H., and S. Penman. 1973. Messenger RNA in HeLa cells: kinetics of formation and decay. J. Mol. Biol. 78:321–334.
   PubMed Web of Science ®Google Scholar
• Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 99:503–517.
   Google Scholar
• Suzuki, S., M. D. Pierschbacher, E. G. Hayman, K. Nguyen, Y. Ohgren, and E. Ruoslahti. 1984. Domain structure of vitronectin. Alignment of active sites. J. Biol. Chem. 259:15307–15314.
   PubMed Web of Science ®Google Scholar
• Thomas, P. S. 1980. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA 77:5201–5205.
   PubMed Web of Science ®Google Scholar
• Tsou, A.-P., C. Lai, P. Danielson, D. J. Noonan, and J. G. Sutcliffe. 1986. Structural characterization of a heterogeneous family of rat brain mRNAs. Mol. Cell. Biol. 6:768–778.
   PubMedGoogle Scholar
• Ullrich, A., J. Shine, J. Chergwin, R. Pictet, E. Fischer, W. J. Rutter, and H. M. Goodman. 1977. Rat insulin genes: construction of plasmids containing the coding sequences. Science 196:1313–1319.
   PubMed Web of Science ®Google Scholar
• Van Beveren, C., F. van Straaten, T. Curran, R. Muller, and I. M. Verma. 1983. Analysis of FBJ-MuSV provirus and cfos (mouse) gene reveals that viral and cellular fos gene products have different carboxytermini. Cell 32:1241–1255.
   PubMed Web of Science ®Google Scholar
• Woodley, D. T., C. N. Rao, J. R. Hassell, L. A. Liotta, G. R. Martin, and H. K. Kleinman. 1983. Interactions of basement membrane components. Biochim. Biophys. Acta 761:287–283.
   Google Scholar
• Young, R. A., O. Hagenbüchle, and U. Schibler. 1981. A single mouse α-amylase gene specifies two differet tissue-specific mRNAs. Cell 23:451–458.
   PubMed Web of Science ®Google Scholar