Regulation of Osteopontin Expression by Type I Collagen in Preosteoblastic UMR201 Cells

References

• Owen T. A., Aronow M., Shaloub V., Barone L. M., Wilming L., Tassinari M. S., Kennedy M. B., Pockwinse S., Lian H. B., Stein G. S. Progressive development of the rat osteoblast phenotype in vitro: Reciprocal relationships in expression of genes associated with osteoblast proliferation and differentiation during formation of the bone extracellular matrix. J. Cell Physiol. 1990; 143: 420–430
   PubMed Web of Science ®Google Scholar
• Zhou H., Choong P., McCarthy R., Chou S. T., Martin T. J., Ng K. W. In situ hybridization to show sequential expression of osteoblast gene markers during bone formation in vivo. J. Bone Min. Res. 1994; 9: 1489–1499
   PubMed Web of Science ®Google Scholar
• Traianedes K., Ng K. W., Martin T. J., Findlay D. M. Cell substratum modulates responses of preosteoblasts to retinoic acid. J. Cell. Physiol. 1993; 157: 243–252
   PubMed Web of Science ®Google Scholar
• Andrianarivo A. G., Robinson J. A., Mann K. G., Tracy R. P. Growth on type I collagen promotes expression of the osteoblastic phenotype in human osteosarcoma MG-63 cells. J. Cell. Physiol. 1992; 153: 256–265
   PubMed Web of Science ®Google Scholar
• Southey M. C., Findlay D. M., Kemp B. E. Regulation of membrane-associated tyrosine phosphatases in UMR 106.06 osteoblast-like cells. Biochem. J. 1995; 305: 485–490
   PubMed Web of Science ®Google Scholar
• Ikeda K., Michelangeli V. P., Martin T. J., Findlay D. M. A type 1 collagen substrate increases CT and PTH receptor mediated signal transduction in UMR 106-06 osteoblast-like cells. J. Cell. Physiol. 1993; 156: 130–137
   PubMed Web of Science ®Google Scholar
• Green J., Schotland S., Stauber D. J., Kleeman C. R., Clemens T. S. Cell-matrix interaction in bone: type I collagen modulates signal transduction in osteoblast-like cells. Am. J. Physiol. 1995; 37: CI090–CI103
   Google Scholar
• Mark M. P., Prince C. W., Osawa T., Gay S., Bronkers A. L. J. J., Butler W. T. Immunohistochemical demonstration of a 44kdal phosphoprotein in developing rat bones. J. Histochem. Cviochem. 1987; 35: 707–716
   PubMed Web of Science ®Google Scholar
• Mark M. P., Prince C. W., Gay S., Austin R. L., Butler W. T. 44kDal bone phosphoprotein antigenicity at ectopic sites in newborn rats: Kidney and nervous tissue. Cell Tissue Res. 1988; 251: 23–30
   PubMed Web of Science ®Google Scholar
• Somerman M. J., Prince C. W., Butler W. T., Foster R. A., Moehring J. M., Sauk J. J. Cell attachment activity of the 44 kilodalton bone phosphoprotein is not restricted to bone cells. Matrix 1989; 9: 49–54
   PubMedGoogle Scholar
• Reinholt F. P., Hultenby K., Oldberg Å., Heinegård D. Osteopontin—a possible anchor of osteoclasts to bone. Proc. Natl. Acad. Sci. USA 1990; 87: 4473–4475
   PubMed Web of Science ®Google Scholar
• Flores M., Norgård M., Heinegård D., Reinholt F. P., Andersson G. RGD-directed attachment of isolated rat osteoclasts to osteopontin, bone sialoprotein and fibronectin. Exp. Cell Res. 1992; 201: 526–530
   PubMed Web of Science ®Google Scholar
• Helfrich M. H., Nesbitt S. A., Dorey E. L., Horton M. A. Rat osteoclasts adhere to a wide range of RGD (Arg-Gly-Asp) pep-tide-containing proteins, including the bone sialoproteins and fibronectin via β3 integrins. J. Bone Min. Res. 1992; 7: 335–343
   PubMed Web of Science ®Google Scholar
• Ross F. P., Chappel J., Alvarez J. I., Sander D., Butler W. T., Farach-Carson M. C., Mintz K. A., Gehron Robey P., Teitelbaum S. L., Chercsh D. A. Interactions between the bone matrix proteins osteopontin and bone sialoprotein and the osteoclast integrin αvβ3 potentiate resorption. J. Biol. Chem. 1993; 268: 9901–9907
   PubMed Web of Science ®Google Scholar
• Hynes R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992; 69: 11–25
   PubMed Web of Science ®Google Scholar
• Young M. F., Ibaraki K., Kerr J. M., Heegaard A-M. “Molecular and cellular biology of the major noncollagenous proteins in bone”. Cellular and Molecular Biology of Bone, edited by M. Noda, 191-234. Academic Press., San Diego 1993
   Google Scholar
• Ek-Rylander B., Flores M., Wendel M., Heinegard D., Andersson G. Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. J. Biol. Chem. 1994; 269: 14853–14856
   PubMed Web of Science ®Google Scholar
• Prince C. W., Butler W. T. 1,25-Dihydroxyvitamin D3 regulates the biosynthesis of osteopontin, a bone-derived cell attachment protein, in clonal osteoblast-like osteosarcoma cells. Matrix. 1987; 7: 305–313
   Google Scholar
• Yoon K., Buenaga R., Rodan G. Tissue specificity and developmental expression of rat osteopontin. Biochem. Biophys. Res. Commun. 1987; 148: 1129–1136
   PubMed Web of Science ®Google Scholar
• Noda M., Yoon K., Prince C. W., Butler W. T., Rodan G. A. Transcriptional regulation of osteopontin production in rat osteosarcoma cells by type beta transforming growth factor. J. Biol. Chem. 1988; 263: 13916–13921
   PubMed Web of Science ®Google Scholar
• Kubota T., Zhang Q., Wrana J. L., Ber R., Aubin J. E., Butler W. T., Sodek J. Multiple forms of spp (secreted phospho-protein, osteopontin) synthesized by normal and transformed bone cell populations: Regulation by TGF-β. Biochem. Biophys. Res. Commun. 1989; 162: 1453–1459
   PubMed Web of Science ®Google Scholar
• Ng K. W., Gummer P. R., Michelangeli V. P., Bateman J. F., Mascara T., Cole W. G., Martin T. J. Regulation of alkaline phosphatase expression in neonatal rat clonal calvarial cell strain by retinoic acid. J. Bone Miner. Res. 1988; 3: 53–61
   PubMed Web of Science ®Google Scholar
• Dulbecco R., Vogt M. Plaque formation and isolation of pure cell lines with poliomyelitis viruses. J. Exp. Med. 1954; 199: 167–182
   Google Scholar
• Majeska R. B., Port M., Einhorn T. A. Attachment to extracellular matrix molecules by cells differing in the expression of osteoblastic traits. J. Bone Miner. Res. 1993; 8: 277–288
   PubMed Web of Science ®Google Scholar
• Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual. Cold Springs Harbor Laboratory, 2nd edition. Cold springs Harbor, New York 1989
   Google Scholar
• Young M. F., Kerr J. M., Termine J. D., Wewer U. M., Wang M. G., McBride O. W., Fisher L. W. cDNA cloning, mRNA distribution and heterogeneity, chromosomal location, and RFLP analysis of human osteopontin (OPN). Genomics 1990; 7: 491–502
   PubMed Web of Science ®Google Scholar
• Noda M., Yoon K., Thiede M., Buenaga R., Weiss M., Henthorn P., Harris H., Rodan G. A. cDNA cloning of alkaline phosphatase from rat osteosarcoma (ROS 17/2.8) cells. J. Bone Miner. Res. 1987; 2: 161–164
   PubMed Web of Science ®Google Scholar
• Zelent A., Krust A., Petkovich M., Kastner P., Chambon P. Cloning of murine α and β retinoic acid receptors and a novel receptor γ predominantly expressed in skin. Nature 1989; 339: 714–717
   PubMed Web of Science ®Google Scholar
• Kastner P., Krust A., Mendelsohn C., Gamier J. M., Zelent A., Leroy P., Staub A., Chambon P. Murine isoforms of retinoic acid receptor γ with specific patterns of expression. Proc. Natl. Acad. Set USA 1990; 87: 2700–2704
   PubMed Web of Science ®Google Scholar
• Dugaiczyk A., Haron J. A., Stone E. M., Dennison O. E., Rothblum K. N., Schwartz R. J. Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle. Biochem. 1983; 22: 1605–1613
   PubMed Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Chambers A. F., Behrend E. I., Wilson S. M., Denhardt D. T. Induction of expression of osteopontin (OPN; secreted phosphoprotein) in metastatic, ras-transformed NIH 3T3 cells. Anticancer Res. 1992; 12: 43–48
   PubMed Web of Science ®Google Scholar
• Current Protocols in Molecular Biology. Identification of newly transcribed RNA, Unit 4.10. John Wiley and Sons, Inc, MAUSA 1994
   Google Scholar
• Harrison J. R., Vargas S. J., Petersen D. N., Lorenzo J. A., Kream B. E. Interleukin-1α and phorbol ester inhibit collagen synthesis in osteoblastic MC3T3-E1 cells by a transcriptional mechanism. Mol. Endocrinol. 1990; 4: 184–190
   PubMed Web of Science ®Google Scholar
• Gough N. M. Rapid and quantitative preparation of cytoplasmic RNA from small numbers of cells. Anal. Biochem. 1988; 173: 93–95
   PubMed Web of Science ®Google Scholar
• Chang P-L., Prince C. W. 1α,25-Dihydroxyvitamin D3 stimulates synthesis of and secretion of nonphosphorylated osteopontin (secreted phosphoprotein 1) in mouse JB6 epidermal cells. Cancer Res. 1991; 51: 2144–2150
   PubMed Web of Science ®Google Scholar
• Nemir M., DeVouge M. W., Mukherjee B. B. Normal rat kidney cells secrete both phosphorylated and nonphosphorylated forms of osteopontin showing different physiological properties. J. Biol. Chem. 1989; 264: 18202–18208
   PubMed Web of Science ®Google Scholar
• Chang P-L., Ridall A. L., Prince C. W. Calcitriol regulation of osteopontin expression in mouse epidermal cells. Endocrinology 1994; 135: 863–869
   PubMed Web of Science ®Google Scholar
• Manji S. S., Zhou H., Findlay D. M., Martin T. J., Ng K. W. Tumour necrosis factor a facilitates nuclear actions of retinoic acid to regulate expression of the alkaline phosphatase gene in pre-osteoblasts. J. Biol. Chem. 1995, (in press).
   PubMed Web of Science ®Google Scholar
• Zhou H., Hammonds R. G., Findlay D. M., Fuller P. J., Martin T. J., Ng K. W. Retinoic acid modulation of mRNA levels in malignant, non transformed, and immortalized osteoblasts. J. Bone Miner. Res. 1991; 6: 767–777
   PubMed Web of Science ®Google Scholar
• Miyaichi A., Alverez J., Greenfield E. M., Teti A., Grano M., Colucci S., Zambonin-Zallone A., Ross F. P., Teitelbaum S. L., Cheresh D., Hruska K. A. Recognition of osteopontin and related peptides by an avpo integrin stimulates immediate cell signals in osteoclasts. J. Biol. Chem. 1991; 266: 20369–20374
   PubMed Web of Science ®Google Scholar
• Gehron Robey P. Calcified Tissue Matrix: Composition and Regulation. Workshop C of the American Society for Bone and Mineral Research. 1990; 1–15
   Google Scholar
• Mikuni-Takagaki Y., Kakai Y., Satoyoshi M., Kawano E., Suzuki Y., Kawase T., Saito S. Matrix mineralization and the differentiation of osteocyte-like cells in culture. J. Bone Min. Res. 1995; 10: 231–242
   PubMed Web of Science ®Google Scholar
• Mikuni-Takagaki Y., Glimcher M. J. Post-translational processing of chicken bone phosphoproteins. Identification of bone phosphoprotein kinase. Biochem. J. 1990; 268: 593–597
   PubMed Web of Science ®Google Scholar
• Sfeir C., Veis A. Casein kinase localization in the endoplasmic reticulum of the ROS 17/2.8 cell line. J. Bone Min. Res. 1995; 10: 607–615
   PubMed Web of Science ®Google Scholar
• Denhardt D. T., Guo X. Osteopontin: a protein with diverse functions. FASEB J. 1993; 7: 1475–1482
   PubMed Web of Science ®Google Scholar
• Heath J. K., Suva L. J., Yoon K., Kiledjian M., Martin T. J., Rodan G. A. Retinoic acid stimulates transcriptional activity for the alkaline phosphatase promoter in the immortal rat calvarial cell line RCT-1. Mol. Endocrinol. 1992; 6: 636–646
   PubMed Web of Science ®Google Scholar
• Zhou H., Manji S. S., Findlay D. M., Martin T. J., Heath J. K., Ng K. W. Novel action of retinoic acid. J. Biol. Chem. 1994; 269: 22433–22439
   PubMed Web of Science ®Google Scholar
• Kiledjian M., Kadesch T. Post-transcriptional regulation of the human liver/bone/kidney alkaline phosphatase gene. J. Biol. Chem. 1991; 266: 4207–4213
   PubMed Web of Science ®Google Scholar
• Jarrous N., Kaempfer R. Induction of human interleukin-1 gene expression by retinoic acid and its regulation at processing of precursor transcripts. J. Biol. Chem. 1994; 269: 23141–23149
   PubMed Web of Science ®Google Scholar