Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1998 Feb 15;330(Pt 1):549–557. doi: 10.1042/bj3300549

Chondroadherin expression changes in skeletal development.

Z Shen 1, S Gantcheva 1, B Mânsson 1, D Heinegârd 1, Y Sommarin 1
PMCID: PMC1219172  PMID: 9461555

Abstract

Chondroadherin is a cartilage protein with cell binding properties. The expression of chondroadherin was studied in rat tissues and during postnatal femoral head development. For design of oligonucleotide probes and primers a 1664 bp, full length, rat chondroadherin cDNA was isolated from a rat chondrosarcoma library and sequenced. Northern blot analysis showed chondroadherin mRNA to be present in femoral head and rib cartilage, as well as in tendon. More sensitive reverse-transcriptase PCR additionally identified the mRNA in calvaria, long bone and bone marrow. Localization of chondroadherin by immunocytochemistry in the developing femoral head from postnatal day 14 to day 60 showed presence of the protein in cartilaginous regions. With increasing age a very distinct localization of chondroadherin was seen in the territorial matrix around late proliferative cells in the growth plate as well as in the developing articular cartilage in the maturing femoral head. Localization of chondroadherin mRNA by in situ hybridization was in agreement with immunocytochemistry with strong hybridization signals in late proliferative cells in the growth plate. In the articular cartilage the expression was restricted to cells in the lower regions. A three-fold increase of cartilage chondroadherin content in the growing femoral head was demonstrated by Western blot analysis. The high expression of this cell binding protein in a dynamic region of cartilage suggests an important role for chondroadherin in the regulation of chondrocyte growth and proliferation.

Full Text

The Full Text of this article is available as a PDF (712.1 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blochberger T. C., Vergnes J. P., Hempel J., Hassell J. R. cDNA to chick lumican (corneal keratan sulfate proteoglycan) reveals homology to the small interstitial proteoglycan gene family and expression in muscle and intestine. J Biol Chem. 1992 Jan 5;267(1):347–352. [PubMed] [Google Scholar]
  2. Camper L., Heinegârd D., Lundgren-Akerlund E. Integrin alpha2beta1 is a receptor for the cartilage matrix protein chondroadherin. J Cell Biol. 1997 Sep 8;138(5):1159–1167. doi: 10.1083/jcb.138.5.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  4. DiCesare P., Hauser N., Lehman D., Pasumarti S., Paulsson M. Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon. FEBS Lett. 1994 Nov 7;354(2):237–240. doi: 10.1016/0014-5793(94)01134-6. [DOI] [PubMed] [Google Scholar]
  5. 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 Mar 15;264(8):4571–4576. [PubMed] [Google Scholar]
  6. Franzén A., Heinegård D., Reiland S., Olsson S. E. Proteoglycans and calcification of cartilage in the femoral head epiphysis of the immature rat. J Bone Joint Surg Am. 1982 Apr;64(4):558–566. [PubMed] [Google Scholar]
  7. Hedbom E., Heinegård D. Binding of fibromodulin and decorin to separate sites on fibrillar collagens. J Biol Chem. 1993 Dec 25;268(36):27307–27312. [PubMed] [Google Scholar]
  8. Kobe B., Deisenhofer J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature. 1993 Dec 23;366(6457):751–756. doi: 10.1038/366751a0. [DOI] [PubMed] [Google Scholar]
  9. Koshino T. Development of femoral head to the rat from calcification to ossification. Acta Radiol Suppl. 1975;344:33–46. doi: 10.1177/0284185175016s34404. [DOI] [PubMed] [Google Scholar]
  10. Larsson T., Sommarin Y., Paulsson M., Antonsson P., Hedbom E., Wendel M., Heinegård D. Cartilage matrix proteins. A basic 36-kDa protein with a restricted distribution to cartilage and bone. J Biol Chem. 1991 Oct 25;266(30):20428–20433. [PubMed] [Google Scholar]
  11. Mizuno M., Fujisawa R., Kuboki Y. Bone chondroadherin promotes attachment of osteoblastic cells to solid-state substrates and shows affinity to collagen. Calcif Tissue Int. 1996 Sep;59(3):163–167. doi: 10.1007/s002239900103. [DOI] [PubMed] [Google Scholar]
  12. Neame P. J., Sommarin Y., Boynton R. E., Heinegård D. The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated from bovine cartilage. J Biol Chem. 1994 Aug 26;269(34):21547–21554. [PubMed] [Google Scholar]
  13. Oldberg A., Antonsson P., Lindblom K., Heinegård D. A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin). EMBO J. 1989 Sep;8(9):2601–2604. doi: 10.1002/j.1460-2075.1989.tb08399.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rada J. A., Cornuet P. K., Hassell J. R. Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins. Exp Eye Res. 1993 Jun;56(6):635–648. doi: 10.1006/exer.1993.1081. [DOI] [PubMed] [Google Scholar]
  15. Robbins J. R., Vogel K. G. Regional expression of mRNA for proteoglycans and collagen in tendon. Eur J Cell Biol. 1994 Aug;64(2):264–270. [PubMed] [Google Scholar]
  16. Sandberg M., Vuorio E. Localization of types I, II, and III collagen mRNAs in developing human skeletal tissues by in situ hybridization. J Cell Biol. 1987 Apr;104(4):1077–1084. doi: 10.1083/jcb.104.4.1077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Shen Z., Heinegård D., Sommarin Y. Distribution and expression of cartilage oligomeric matrix protein and bone sialoprotein show marked changes during rat femoral head development. Matrix Biol. 1995 Dec;14(9):773–781. doi: 10.1016/s0945-053x(05)80020-4. [DOI] [PubMed] [Google Scholar]
  18. Sommarin Y., Larsson T., Heinegård D. Chondrocyte-matrix interactions. Attachment to proteins isolated from cartilage. Exp Cell Res. 1989 Sep;184(1):181–192. doi: 10.1016/0014-4827(89)90376-5. [DOI] [PubMed] [Google Scholar]
  19. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Vortkamp A., Lee K., Lanske B., Segre G. V., Kronenberg H. M., Tabin C. J. Regulation of rate of cartilage differentiation by Indian hedgehog and PTH-related protein. Science. 1996 Aug 2;273(5275):613–622. doi: 10.1126/science.273.5275.613. [DOI] [PubMed] [Google Scholar]
  21. Whinna H. C., Choi H. U., Rosenberg L. C., Church F. C. Interaction of heparin cofactor II with biglycan and decorin. J Biol Chem. 1993 Feb 25;268(6):3920–3924. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES