Skip to main content
Biochemical Journal logoLink to Biochemical Journal
letter
. 1993 Jun 15;292(Pt 3):947–949. doi: 10.1042/bj2920947

Evolution of the hyaluronan-binding module of link protein.

E Barta, F Deák, I Kiss
PMCID: PMC1134205  PMID: 8318021

Full text

PDF
947

Selected References

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

  1. Antonsson P., Heinegård D., Oldberg A. The keratan sulfate-enriched region of bovine cartilage proteoglycan consists of a consecutively repeated hexapeptide motif. J Biol Chem. 1989 Sep 25;264(27):16170–16173. [PubMed] [Google Scholar]
  2. Aruffo A., Stamenkovic I., Melnick M., Underhill C. B., Seed B. CD44 is the principal cell surface receptor for hyaluronate. Cell. 1990 Jun 29;61(7):1303–1313. doi: 10.1016/0092-8674(90)90694-a. [DOI] [PubMed] [Google Scholar]
  3. Bonnet F., Périn J. P., Lorenzo F., Jollès J., Jollès P. An unexpected sequence homology between link proteins of the proteoglycan complex and immunoglobulin-like proteins. Biochim Biophys Acta. 1986 Sep 5;873(1):152–155. doi: 10.1016/0167-4838(86)90202-5. [DOI] [PubMed] [Google Scholar]
  4. Bosworth B. T., St John T., Gallatin W. M., Harp J. A. Sequence of the bovine CD44 cDNA: comparison with human and mouse sequences. Mol Immunol. 1991 Oct;28(10):1131–1135. doi: 10.1016/0161-5890(91)90028-i. [DOI] [PubMed] [Google Scholar]
  5. Chandrasekaran L., Tanzer M. L. Molecular cloning of chicken aggrecan. Structural analyses. Biochem J. 1992 Dec 15;288(Pt 3):903–910. doi: 10.1042/bj2880903. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Deák F., Kiss I., Sparks K. J., Argraves W. S., Hampikian G., Goetinck P. F. Complete amino acid sequence of chicken cartilage link protein deduced from cDNA clones. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3766–3770. doi: 10.1073/pnas.83.11.3766. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Doege K. J., Sasaki M., Kimura T., Yamada Y. Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms. J Biol Chem. 1991 Jan 15;266(2):894–902. [PubMed] [Google Scholar]
  9. Doege K., Sasaki M., Horigan E., Hassell J. R., Yamada Y. Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones. J Biol Chem. 1987 Dec 25;262(36):17757–17767. [PubMed] [Google Scholar]
  10. Dudhia J., Hardingham T. E. The primary structure of human cartilage link protein. Nucleic Acids Res. 1990 Mar 11;18(5):1292–1292. doi: 10.1093/nar/18.5.1292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fosang A. J., Hardingham T. E. Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Identification of G2 domain and its lack of interaction with hyaluronate and link protein. Biochem J. 1989 Aug 1;261(3):801–809. doi: 10.1042/bj2610801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Goetinck P. F., Stirpe N. S., Tsonis P. A., Carlone D. The tandemly repeated sequences of cartilage link protein contain the sites for interaction with hyaluronic acid. J Cell Biol. 1987 Nov;105(5):2403–2408. doi: 10.1083/jcb.105.5.2403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Goldstein L. A., Zhou D. F., Picker L. J., Minty C. N., Bargatze R. F., Ding J. F., Butcher E. C. A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins. Cell. 1989 Mar 24;56(6):1063–1072. doi: 10.1016/0092-8674(89)90639-9. [DOI] [PubMed] [Google Scholar]
  14. Gribskov M., Burgess R. R. Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins. Nucleic Acids Res. 1986 Aug 26;14(16):6745–6763. doi: 10.1093/nar/14.16.6745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Günthert U., Hofmann M., Rudy W., Reber S., Zöller M., Haussmann I., Matzku S., Wenzel A., Ponta H., Herrlich P. A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cells. Cell. 1991 Apr 5;65(1):13–24. doi: 10.1016/0092-8674(91)90403-l. [DOI] [PubMed] [Google Scholar]
  16. Idzerda R. L., Carter W. G., Nottenburg C., Wayner E. A., Gallatin W. M., St John T. Isolation and DNA sequence of a cDNA clone encoding a lymphocyte adhesion receptor for high endothelium. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4659–4663. doi: 10.1073/pnas.86.12.4659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kiss I., Deák F., Mestrić S., Delius H., Soos J., Dékány K., Argraves W. S., Sparks K. J., Goetinck P. F. Structure of the chicken link protein gene: exons correlate with the protein domains. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6399–6403. doi: 10.1073/pnas.84.18.6399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lee T. H., Wisniewski H. G., Vilcek J. A novel secretory tumor necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44. J Cell Biol. 1992 Jan;116(2):545–557. doi: 10.1083/jcb.116.2.545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Neame P. J., Christner J. E., Baker J. R. Cartilage proteoglycan aggregates. The link protein and proteoglycan amino-terminal globular domains have similar structures. J Biol Chem. 1987 Dec 25;262(36):17768–17778. [PubMed] [Google Scholar]
  20. Neame P. J., Christner J. E., Baker J. R. The primary structure of link protein from rat chondrosarcoma proteoglycan aggregate. J Biol Chem. 1986 Mar 15;261(8):3519–3535. [PubMed] [Google Scholar]
  21. Nottenburg C., Rees G., St John T. Isolation of mouse CD44 cDNA: structural features are distinct from the primate cDNA. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8521–8525. doi: 10.1073/pnas.86.21.8521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Perkins S. J., Nealis A. S., Dudhia J., Hardingham T. E. Immunoglobulin fold and tandem repeat structures in proteoglycan N-terminal domains and link protein. J Mol Biol. 1989 Apr 20;206(4):737–753. doi: 10.1016/0022-2836(89)90580-9. [DOI] [PubMed] [Google Scholar]
  23. Rauch U., Karthikeyan L., Maurel P., Margolis R. U., Margolis R. K. Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain. J Biol Chem. 1992 Sep 25;267(27):19536–19547. [PubMed] [Google Scholar]
  24. Rhodes C., Doege K., Sasaki M., Yamada Y. Alternative splicing generates two different mRNA species for rat link protein. J Biol Chem. 1988 May 5;263(13):6063–6067. [PubMed] [Google Scholar]
  25. Stamenkovic I., Amiot M., Pesando J. M., Seed B. A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family. Cell. 1989 Mar 24;56(6):1057–1062. doi: 10.1016/0092-8674(89)90638-7. [DOI] [PubMed] [Google Scholar]
  26. Zimmermann D. R., Ruoslahti E. Multiple domains of the large fibroblast proteoglycan, versican. EMBO J. 1989 Oct;8(10):2975–2981. doi: 10.1002/j.1460-2075.1989.tb08447.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES