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. 1989 Nov;86(21):8521–8525. doi: 10.1073/pnas.86.21.8521

Isolation of mouse CD44 cDNA: structural features are distinct from the primate cDNA.

C Nottenburg 1, G Rees 1, T St John 1
PMCID: PMC298314  PMID: 2682651

Abstract

CD44 is a glycoprotein that participates in adhesion of lymphocytes to high endothelial cells of lymph organs and likely functions in other intercellular adhesions as well. We have isolated a mouse CD44 cDNA by polymerase chain reaction amplification of cDNA synthesized from total cellular RNA isolated from 38C-13, a B-lymphocyte cell line. The oligonucleotide sequences were based at the 5' end on the baboon CD44 sequence upstream of and including the translation initiator ATG and at the 3' end on a mouse CD44 sequence that was determined from a rare, incomplete cDNA clone. The mouse CD44 DNA sequence is similar to the baboon CD44 sequence but has structural features that are distinct. The external domain has a region that is only 35% similar between the mouse and primate proteins, in contrast to 85%-90% similarity in the rest of the sequence. In addition, just upstream from the predicted cleavage site of the leader peptide, nucleotide insertions result in the addition of two or four amino acids, depending upon the mouse strain. An amino acid replacement between two strains carrying different CD44 (also called Pgp-1) allotypes is likely responsible for the Pgp-1 polymorphism. The most striking aspect of mouse CD44 is that the RNA does not fractionate with polyadenylylated RNA, unlike the CD44 RNA in human, baboon, rat, and chicken.

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Selected References

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  1. Badley J. E., Bishop G. A., St John T., Frelinger J. A. A simple, rapid method for the purification of poly A+ RNA. Biotechniques. 1988 Feb;6(2):114–116. [PubMed] [Google Scholar]
  2. Bellvé A. R., Millette C. F., Bhatnagar Y. M., O'Brien D. A. Dissociation of the mouse testis and characterization of isolated spermatogenic cells. J Histochem Cytochem. 1977 Jul;25(7):480–494. doi: 10.1177/25.7.893996. [DOI] [PubMed] [Google Scholar]
  3. Carter W. G., Wayner E. A. Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells. J Biol Chem. 1988 Mar 25;263(9):4193–4201. [PubMed] [Google Scholar]
  4. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  5. Gallatin W. M., Wayner E. A., Hoffman P. A., St John T., Butcher E. C., Carter W. G. Structural homology between lymphocyte receptors for high endothelium and class III extracellular matrix receptor. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4654–4658. doi: 10.1073/pnas.86.12.4654. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Hentschel C. C., Birnstiel M. L. The organization and expression of histone gene families. Cell. 1981 Aug;25(2):301–313. doi: 10.1016/0092-8674(81)90048-9. [DOI] [PubMed] [Google Scholar]
  8. Hunter T., Garrels J. I. Characterization of the mRNAs for alpha-, beta- and gamma-actin. Cell. 1977 Nov;12(3):767–781. doi: 10.1016/0092-8674(77)90276-8. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Isacke C. M., Sauvage C. A., Hyman R., Lesley J., Schulte R., Trowbridge I. S. Identification and characterization of the human Pgp-1 glycoprotein. Immunogenetics. 1986;23(5):326–332. doi: 10.1007/BF00398797. [DOI] [PubMed] [Google Scholar]
  11. Jacobson K., O'Dell D., August J. T. Lateral diffusion of an 80,000-dalton glycoprotein in the plasma membrane of murine fibroblasts: relationships to cell structure and function. J Cell Biol. 1984 Nov;99(5):1624–1633. doi: 10.1083/jcb.99.5.1624. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jalkanen S. T., Bargatze R. F., Herron L. R., Butcher E. C. A lymphoid cell surface glycoprotein involved in endothelial cell recognition and lymphocyte homing in man. Eur J Immunol. 1986 Oct;16(10):1195–1202. doi: 10.1002/eji.1830161003. [DOI] [PubMed] [Google Scholar]
  13. Jalkanen S., Bargatze R. F., de los Toyos J., Butcher E. C. Lymphocyte recognition of high endothelium: antibodies to distinct epitopes of an 85-95-kD glycoprotein antigen differentially inhibit lymphocyte binding to lymph node, mucosal, or synovial endothelial cells. J Cell Biol. 1987 Aug;105(2):983–990. doi: 10.1083/jcb.105.2.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kalomiris E. L., Bourguignon L. Y. Mouse T lymphoma cells contain a transmembrane glycoprotein (GP85) that binds ankyrin. J Cell Biol. 1988 Feb;106(2):319–327. doi: 10.1083/jcb.106.2.319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kozak M. An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 1987 Oct 26;15(20):8125–8148. doi: 10.1093/nar/15.20.8125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lesley J., Trowbridge I. S. Genetic characterization of a polymorphic murine cell-surface glycoprotein. Immunogenetics. 1982 Mar;15(3):313–320. doi: 10.1007/BF00364339. [DOI] [PubMed] [Google Scholar]
  17. McMaster G. K., Carmichael G. G. Analysis of single- and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4835–4838. doi: 10.1073/pnas.74.11.4835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Milcarek C., Price R., Penman S. The metabolism of a poly(A) minus mRNA fraction in HeLa cells. Cell. 1974 Sep;3(1):1–10. doi: 10.1016/0092-8674(74)90030-0. [DOI] [PubMed] [Google Scholar]
  19. Picker L. J., De los Toyos J., Telen M. J., Haynes B. F., Butcher E. C. Monoclonal antibodies against the CD44 [In(Lu)-related p80], and Pgp-1 antigens in man recognize the Hermes class of lymphocyte homing receptors. J Immunol. 1989 Mar 15;142(6):2046–2051. [PubMed] [Google Scholar]
  20. Rosenthal E. T., Tansey T. R., Ruderman J. V. Sequence-specific adenylations and deadenylations accompany changes in the translation of maternal messenger RNA after fertilization of Spisula oocytes. J Mol Biol. 1983 May 25;166(3):309–327. doi: 10.1016/s0022-2836(83)80087-4. [DOI] [PubMed] [Google Scholar]
  21. Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn G. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science. 1988 Jan 29;239(4839):487–491. doi: 10.1126/science.2448875. [DOI] [PubMed] [Google Scholar]
  22. Saiki R. K., Scharf S., Faloona F., Mullis K. B., Horn G. T., Erlich H. A., Arnheim N. Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science. 1985 Dec 20;230(4732):1350–1354. doi: 10.1126/science.2999980. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Stoolman L. M. Adhesion molecules controlling lymphocyte migration. Cell. 1989 Mar 24;56(6):907–910. doi: 10.1016/0092-8674(89)90620-x. [DOI] [PubMed] [Google Scholar]
  25. Swartwout S. G., Preisler H., Guan W. D., Kinniburgh A. J. Relatively stable population of c-myc RNA that lacks long poly(A). Mol Cell Biol. 1987 Jun;7(6):2052–2058. doi: 10.1128/mcb.7.6.2052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Telen M. J., Eisenbarth G. S., Haynes B. F. Human erythrocyte antigens. Regulation of expression of a novel erythrocyte surface antigen by the inhibitor Lutheran In(Lu) gene. J Clin Invest. 1983 Jun;71(6):1878–1886. doi: 10.1172/JCI110943. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Trowbridge I. S., Lesley J., Schulte R., Hyman R., Trotter J. Biochemical characterization and cellular distribution of a polymorphic, murine cell-surface glycoprotein expressed on lymphoid tissues. Immunogenetics. 1982 Mar;15(3):299–312. doi: 10.1007/BF00364338. [DOI] [PubMed] [Google Scholar]
  28. Wilson T., Treisman R. Removal of poly(A) and consequent degradation of c-fos mRNA facilitated by 3' AU-rich sequences. Nature. 1988 Nov 24;336(6197):396–399. doi: 10.1038/336396a0. [DOI] [PubMed] [Google Scholar]
  29. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

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