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PMID: 2530588 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Expression of CD45 alters phosphorylation of the lck-encoded tyrosine protein kinase in murine lymphoma T-cell lines.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 22 ·1989-11-00 ·Pages 8959-63

Ostergaard HL, Shackelford DA, Hurley TR, Johnson P, Hyman R, Sefton BM, Trowbridge IS

Abstract

CD45 is a family of high molecular weight leukocyte cell surface glycoproteins. Recently, two related subregions of the cytoplasmic domain of CD45 have been shown to have 30-40% amino acid identity with a human placental protein phosphotyrosine phosphatase, and CD45 isolated from human spleen was found to exhibit intrinsic protein phosphotyrosine phosphatase (EC 3.1.3.48) activity. In the present studies, we demonstrate that each of the known isoforms of murine CD45 has an equivalent basal level of protein phosphotyrosine phosphatase activity and establish that this enzymatic activity is associated with the cytoplasmic domain of the glycoprotein. Studies with three independent sets of well-characterized parental CD45+, mutant CD45-, and revertant CD45+ lymphoma cell lines indicate that loss of CD45 increases the phosphorylation of the src-related leukocyte-specific tyrosine protein kinase p56lck on tyrosine-505, a putative negative regulatory site. This suggests that CD45 may play a role in leukocyte growth regulation by altering the kinase activity of p56lck.

MeSH Terms
Animals Antigens, Differentiation/genetics,immunology Cell Line Gene Expression Histocompatibility Antigens/genetics,immunology Immunoblotting Kinetics Leukocyte Common Antigens Lymphocyte Activation Lymphoma/enzymology,immunology Membrane Glycoproteins/genetics Mice Mutation Peptide Fragments/isolation & purification Phosphorylation Protein-Tyrosine Kinases/genetics,metabolism T-Lymphocytes/enzymology,immunology Trypsin
Chemicals
Antigens, Differentiation Histocompatibility Antigens Membrane Glycoproteins Peptide Fragments Protein-Tyrosine Kinases Leukocyte Common Antigens Trypsin
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Ostergaard H L
Department of Cancer Biology, Salk Institute, San Diego, CA 92138.
Shackelford D A
Hurley T R
Johnson P
Hyman R
Sefton B M
Trowbridge I S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.22.8959
Published
1989-11-00
Pages
8959-63
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298410
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.86.22.8959 PMC Full Text View journal details
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