Structure and Function of CD45: A Leukocyte-Specific Protein Tyrosine Phosphatase

  • Ian S. Trowbridge
  • Pauline Johnson
  • Hanne Ostergaard
  • Nicholas Hole
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 323)


CD45 is a large abundant leukocyte-specific cell surface glycoprotein 1. It is structurally heterogeneous consisting of a family of isoforms (Mr ~ 180-220K) that are distributed in characteristic cell-type specific patterns on different leukocyte sUbpopulations. Because of its leukocyte-specific tissue distribution, CD45 is a useful marker for the differential diagnosis of undifferentiated lymphoma 2. The primary structures of rat, mouse and human CD45 deduced from cDNA sequencing in the mid-1980’s revealed that the cytoplasmic domain of CD45 was unusually large 1, confirming earlier studies of a mutant CD45 molecule 3. Charbonneau et al. showed in 1988 that two tandem imperfect repeats within the large cytoplasmic domain of CD45 had highly significant sequence similarity with PTP1B, a soluble ~37K human placental protein tyrosine phosphatase (PTP) 4. Subsequently, CD45 was shown to have intrinsic PTP activity 5, suggesting that transmembrane PTPs might represent a novel class of receptors that oppose the action of protein tyrosine kinases (PTKs) and playa fundamental role in the regulation of cell growth and differentiation. Other putative transmembrane and intracellular PTPs in organisms as diverse as higher eukaryotes, Drosophila, yeast, bacteria, and viruses have now been identified and the complete primary structures of at least twenty PTPs have been determined (reviewed in Ref 6). CD45 is the best characterized of the transmembrane PTPs and serves as a prototype for this class of enzyme. An understanding of the function of CD45 in leukocyte physiology requires identification of its substrates, elucidation of the structuralfeatures of the molecule essential for PTP activity, and information about how its activity is regulated. This paper will review recent progress in defining the role of CD45 in lymphocyte signal transduction and summarize the current status of the rapidly growing PTP family.


Protein Tyrosine Phosphatase Leukocyte Common Antigen External Domain Murine CD45 Protein Tyrosine Phosphatase Activity 
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Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Ian S. Trowbridge
    • 1
  • Pauline Johnson
    • 1
    • 2
  • Hanne Ostergaard
    • 1
    • 3
  • Nicholas Hole
    • 1
    • 4
  1. 1.Department of Cancer BiologyThe Salk InstituteSan DiegoUSA
  2. 2.Department of MicrobiologyUniversity of British ColumbiaVancouverCanada
  3. 3.Department of ImmunobiologyUniversity of AlbertaEdmontonCanada
  4. 4.AFRC Center for Animal Genome ResearchUniversity of EdinburghEdinburghUK

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