The cytoplasmic tail of CD45 is released from activated phagocytes and can act as an inhibitory messenger for T cells

Author:

Kirchberger Stefanie1,Majdic Otto1,Blüml Stefan1,Schrauf Catharina1,Leitner Judith1,Gerner Christopher2,Paster Wolfgang3,Gundacker Nina2,Sibilia Maria2,Stöckl Johannes1

Affiliation:

1. Institute of Immunology,

2. Institute of Cancer Research, and

3. Department of Molecular Immunology, Medical University of Vienna, Vienna, Austria

Abstract

AbstractCD45 is the prototypic transmembrane protein tyrosine phosphatase (PTP), which is expressed on all nucleated hematopoietic cells and plays a central role in the integration of environmental signals into immune cell responses. Here we report an alternative function for the intracellular domain of CD45. We dis-covered that CD45 is sequentially cleaved by serine/metalloproteinases and γ-secretases during activation of human monocytes and granulocytes by fungal stimuli or phorbol 12-myristate 13-acetate but not by other microbial stimuli. Proteolytic processing of CD45 occurred upon activation of monocytes or granulocytes but not of T cells, B cells, or dendritic cells and resulted in a 95-kDa fragment of the cytoplasmic tail of CD45 (ct-CD45). ct-CD45 was released from monocytes and granulocytes upon activation-induced cell death. Binding studies with ct-CD45 revealed a counter-receptor on preactivated T cells. Moreover, T-cell proliferation induced by dendritic cells or CD3 antibodies was inhibited in the presence of ct-CD45. Taken together, the results of our study demonstrate that fragments of the intracellular domain of CD45 from human phagocytes can function as intercellular regulators of T-cell activation.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

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