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Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes

Torimoto, Y, Dang, N H, Vivier, E, Tanaka, T, Schlossman, S F, Morimoto, C·1991·The Journal of Immunology

Abstract

In the present report, we demonstrated that modulation of CD26 from T cell surface induced by antiCD26 (1F7) led to enhanced phosphorylation of CD3 zeta tyrosine residues and increased CD4 associated p56lck tyrosine kinase activity. We further showed that CD26 was comodulated on the T cell surface with CD45, a known membrane-linked protein tyrosine phosphatase and that anti-CD26 was capable of precipitating CD45 from T cell lysates. These findings strongly suggest that CD26 may be closely associated with the CD45 protein tyrosine phosphatase on T cell surface and further support the notion that the interaction of CD26 with CD45 results in enhanced tyrosine kinase activity, zeta chain phosphorylation, and T cell activation.

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Metadata

Authors
Torimoto, Y., Dang, N. H., Vivier, E., Tanaka, T., Schlossman, S. F., & Morimoto, C.
Venue
The Journal of Immunology
Published
1991-10
Volume
147
Issue
8
Pages
2514-2517
ISSN
  • 0022-1767 (ISSN-L)
  • 1550-6606
OpenAlex
W2098511235
Cited by
206
References
0
FWCI
3.55
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes. https://app.cochat.ai/papers/10.4049/jimmunol.147.8.2514
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Torimoto, Y., Dang, N. H., Vivier, E., Tanaka, T., Schlossman, S. F., & Morimoto, C. (1991). Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes. The Journal of Immunology. https://doi.org/10.4049/jimmunol.147.8.2514

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.