Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology (Q28211362)

CD148, a membrane protein tyrosine phosphatase, is able to induce tyrosine phosphorylation on human lymphocytes.

Europe PubMed Central

title

Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology (English)

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main subject

transmembrane protein

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2

Louis B Justement

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author name string

Thomas R Harrod

series ordinal

1

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language of work or name

English

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publication date

2002

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published in

Immunologic Research

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volume

26

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issue

1-3

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page(s)

153-66

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cites work

1 reference

12 December 2020

Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1

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CD148: a receptor-type protein tyrosine phosphatase involved in the regulation of human T cell activation

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Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation

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Expression on human eosinophils of CD148: a membrane tyrosine phosphatase. Implications in the effector function of eosinophils

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The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells.

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Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1).

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Expression of the membrane protein tyrosine phosphatase CD148 in human tissues

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Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed in macrophages and is regulated by CSF-1 and LPS.

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Orthovanadate both mimics and antagonizes the transforming growth factor beta action on normal rat kidney cells.

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Syntenin, a PDZ protein that binds syndecan cytoplasmic domains

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The activation of the phosphotyrosine phosphatase eta (r-PTP eta) is responsible for the somatostatin inhibition of PC Cl3 thyroid cell proliferation

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Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1.

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Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density

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Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148

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Identification of functional human splenic memory B cells by expression of CD148 and CD27.

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Novel molecular mechanisms of dendritic cell-induced T cell activation.

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The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase

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From sentinel to messenger: an extended phenotypic analysis of the monocyte to dendritic cell transition

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An extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1.

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CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes

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Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta

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Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin

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Cloning and characterization of rat density-enhanced phosphatase-1, a protein tyrosine phosphatase expressed by vascular cells

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Thyroid cell transformation inhibits the expression of a novel rat protein tyrosine phosphatase

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Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments

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Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein

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Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins

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Functional characterization of receptor-type protein tyrosine phosphatase CD148 (HPTP eta/DEP-1) in Fc gamma receptor IIa signal transduction of human neutrophils

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12 December 2020