10 results match your criteria lacking ptprj

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PTPRJ promotes osteoclast maturation and activity by inhibiting Cbl-mediated ubiquitination of NFATc1 in late osteoclastogenesis.

FEBS J 2021 08 5;288(15):4702-4723. Epub 2021 Mar 5.

Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot, Israel.

Bone-resorbing osteoclasts (OCLs) are multinucleated phagocytes, whose central roles in regulating bone formation and homeostasis are critical for normal health and development. OCLs are produced from precursor monocytes in a multistage process that includes initial differentiation, cell-cell fusion, and subsequent functional and morphological maturation; the molecular regulation of osteoclastogenesis is not fully understood. Here, we identify the receptor-type protein tyrosine phosphatase PTPRJ as an essential regulator specifically of OCL maturation. Read More

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CD148 tyrosine phosphatase promotes cadherin cell adhesion.

PLoS One 2014 11;9(11):e112753. Epub 2014 Nov 11.

Department of Medicine, Vanderbilt University School of Medicine, Nashville, TN, United States of America; Department of Cancer Biology, Vanderbilt University School of Medicine, Nashville, TN, United States of America.

CD148 is a transmembrane tyrosine phosphatase that is expressed at cell junctions. Recent studies have shown that CD148 associates with the cadherin/catenin complex and p120 catenin (p120) may serve as a substrate. However, the role of CD148 in cadherin cell-cell adhesion remains unknown. Read More

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The phosphatase CD148 promotes airway hyperresponsiveness through SRC family kinases.

J Clin Invest 2013 May 1;123(5):2037-48. Epub 2013 Apr 1.

Division of Rheumatology and Rosalind Russell Medical Research Center for Arthritis, University of California San Francisco (UCSF), San Francisco, California, USA.

Increased airway smooth muscle (ASM) contractility and the development of airway hyperresponsiveness (AHR) are cardinal features of asthma, but the signaling pathways that promote these changes are poorly understood. Tyrosine phosphorylation is tightly regulated by the opposing actions of protein tyrosine kinases and phosphatases, but little is known about whether tyrosine phosphatases influence AHR. Here, we demonstrate that genetic inactivation of receptor-like protein tyrosine phosphatase J (Ptprj), which encodes CD148, protected mice from the development of increased AHR in two different asthma models. Read More

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Receptor tyrosine phosphatases control tracheal tube geometries through negative regulation of Egfr signaling.

Mili Jeon Kai Zinn

Development 2009 Sep 12;136(18):3121-9. Epub 2009 Aug 12.

Broad Center, Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.

The formation of epithelial tubes with defined shapes and sizes is essential for organ development. We describe a unique tracheal tubulogenesis phenotype caused by loss of both Drosophila type III receptor tyrosine phosphatases (RPTPs), Ptp4E and Ptp10D. Ptp4E is the only widely expressed Drosophila RPTP, and is the last of the six fly RPTPs to be genetically characterized. Read More

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September 2009

Proteomic analysis of malignant B-cell derived microparticles reveals CD148 as a potentially useful antigenic biomarker for mantle cell lymphoma diagnosis.

J Proteome Res 2009 Jul;8(7):3346-54

Laboratoire de Spectrometrie de Masse Bio-Organique, IPHC-DSA, UDS, CNRS, UMR7178, ECPM 25 rue Becquerel, 67087 Strasbourg, France.

The diagnosis of mature B-cell neoplasms (MBCN) remains difficult in a number of cases, especially leukemic phases of non-Hodgkin lymphoma, for which discriminating criteria or biomarker are often lacking. To identify new surface biomarkers, we developed an original proteomic approach based on mass spectrometry analysis of plasma membrane microparticles derived from chronic B-cell lymphoproliferations of single patients: chronic lymphocytic leukemia (CLL), small cell lymphoma (SLL) and mantle cell lymphoma (MCL). A straightforward selection process for proteomic-based candidate biomarker identification was further constructed in order to propose potentially useful and relevant biomarkers. Read More

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The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis.

Blood 2009 May 25;113(20):4942-54. Epub 2009 Feb 25.

Centre for Cardiovascular Sciences, Institute of Biomedical Research, University of Birmingham, United Kingdom.

Platelets play a fundamental role in hemostasis and thrombosis. They are also involved in pathologic conditions resulting from blocked blood vessels, including myocardial infarction and ischemic stroke. Platelet adhesion, activation, and aggregation at sites of vascular injury are regulated by a diverse repertoire of tyrosine kinase-linked and G protein-coupled receptors. Read More

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Angiocentric glioma: report of clinico-pathologic and genetic findings in 8 cases.

Am J Surg Pathol 2007 Nov;31(11):1709-18

Institute of Neurology, Medical University of Vienna, Vienna, Austria.

Angiocentric glioma has recently been described as a novel epilepsy associated tumor with distinct clinico-pathologic features. We report the clinical and pathologic findings in 8 additional cases of this rare tumor type and extend its characterization by genomic profiling. Almost all patients had a history of long-standing drug-resistant epilepsy. Read More

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November 2007

The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn).

Oncogene 2002 Oct;21(46):7067-76

SUGEN Inc., 230 East Grand Avenue, South San Francisco, California, CA 94080, USA.

The receptor-like protein tyrosine phosphatase DEP1, also known as CD148, is expressed predominantly in epithelial cells, in a variety of tumor cell lines, and in lymphocytes. Expression of DEP1 is enhanced at high cell density, and this observation suggests that DEP1 may function in the regulation of cell adhesion and possibly contact inhibition of cell growth. In order to investigate the function of DEP1, substrate-trapping mutants of the phosphatase were used to identify potential substrates. Read More

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October 2002

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

Oncogene 2001 Aug;20(37):5219-24

Ludwig Institute for Cancer Research, Box 595, S-751 24 Uppsala, Sweden.

Cellular growth, differentiation and migration is regulated by protein tyrosine phosphorylation. Receptor-like protein tyrosine phosphatases are thus likely to be key regulators of vital cellular processes. The regulation of these enzymes is in general poorly understood. Read More

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Expression of the protein tyrosine phosphatase beta2 gene in mouse erythroleukemia cells induces terminal erythroid differentiation.

J Biol Chem 1996 Nov;271(48):30916-21

Institute of Molecular and Cellular Biosciences, University of Tokyo, Bunkyo-ku 113, Tokyo, Japan.

We have cloned cDNA for protein tyrosine phosphatase beta2, which had been implicated in erythroid differentiation of mouse erythroleukemia cells. Expression of cDNA constructs, in which beta2 cDNA is placed under the control of mouse metallothionein-I promoter, by ZnCl2 converted a significant portion (20 to 38%) of the cells to erythroid-like cells, which is 25-50% of the erythroid differentiation efficiency observed by conventional erythroid-inducing agents. Furthermore, introduction and expression of altered protein tyrosine phosphatase beta2 cDNA constructs designed to produce the enzyme lacking the phosphatase activity inhibited erythroid differentiation by 100-20%, depending upon the concentration of erythroid-inducing agents employed. Read More

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November 1996
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