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[Expression of SOCS3 and Pyk2 and their correlation in non-small cell lung cancer].
Zhonghua Bing Li Xue Za Zhi
October 2012
Department of Pathology, the First Affiliated Hospital and College of Basic Sciences, China Medical University, Shenyang 110001, China.
Objective: To investigate the expression of SOCS3 and Pyk2 and their correlations in non-small cell lung cancer (NSCLC).
Methods: The expression of SOCS3 and Pyk2 was detected in 100 cases of NSCLC, human bronchial epithelial cells (HBE) and 6 lung cancer cell lines by immunohistochemistry and immunofluorescence staining. The methylation status of SOCS3 was investigated in A549 cells by methylation-specific PCR.
Pyk2 inhibition of p53 as an adaptive and intrinsic mechanism facilitating cell proliferation and survival.
J Biol Chem
January 2010
Department of Reproductive Medicine, Moores Cancer Center, University of California San Diego, La Jolla, California 92093, USA.
Pyk2 is a cytoplasmic tyrosine kinase related to focal adhesion kinase (FAK). Compensatory Pyk2 expression occurs upon FAK loss in mice. However, the impact of Pyk2 up-regulation remains unclear.
View Article and Find Full Text PDFDynamin reduces Pyk2 Y402 phosphorylation and SRC binding in osteoclasts.
Mol Cell Biol
July 2009
Department of Oral Biology, Indiana University School of Dentistry, 1121 W. Michigan St., DS241, Indianapolis, IN 46202-5186, USA.
Signaling via the Pyk2-Src-Cbl complex downstream of integrins contributes to the assembly, organization, and dynamics of podosomes, which are the transient adhesion complexes of highly motile cells such as osteoclasts and dendritic cells. We previously demonstrated that the GTPase dynamin is associated with podosomes, regulates actin flux in podosomes, and promotes bone resorption by osteoclasts. We report here that dynamin associates with Pyk2, independent of dynamin's GTPase activity, and reduces Pyk2 Y402 phosphorylation in a GTPase-dependent manner, leading to decreased Src binding to Pyk2.
View Article and Find Full Text PDFMutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant cone dystrophy (CORD5) in two Swedish families.
Adv Exp Med Biol
February 2008
Medical and Clinical Genetics, Department of Medical Biosciences, Umeå University, S-901 85 Umeå, Sweden.
Mutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant cone dystrophy (CORD5) in two Swedish families.
Eur J Hum Genet
June 2007
Medical and Clinical Genetics, Department of Medical Biosciences, Umeå University, SE 901 85 Umeå, Sweden.
Autosomal dominant cone dystrophy (CORD5) (MIM 600977) is a rare disease predominantly affecting cone photoreceptors. Here we refine the CORD5 locus previously mapped to 17p13 from 27 to 14.3 cM and identified a missense mutation, Q626H in the phosphatidylinositol transfer (PIT) membrane-associated protein (PITPNM3) (MIM 608921) in two Swedish families.
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