scholarly journals Syndecan-2 is a novel ligand for the protein tyrosine phosphatase receptor CD148

2011 ◽  
Vol 22 (19) ◽  
pp. 3609-3624 ◽  
Author(s):  
James R. Whiteford ◽  
Xiaojie Xian ◽  
Claire Chaussade ◽  
Bart Vanhaesebroeck ◽  
Sussan Nourshargh ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Transmembrane Domain ◽  
Core Protein ◽  
Tyrosine Phosphatase ◽  
Β1 Integrin ◽  
Potential Implication ◽  
Protein Tyrosine ◽  
Cellular Processes ◽  
A Cell

Syndecan-2 is a heparan sulfate proteoglycan that has a cell adhesion regulatory domain contained within its extracellular core protein. Cell adhesion to the syndecan-2 extracellular domain (S2ED) is β1 integrin dependent; however, syndecan-2 is not an integrin ligand. Here the protein tyrosine phosphatase receptor CD148 is shown to be a key intermediary in cell adhesion to S2ED, with downstream β1 integrin–mediated adhesion and cytoskeletal organization. We show that S2ED is a novel ligand for CD148 and identify the region proximal to the transmembrane domain of syndecan-2 as the site of interaction with CD148. A mechanism for the transduction of the signal from CD148 to β1 integrins is elucidated requiring Src kinase and potential implication of the C2β isoform of phosphatidylinositol 3 kinase. Our data uncover a novel pathway for β1 integrin–mediated adhesion of importance in cellular processes such as angiogenesis and inflammation.

scholarly journals Inhibitory Effects of Secondary Metabolites from the Lichen Stereocaulon evolutum on Protein Tyrosine Phosphatase 1B

Planta Medica ◽  
2021 ◽  
Author(s):  
Birgit Waltenberger ◽  
Françoise Lohézic-Le Dévéhat ◽  
Thi Huyen Vu ◽  
Olivier Delalande ◽  
Claudia Lalli ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Inhibitory Activity ◽  
Tyrosine Phosphatase ◽  
Inhibitory Effect ◽  
Positive Control ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Ic50 Values ◽  
A Cell

AbstractProtein tyrosine phosphatase 1B plays a significant role in type 2 diabetes mellitus and other diseases and is therefore considered a new drug target. Within this study, an acetone extract from the lichen Stereocaulon evolutum was identified to possess strong protein tyrosine phosphatase 1B inhibition in a cell-free assay (IC50 of 11.8 µg/mL). Fractionation of this bioactive extract led to the isolation of seven known molecules belonging to the depsidones and the related diphenylethers and one new natural product, i.e., 3-butyl-3,7-dihydroxy-5-methoxy-1(3H)-isobenzofurane. The isolated compounds were evaluated for their inhibition of protein tyrosine phosphatase 1B. Two depsidones, lobaric acid and norlobaric acid, and the diphenylether anhydrosakisacaulon A potently inhibited protein tyrosine phosphatase 1B with IC50 values of 12.9, 15.1, and 16.1 µM, respectively, which is in the range of the protein tyrosine phosphatase 1B inhibitory activity of the positive control ursolic acid (IC50 of 14.4 µM). Molecular simulations performed on the eight compounds showed that i) a contact between the molecule and the four main regions of the protein is required for inhibitory activity, ii) the relative rigidity of the depsidones lobaric acid and norlobaric acid and the reactivity related to hydrogen bond donors or acceptors, which interact with protein tyrosine phosphatase 1B key amino acids, are involved in the bioactivity on protein tyrosine phosphatase 1B, iii) the cycle opening observed for diphenylethers decreased the inhibition, except for anhydrosakisacaulon A where its double bond on C-8 offsets this loss of activity, iv) the function present at C-8 is a determinant for the inhibitory effect on protein tyrosine phosphatase 1B, and v) the more hydrogen bonds with Arg221 there are, the more anchorage is favored.

scholarly journals Functional Analysis of a Cell Cycle–Associated, Tumor-Suppressive Gene, Protein Tyrosine Phosphatase Receptor Type G, in Nasopharyngeal Carcinoma

2008 ◽  
Vol 68 (19) ◽  
pp. 8137-8145 ◽  
Author(s):  
Arthur Kwok Leung Cheung ◽  
Hong Lok Lung ◽  
Siu Chun Hung ◽  
Evan Wai Lok Law ◽  
Yue Cheng ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Functional Analysis ◽  
Nasopharyngeal Carcinoma ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
A Cell

scholarly journals Regulatory Functions of Protein Tyrosine Phosphatase Receptor Type O in Immune Cells

2021 ◽  
Vol 12 ◽  
Author(s):  
Feiling Xie ◽  
Hongmei Dong ◽  
Hao Zhang
Keyword(s):  
T Cells ◽  
B Cells ◽  
Immune Cells ◽  
Protein Tyrosine Phosphatase ◽  
Molecular Mechanisms ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
Cellular Processes

The members of the protein tyrosine phosphatase (PTP) family are key regulators in multiple signal transduction pathways and therefore they play important roles in many cellular processes, including immune response. As a member of PTP family, protein tyrosine phosphatase receptor type O (PTPRO) belongs to the R3 receptor-like protein tyrosine phosphatases. The expression of PTPRO isoforms is tissue-specific and the truncated PTPRO (PTPROt) is mainly observed in hematopoietic cells, including B cells, T cells, macrophages and other immune cells. Therefore, PTPROt may play an important role in immune cells by affecting their growth, differentiation, activation and immune responses. In this review, we will focus on the regulatory roles and underlying molecular mechanisms of PTPRO/PTPROt in immune cells, including B cells, T cells, and macrophages.

scholarly journals Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn

2009 ◽  
Vol 28 (22) ◽  
pp. 3564-3578 ◽  
Author(s):  
So-Hee Lim ◽  
Seok-Kyu Kwon ◽  
Myung Kyu Lee ◽  
Jeonghee Moon ◽  
Dae Gwin Jeong ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Protein Tyrosine Phosphatase ◽  
Cell Adhesion Molecules ◽  
Synapse Formation ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine

scholarly journals Effects of Overexpression of PTP36, a Putative Protein Tyrosine Phosphatase, on Cell Adhesion, Cell Growth, and Cytoskeletons in HeLa Cells

1999 ◽  
Vol 274 (18) ◽  
pp. 12905-12909 ◽  
Author(s):  
Masato Ogata ◽  
Tsuyoshi Takada ◽  
Yoshiko Mori ◽  
Masatsugu Oh-hora ◽  
Yohzo Uchida ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Growth ◽  
Hela Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Putative Protein

scholarly journals Phospholipase D2 restores endothelial barrier function by promoting PTPN14-mediated VE-cadherin dephosphorylation

2020 ◽  
Vol 295 (22) ◽  
pp. 7669-7685 ◽  
Author(s):  
Panfeng Fu ◽  
Ramaswamy Ramchandran ◽  
Mark Shaaya ◽  
Longshuang Huang ◽  
David L. Ebenezer ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Barrier Function ◽  
Adherens Junctions ◽  
Tyrosine Phosphatase ◽  
Endothelial Barrier ◽  
Endothelial Barrier Function ◽  
Protein Tyrosine ◽  
Adhesion Junctions

Increased permeability of vascular lung tissues is a hallmark of acute lung injury and is often caused by edemagenic insults resulting in inflammation. Vascular endothelial (VE)-cadherin undergoes internalization in response to inflammatory stimuli and is recycled at cell adhesion junctions during endothelial barrier re-establishment. Here, we hypothesized that phospholipase D (PLD)-generated phosphatidic acid (PA) signaling regulates VE-cadherin recycling and promotes endothelial barrier recovery by dephosphorylating VE-cadherin. Genetic deletion of PLD2 impaired recovery from protease-activated receptor-1–activating peptide (PAR-1–AP)-induced lung vascular permeability and potentiated inflammation in vivo. In human lung microvascular endothelial cells (HLMVECs), inhibition or deletion of PLD2, but not of PLD1, delayed endothelial barrier recovery after thrombin stimulation. Thrombin stimulation of HLMVECs increased co-localization of PLD2-generated PA and VE-cadherin at cell-cell adhesion junctions. Inhibition of PLD2 activity resulted in prolonged phosphorylation of Tyr-658 in VE-cadherin during the recovery phase 3 h post-thrombin challenge. Immunoprecipitation experiments revealed that after HLMVECs are thrombin stimulated, PLD2, VE-cadherin, and protein-tyrosine phosphatase nonreceptor type 14 (PTPN14), a PLD2-dependent protein-tyrosine phosphatase, strongly associate with each other. PTPN14 depletion delayed VE-cadherin dephosphorylation, reannealing of adherens junctions, and barrier function recovery. PLD2 inhibition attenuated PTPN14 activity and reversed PTPN14-dependent VE-cadherin dephosphorylation after thrombin stimulation. Our findings indicate that PLD2 promotes PTPN14-mediated dephosphorylation of VE-cadherin and that redistribution of VE-cadherin at adherens junctions is essential for recovery of endothelial barrier function after an edemagenic insult.

scholarly journals Protein tyrosine phosphatase PTP1B in cell adhesion and migration

2013 ◽  
Vol 7 (5) ◽  
pp. 418-423 ◽  
Author(s):  
Carlos O Arregui ◽  
Ángela González ◽  
Juan E Burdisso ◽  
Ana E González Wusener
Keyword(s):  
Cell Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Cell Adhesion And Migration ◽  
And Migration
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