scholarly journals Gelsolin expression increases β1-integrin affinity and L1210 cell adhesion

Cytoskeleton ◽  
2013 ◽  
Vol 70 (7) ◽  
pp. 385-393 ◽  
Author(s):  
Jeroen D. Langereis ◽  
Leo Koenderman ◽  
Anna Huttenlocher ◽  
Laurien H. Ulfman
Keyword(s):  
Cell Adhesion ◽  
L1210 Cell ◽  
Β1 Integrin

Differences in phosphatase modulation of α4 β1 and α5 β1 integrin-mediated adhesion and migration of B16F1 cells

1999 ◽  
Vol 77 (5) ◽  
pp. 409-420 ◽  
Author(s):  
Dolores Hangan-Steinman ◽  
Wai-chi Ho ◽  
Priti Shenoy ◽  
Bosco MC Chan ◽  
Vincent L Morris
Keyword(s):  
Cell Adhesion ◽  
Adhesive Strength ◽  
Cell Movement ◽  
Protein Tyrosine Phosphatases ◽  
Β1 Integrin ◽  
Phosphatase Inhibitors ◽  
Β1 Integrins ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
B16f1 Cell

It is well established that a biphasic relationship exists between the adhesive strength of β1 integrins and their ability to mediate cell movement. Thus, cell movement increases progressively with adhesive strength, but beyond a certain point of optimal interaction, cell movement is reduced with further increases in adhesive function. The interplay between the various kinase and phosphatase activities provides the balance in β1 integrin-mediated cell adhesion and migration. In the present study, the significance of protein tyrosine phosphatases (PTP) and ser/thr protein phosphatases (PP) in α4β1 and α5β1 integrin-mediated mouse melanoma B16F1 cell anchorage and migration on fibronectin was characterized using phosphatase inhibitors. At low fibronectin concentration, α5β1 functioned as the predominant receptor for cell movement; a role for α4β1 in B16F1 cell migration increased progressively with fibronectin concentration. Treatment of B16F1 cells with PTP inhibitors, sodium orthovanadate (Na3VO4) and phenylarsine oxide (PAO), or PP-1/2A inhibitor, okadaic acid (OA), abolished cell movement. Inhibition of cell movement by PAO and OA was associated by a reduction in the adhesive strength of α4β1 and α5β1. In contrast, treatment of B16F1 cells with Na3VO4 resulted in selective stimulation of the adhesive function of α5β1, but not α4β1. Therefore, our results demonstrate that (i) both PTP and PP-1/2A have roles in cell movement, (ii) modulation of cell movement by PTP and PP-1/2A may involve either a stimulation or reduction of β1 integrin adhesive strength, and (iii) distinct phosphatase-mediated signaling pathways for differential regulation of the various β1 integrins exist. Key words: phosphatases, integrins, cell movement, cell adhesion.

scholarly journals JAK2-V617F activates β1-integrin-mediated adhesion of granulocytes to vascular cell adhesion molecule 1

Leukemia ◽  
2017 ◽  
Vol 31 (5) ◽  
pp. 1223-1226 ◽  
Author(s):  
N Gupta ◽  
B Edelmann ◽  
T M Schnoeder ◽  
F C Saalfeld ◽  
D Wolleschak ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Jak2 V617f ◽  
Β1 Integrin ◽  
Vascular Cell Adhesion ◽  
Vascular Cell ◽  
Vascular Cell Adhesion Molecule ◽  
Cell Adhesion Molecule 1

Podoplanin suppresses the cell adhesion of epidermal keratinocytes via functional regulation of β1-integrin

2018 ◽  
Vol 311 (1) ◽  
pp. 45-53 ◽  
Author(s):  
Takashi Shibuya ◽  
Masaru Honma ◽  
Mizue Fujii ◽  
Shin Iinuma ◽  
Akemi Ishida-Yamamoto
Keyword(s):  
Cell Adhesion ◽  
Epidermal Keratinocytes ◽  
Β1 Integrin ◽  
Functional Regulation

scholarly journals CD13 tethers the IQGAP1-ARF6-EFA6 complex to the plasma membrane to promote ARF6 activation, β1 integrin recycling, and cell migration

2019 ◽  
Vol 12 (579) ◽  
pp. eaav5938 ◽  
Author(s):  
Mallika Ghosh ◽  
Robin Lo ◽  
Ivan Ivic ◽  
Brian Aguilera ◽  
Veneta Qendro ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Migration ◽  
Cell Adhesion ◽  
Cell Attachment ◽  
Leading Edge ◽  
Small Gtpase ◽  
Β1 Integrin ◽  
Recycling Endosomes ◽  
Cellular Processes ◽  
Early Endosomes

Cell attachment to the extracellular matrix (ECM) requires a balance between integrin internalization and recycling to the surface that is mediated by numerous proteins, emphasizing the complexity of these processes. Upon ligand binding in various cells, the β1 integrin is internalized, traffics to early endosomes, and is returned to the plasma membrane through recycling endosomes. This trafficking process depends on the cyclical activation and inactivation of small guanosine triphosphatases (GTPases) by their specific guanine exchange factors (GEFs) and their GTPase-activating proteins (GAPs). In this study, we found that the cell surface antigen CD13, a multifunctional transmembrane molecule that regulates cell-cell adhesion and receptor-mediated endocytosis, also promoted cell migration and colocalized with β1 integrin at sites of cell adhesion and at the leading edge. A lack of CD13 resulted in aberrant trafficking of internalized β1 integrin to late endosomes and its ultimate degradation. Our data indicate that CD13 promoted ARF6 GTPase activity by positioning the ARF6-GEF EFA6 at the cell membrane. In migrating cells, a complex containing phosphorylated CD13, IQGAP1, GTP-bound (active) ARF6, and EFA6 at the leading edge promoted the ARF6 GTPase cycling and cell migration. Together, our findings uncover a role for CD13 in the fundamental cellular processes of receptor recycling, regulation of small GTPase activities, cell-ECM interactions, and cell migration.

scholarly journals Integrin α2β1 Is a Receptor for the Cartilage Matrix Protein Chondroadherin

1997 ◽  
Vol 138 (5) ◽  
pp. 1159-1167 ◽  
Author(s):  
Lisbet Camper ◽  
Dick Heinegård ◽  
Evy Lundgren-Åkerlund
Keyword(s):  
Cell Adhesion ◽  
Matrix Protein ◽  
Collagen Type ◽  
Human Fibroblasts ◽  
Cartilage Matrix ◽  
Affinity Column ◽  
Integrin Subunit ◽  
Β1 Integrin ◽  
Type Ii ◽  
Collagen Type Ii

Chondroadherin (the 36-kD protein) is a leucine-rich, cartilage matrix protein known to mediate adhesion of isolated chondrocytes. In the present study we investigated cell surface proteins involved in the interaction of cells with chondroadherin in cell adhesion and by affinity purification. Adhesion of bovine articular chondrocytes to chondroadherin-coated dishes was dependent on Mg2+ or Mn2+ but not Ca2+. Adhesion was partially inhibited by an antibody recognizing β1 integrin subunit. Chondroadherin-binding proteins from chondrocyte lysates were affinity purified on chondroadherin-Sepharose. The β1 integrin antibody immunoprecipitated two proteins with molecular mass ∼110 and 140 kD (nonreduced) from the EDTA-eluted material. These results indicate that a β1 integrin on chondrocytes interacts with chondroadherin. To identify the α integrin subunit(s) involved in interaction of cells with the protein, we affinity purified chondroadherin-binding membrane proteins from human fibroblasts. Immunoprecipitation of the EDTA-eluted material from the affinity column identified α2β1 as a chondroadherin-binding integrin. These results are in agreement with cell adhesion experiments where antibodies against the integrin subunit α2 partially inhibited adhesion of human fibroblast and human chondrocytes to chondroadherin. Since α2β1 also is a receptor for collagen type II, we tested the ability of different antibodies against the α2 subunit to inhibit adhesion of T47D cells to collagen type II and chondroadherin. The results suggested that adhesion to collagen type II and chondroadherin involves similar or nearby sites on the α2β1 integrin. Although α2β1 is a receptor for both collagen type II and chondroadherin, only adhesion of cells to collagen type II was found to mediate spreading.

High dose fractionated ionizing radiation inhibits prostate cancer cell adhesion and β1 integrin expression

The Prostate ◽  
2005 ◽  
Vol 64 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Edmund L. Simon ◽  
Hira L. Goel ◽  
Natalia Teider ◽  
Tao Wang ◽  
Lucia R. Languino ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Ionizing Radiation ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
High Dose ◽  
Β1 Integrin ◽  
Integrin Expression ◽  
Cancer Cell Adhesion

scholarly journals Alkaline ceramidase 2 regulates β1 integrin maturation and cell adhesion

2008 ◽  
Vol 23 (2) ◽  
pp. 656-666 ◽  
Author(s):  
Wei Sun ◽  
Wei Hu ◽  
Ruijuan Xu ◽  
Junfei Jin ◽  
Zdzislaw M. Szulc ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Β1 Integrin

scholarly journals CD44 and β1 Integrin Mediate Ovarian Carcinoma Cell Adhesion to Peritoneal Mesothelial Cells

1999 ◽  
Vol 154 (5) ◽  
pp. 1525-1537 ◽  
Author(s):  
Khashayar Lessan ◽  
Dean J. Aguiar ◽  
Theodore Oegema ◽  
Lisa Siebenson ◽  
Amy P.N. Skubitz
Keyword(s):  
Cell Adhesion ◽  
Ovarian Carcinoma ◽  
Carcinoma Cell ◽  
Mesothelial Cells ◽  
Β1 Integrin ◽  
Peritoneal Mesothelial Cells
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