scholarly journals The LG3 Module of Laminin-5 Harbors a Binding Site for Integrin α3β1That Promotes Cell Adhesion, Spreading, and Migration

2001 ◽  
Vol 276 (35) ◽  
pp. 33045-33053 ◽  
Author(s):  
Meiling Shang ◽  
Naohiko Koshikawa ◽  
Susann Schenk ◽  
Vito Quaranta
Keyword(s):  
Cell Adhesion ◽  
Binding Site ◽  
Laminin 5 ◽  
And Migration

scholarly journals Connective tissue growth factor with a novel fibronectin binding site promotes cell adhesion and migration during rat oval cell activation

Hepatology ◽  
2007 ◽  
Vol 47 (3) ◽  
pp. 996-1004 ◽  
Author(s):  
Liya Pi ◽  
Xiaodong Ding ◽  
Marda Jorgensen ◽  
Jen-Jung Pan ◽  
Seh-Hoon Oh ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Growth Factor ◽  
Connective Tissue ◽  
Binding Site ◽  
Cell Activation ◽  
Tissue Growth ◽  
Oval Cell ◽  
Cell Adhesion And Migration ◽  
Fibronectin Binding ◽  
And Migration

scholarly journals Structural Requirement of Carboxyl-terminal Globular Domains of Laminin α3 Chain for Promotion of Rapid Cell Adhesion and Migration by Laminin-5

2000 ◽  
Vol 275 (29) ◽  
pp. 22495-22502 ◽  
Author(s):  
Tomomi Hirosaki ◽  
Hiroto Mizushima ◽  
Yoshiaki Tsubota ◽  
Kayano Moriyama ◽  
Kaoru Miyazaki
Keyword(s):  
Cell Adhesion ◽  
Structural Requirement ◽  
Laminin 5 ◽  
Cell Adhesion And Migration ◽  
Carboxyl Terminal ◽  
And Migration

scholarly journals The Short Arm of Laminin γ2 Chain of Laminin-5 (Laminin-332) Binds Syndecan-1 and Regulates Cellular Adhesion and Migration by Suppressing Phosphorylation of Integrin β4 Chain

2007 ◽  
Vol 18 (5) ◽  
pp. 1621-1633 ◽  
Author(s):  
Takashi Ogawa ◽  
Yoshiaki Tsubota ◽  
Junko Hashimoto ◽  
Yoshinobu Kariya ◽  
Kaoru Miyazaki
Keyword(s):  
Cell Adhesion ◽  
Cellular Adhesion ◽  
Proteolytic Processing ◽  
Laminin 5 ◽  
Integrin Β4 ◽  
A Cell ◽  
Adhesion Activity ◽  
And Migration ◽  
Sequence Domain ◽  
Domain V

The proteolytic processing of laminin-5 at the short arm of the γ2 chain (γ2sa) is known to convert this laminin from a cell adhesion type to a motility type. Here, we studied this mechanism by analyzing the functions of γ2sa. In some immortalized or tumorigenic human cell lines, a recombinant γ2sa, in either soluble or insoluble (coated) form, promoted the adhesion of these cells to the processed laminin-5 (Pr-LN5), and it suppressed their migration stimulated by serum or epidermal growth factor (EGF). γ2sa also suppressed EGF-induced tyrosine phosphorylation of integrin β4 and resultant disruption of hemidesmosome-like structures in keratinocytes. γ2sa bound to syndecan-1, and this binding, as well as its cell adhesion activity, was blocked by heparin. By analyzing the activities of three different γ2sa fragments, the active site of γ2sa was localized to the NH2-terminal EGF-like sequence (domain V or LEa). Suppression of syndecan-1 expression by the RNA interference effectively blocked the activities of domain V capable of promoting cell adhesion and inhibiting the integrin β4 phosphorylation. These results demonstrate that domain V of the γ2 chain negatively regulates the integrin β4 phosphorylation, probably through a syndecan-1–mediated signaling, leading to enhanced cell adhesion and suppressed cell motility.

scholarly journals The Short Arm of the Laminin γ2 Chain Plays a Pivotal Role in the Incorporation of Laminin 5 into the Extracellular Matrix and in Cell Adhesion

2001 ◽  
Vol 153 (4) ◽  
pp. 835-850 ◽  
Author(s):  
Laurent Gagnoux-Palacios ◽  
Maryline Allegra ◽  
Flavia Spirito ◽  
Olivier Pommeret ◽  
Christine Romero ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Attachment ◽  
Biologically Active ◽  
Globular Domain ◽  
Stimulated Scattering ◽  
Laminin 5 ◽  
And Migration ◽  
Immunohistochemical Studies ◽  
Adhesion Ligand

Laminin 5 is a basement membrane component that actively promotes adhesion and migration of epithelial cells. Laminin 5 undergoes extracellular proteolysis of the γ2 chain that removes the NH2-terminal short arm of the polypeptide and reduces the size of laminin 5 from 440 to 400 kD. The functional consequence of this event remains obscure, although lines of evidence indicate that cleavage of the γ2 chain potently stimulated scattering and migration of keratinocytes and cancer cells. To define the biological role of the γ2 chain short arm, we expressed mutated γ2 cDNAs into immortalized γ2-null keratinocytes. By immunofluorescence and immunohistochemical studies, cell detachment, and adhesion assays, we found that the γ2 short arm drives deposition of laminin 5 into the extracellular matrix (ECM) and sustains cell adhesion. Our results demonstrate that the unprocessed 440-kD form of laminin 5 is a biologically active adhesion ligand, and that the γ2 globular domain IV is involved in intermolecular interactions that mediate integration of laminin 5 in the ECM and cell attachment.

scholarly journals Lipogenic signalling modulates prostate cancer cell adhesion and migration via modification of Rho GTPases

Oncogene ◽  
2020 ◽  
Vol 39 (18) ◽  
pp. 3666-3679 ◽  
Author(s):  
Mario De Piano ◽  
Valeria Manuelli ◽  
Giorgia Zadra ◽  
Jonathan Otte ◽  
Per-Henrik D. Edqvist ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cancer Cell ◽  
Rho Gtpases ◽  
Prostate Cancer Cell ◽  
Cancer Cell Adhesion ◽  
Cell Adhesion And Migration ◽  
And Migration

scholarly journals CXCL2-CXCR2 axis mediates αV integrin-dependent peritoneal metastasis of colon cancer cells

2021 ◽  
Author(s):  
Mattias Lepsenyi ◽  
Nader Algethami ◽  
Amr A. Al-Haidari ◽  
Anwar Algaber ◽  
Ingvar Syk ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Adhesion ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Colon Cancer Cell ◽  
Colon Cancer Cells ◽  
Cancer Cell Adhesion ◽  
And Migration ◽  
Cxcr2 Antagonist

AbstractPeritoneal metastasis is an insidious aspect of colorectal cancer. The aim of the present study was to define mechanisms regulating colon cancer cell adhesion and spread to peritoneal wounds after abdominal surgery. Mice was laparotomized and injected intraperitoneally with CT-26 colon carcinoma cells and metastatic noduli in the peritoneal cavity was quantified after treatment with a CXCR2 antagonist or integrin-αV-antibody. CT-26 cells expressed cell surface chemokine receptors CXCR2, CXCR3, CXCR4 and CXCR5. Stimulation with the CXCR2 ligand, CXCL2, dose-dependently increased proliferation and migration of CT-26 cells in vitro. The CXCR2 antagonist, SB225002, dose-dependently decreased CXCL2-induced proliferation and migration of colon cancer cells in vitro. Intraperitoneal administration of CT-26 colon cancer cells resulted in wide-spread growth of metastatic nodules at the peritoneal surface of laparotomized animals. Laparotomy increased gene expression of CXCL2 at the incisional line. Pretreatment with CXCR2 antagonist reduced metastatic nodules by 70%. Moreover, stimulation with CXCL2 increased CT-26 cell adhesion to extracellular matrix (ECM) proteins in a CXCR2-dependent manner. CT-26 cells expressed the αV, β1 and β3 integrin subunits and immunoneutralization of αV abolished CXCL2-triggered adhesion of CT-26 to vitronectin, fibronectin and fibrinogen. Finally, inhibition of the αV integrin significantly attenuated the number of carcinomatosis nodules by 69% in laparotomized mice. These results were validated by use of the human colon cancer cell line HT-29 in vitro. Our data show that colon cancer cell adhesion and growth on peritoneal wound sites is mediated by a CXCL2-CXCR2 signaling axis and αV integrin-dependent adhesion to ECM proteins.

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