The β3 chain short arm of laminin-332 (laminin-5) induces matrix assembly and cell adhesion activity of laminin-511 (laminin-10)

2007 ◽  
Vol 100 (3) ◽  
pp. 545-556 ◽  
Author(s):  
Yukiko Nakashima ◽  
Yoshinobu Kariya ◽  
Kaoru Miyazaki
Keyword(s):  
Cell Adhesion ◽  
Matrix Assembly ◽  
Laminin 5 ◽  
Adhesion Activity ◽  
Laminin 332

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.

Endothelial-monocyte activating polypeptide II alters fibronectin based endothelial cell adhesion and matrix assembly via alpha5 beta1 integrin

2005 ◽  
Vol 311 (2) ◽  
pp. 229-239 ◽  
Author(s):  
Margaret A. Schwarz ◽  
Hiahua Zheng ◽  
Jie Liu ◽  
Siobhan Corbett ◽  
Roderich E. Schwarz
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
Matrix Assembly ◽  
Beta1 Integrin ◽  
Endothelial Cell Adhesion

scholarly journals Mammalian and Drosophila cells adhere to the laminin α4 LG4 domain through syndecans, but not glypicans

2004 ◽  
Vol 382 (3) ◽  
pp. 933-943 ◽  
Author(s):  
Hironobu YAMASHITA ◽  
Akira GOTO ◽  
Tatsuhiko KADOWAKI ◽  
Yasuo KITAGAWA
Keyword(s):  
Cell Adhesion ◽  
Umbilical Vein ◽  
Heparan Sulphate ◽  
Direct Interaction ◽  
Binding Activity ◽  
Main Body ◽  
Heparin Binding ◽  
Adhesion Activity ◽  
Umbilical Vein Endothelial Cells

We have previously shown that the LG4 (laminin G-like) domain of the laminin α4 chain is responsible for the significantly higher affinity of the α4 chain to heparin than found for other α chains [Yamaguchi, Yamashita, Mori, Okazaki, Nomizu, Beck and Kitagawa (2000) J. Biol. Chem. 275, 29458–29465]; four basic residues were identified to be essential for this activity [Yamashita, Beck and Kitagawa (2004) J. Mol. Biol. 335, 1145–1149]. By creating GST (glutathione S-transferase)-fused LG1, LG2, LG4 and LG5 proteins, we found that only LG4 is active for the adhesion of human HT1080 cells, human umbilical vein endothelial cells and Drosophila haemocytes Kc167 with a half-saturating concentration of 20 μg/ml. Adhesion was counteracted by treatment of the cells with heparin, heparan sulphate and heparitinase I. Upon mutating the four basic residues essential for heparin binding within LG4, the adhesion activity was abolished. Pull-down experiments using glutathione beads/GST-fusion proteins indicate a direct interaction of LG4 with syndecan-4, which might be the major receptor for cell adhesion. Neither the release of glypican-1 by treating human cells with phosphatidylinositol-specific phospholipase C nor targeted knockdown of dally or dally-like protein impaired the cell-adhesion activity. As the LG4–LG5 domain of the α4 chain is cleaved in vivo from the main body of laminin-8 (α4β1γ1), we suggest that the heparan sulphate proteoglycan-binding activity of LG4 is significant in modulating the signalling of Wnt, Decapentaplegic and fibroblast growth factors.

scholarly journals Role of Nectin in Formation of E-Cadherin–based Adherens Junctions in Keratinocytes: Analysis with the N-Cadherin Dominant Negative Mutant

2003 ◽  
Vol 14 (4) ◽  
pp. 1597-1609 ◽  
Author(s):  
Yoshinari Tanaka ◽  
Hiroyuki Nakanishi ◽  
Shigeki Kakunaga ◽  
Noriko Okabe ◽  
Tomomi Kawakatsu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Adherens Junctions ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Adhesion Activity ◽  
Negative Mutant ◽  
E Cadherin ◽  
Cell Cell

E-Cadherin is a Ca2+-dependent cell-cell adhesion molecule at adherens junctions (AJs) of epithelial cells. A fragment of N-cadherin lacking its extracellular region serves as a dominant negative mutant (DN) and inhibits cell-cell adhesion activity of E-cadherin, but its mode of action remains to be elucidated. Nectin is a Ca2+-independent immunoglobulin-like cell-cell adhesion molecule at AJs and is associated with E-cadherin through their respective peripheral membrane proteins, afadin and catenins, which connect nectin and cadherin to the actin cytoskeleton, respectively. We showed here that overexpression of nectin capable of binding afadin, but not a mutant incapable of binding afadin, reduced the inhibitory effect of N-cadherin DN on the cell-cell adhesion activity of E-cadherin in keratinocytes. Overexpressed nectin recruited N-cadherin DN to the nectin-based cell-cell adhesion sites in an afadin-dependent manner. Moreover, overexpression of nectin enhanced the E-cadherin–based cell-cell adhesion activity. These results suggest that N-cadherin DN competitively inhibits the association of the endogenous nectin-afadin system with the endogenous E-cadherin-catenin system and thereby reduces the cell-cell adhesion activity of E-cadherin. Thus, nectin plays a role in the formation of E-cadherin–based AJs in keratinocytes.

scholarly journals Preparation and Evaluation of Polymer Microspheres with Cell Adhesion Activity.

1993 ◽  
Vol 50 (5) ◽  
pp. 417-423 ◽  
Author(s):  
Yuji KASUYA ◽  
Masaki MIYAMOTO ◽  
Kazuhiro SHIMIZU ◽  
Keiji FUJIMOTO ◽  
Akira OTAKA ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Polymer Microspheres ◽  
Adhesion Activity ◽  
Preparation And Evaluation

Tyrosine phosphorylation of p120(ctn) in v-Src transfected L cells depends on its association with E-cadherin and reduces adhesion activity

2001 ◽  
Vol 114 (3) ◽  
pp. 503-512 ◽  
Author(s):  
M. Ozawa ◽  
T. Ohkubo
Keyword(s):  
Cell Adhesion ◽  
Complex Formation ◽  
Tyrosine Phosphorylation ◽  
Chimeric Protein ◽  
Single Amino Acid ◽  
Membrane Localization ◽  
Wild Type ◽  
L Cells ◽  
Adhesion Activity ◽  
E Cadherin

Cadherins are transmembrane glycoproteins involved in Ca2+-dependent cell-cell adhesion. Using L cells expressing one of three functional E-cadherin constructs, the wild-type, a chimeric molecule with alpha-catenin (EalphaC), and a tail-less one, we determined the effect of v-Src expression on E-cadherin-mediated adhesion. The aggregation of L cells expressing the wild-type or EalphaC chimeric protein, which both interact with p120(ctn), was reduced by v-Src expression, whereas that of L cells expressing the tail-less E-cadherin was not affected by the expression. Tyrosine phosphorylation of p120(ctn) was observed in v-Src-transformed L cells expressing the wild-type or EalphaC chimeric protein, but not in ones expressing the tail-less E-cadherin. Thus, tyrosine phosphorylation of p120(ctn) depends on the complex formation with E-cadherin and the resulting membrane localization. Constitutive phosphorylation of p120(ctn) on serine and threonine residues also depends on the complex formation and membrane localization. Coexpression of the p120(ctn) protein with an N-terminal deletion, which eliminates some potential tyrosine phosphorylation sites, or the protein with a single amino acid substitution (tyrosine at 217 to phenylalanine) resulted in an increase in the aggregation of v-Src-transformed EL and EalphaCL cells. These results indicate that tyrosine phosphorylation of p120(ctn) is involved in the v-Src modulation of E-cadherin-mediated cell adhesion.

scholarly journals BMP-1 disrupts cell adhesion and enhances TGF-β activation through cleavage of the matricellular protein thrombospondin-1

2020 ◽  
Vol 13 (639) ◽  
pp. eaba3880 ◽  
Author(s):  
Cyril Anastasi ◽  
Patricia Rousselle ◽  
Maya Talantikite ◽  
Agnès Tessier ◽  
Caroline Cluzel ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Substantial Effect ◽  
Matricellular Protein ◽  
Matrix Assembly ◽  
Morphogenetic Protein ◽  
Thrombospondin 1

Bone morphogenetic protein 1 (BMP-1) is an important metalloproteinase that synchronizes growth factor activation with extracellular matrix assembly during morphogenesis and tissue repair. The mechanisms by which BMP-1 exerts these effects are highly context dependent. Because BMP-1 overexpression induces marked phenotypic changes in two human cell lines (HT1080 and 293-EBNA cells), we investigated how BMP-1 simultaneously affects cell-matrix interactions and growth factor activity in these cells. Increasing BMP-1 led to a loss of cell adhesion that depended on the matricellular glycoprotein thrombospondin-1 (TSP-1). BMP-1 cleaved TSP-1 between the VWFC/procollagen-like domain and the type 1 repeats that mediate several key TSP-1 functions. This cleavage induced the release of TSP-1 C-terminal domains from the extracellular matrix and abolished its previously described multisite cooperative interactions with heparan sulfate proteoglycans and CD36 on HT1080 cells. In addition, BMP-1–dependent proteolysis potentiated the TSP-1–mediated activation of latent transforming growth factor–β (TGF-β), leading to increased signaling through the canonical SMAD pathway. In primary human corneal stromal cells (keratocytes), endogenous BMP-1 cleaved TSP-1, and the addition of exogenous BMP-1 enhanced cleavage, but this had no substantial effect on cell adhesion. Instead, processed TSP-1 promoted the differentiation of keratocytes into myofibroblasts and stimulated production of the myofibroblast marker α-SMA, consistent with the presence of processed TSP-1 in human corneal scars. Our results indicate that BMP-1 can both trigger the disruption of cell adhesion and stimulate TGF-β signaling in TSP-1–rich microenvironments, which has important potential consequences for wound healing and tumor progression.

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