scholarly journals Intercellular Adhesion Strength Analysis Utilizing Femtosecond Laser Impulse

2017 ◽  
Vol 57 (2) ◽  
pp. 107-110
Author(s):  
Yoichiroh HOSOKAWA ◽  
Takanori IINO ◽  
Man HAGIYAMA ◽  
Akihiko ITO
Keyword(s):  
Femtosecond Laser ◽  
Adhesion Strength ◽  
Intercellular Adhesion ◽  
Strength Analysis ◽  
Laser Impulse

scholarly journals Time-Course Statistical Evaluation of Intercellular Adhesion Maturation by Femtosecond Laser Impulse

2016 ◽  
Vol 111 (10) ◽  
pp. 2255-2262 ◽  
Author(s):  
Takanori Iino ◽  
Man Hagiyama ◽  
Tadahide Furuno ◽  
Akihiko Ito ◽  
Yoichiroh Hosokawa
Keyword(s):  
Femtosecond Laser ◽  
Time Course ◽  
Statistical Evaluation ◽  
Intercellular Adhesion ◽  
Laser Impulse

scholarly journals Phosphatidylinositol-4,5 Bisphosphate Produced by PIP5KIγ Regulates Gelsolin, Actin Assembly, and Adhesion Strength of N-Cadherin Junctions

2007 ◽  
Vol 18 (8) ◽  
pp. 3026-3038 ◽  
Author(s):  
T. Y. El Sayegh ◽  
P. D. Arora ◽  
K. Ling ◽  
C. Laschinger ◽  
P. A. Janmey ◽  
...  
Keyword(s):  
Adhesion Strength ◽  
Intercellular Adhesion ◽  
Actin Binding ◽  
Type I ◽  
Actin Assembly ◽  
Wild Type ◽  
Binding Region ◽  
A Cell ◽  
Intercellular Adhesions ◽  
Phosphatidylinositol 4

Phosphoinositides regulate several actin-binding proteins but their role at intercellular adhesions has not been defined. We found that phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) was generated at sites of N-cadherin–mediated intercellular adhesion and was a critical regulator of intercellular adhesion strength. Immunostaining for PI(4,5)P2 or transfection with GFP-PH-PLCδ showed that PI(4,5)P2 was enriched at sites of N-cadherin adhesions and this enrichment required activated Rac1. Isoform-specific immunostaining for type I phosphatidylinositol 4-phosphate 5 kinase (PIP5KI) showed that PIP5KIγ was spatially associated with N-cadherin–Fc beads. Association of PIP5KIγ with N-cadherin adhesions was in part dependent on the activation of RhoA. Transfection with catalytically inactive PIP5KIγ blocked the enrichment of PI(4,5)P2 around beads. Catalytically inactive PIP5KIγ or a cell-permeant peptide that mimics and competes for the PI(4,5)P2-binding region of the actin-binding protein gelsolin inhibited incorporation of actin monomers in response to N-cadherin ligation and reduced intercellular adhesion strength by more than twofold. Gelsolin null fibroblasts transfected with a gelsolin severing mutant containing an intact PI(4,5)P2 binding region, demonstrated intercellular adhesion strength similar to wild-type transfected controls. We conclude that PIP5KIγ-mediated generation of PI(4,5)P2 at sites of N-cadherin contacts regulates intercellular adhesion strength, an effect due in part to PI(4,5)P2-mediated regulation of gelsolin.

scholarly journals Improving Adhesion Strength Analysis by the Combination of Ultrasonic and Mechanical Tests on Single-Lap Joints

2014 ◽  
Vol 90 (5-6) ◽  
pp. 555-568 ◽  
Author(s):  
Alice Baudot ◽  
Joseph Moysan ◽  
Cédric Payan ◽  
Noëllie Ylla ◽  
Jocelyne Galy ◽  
...  
Keyword(s):  
Adhesion Strength ◽  
Mechanical Tests ◽  
Lap Joints ◽  
Strength Analysis ◽  
Single Lap Joints

scholarly journals Phosphorylation of N-Cadherin-associated Cortactin by Fer Kinase Regulates N-Cadherin Mobility and Intercellular Adhesion Strength

2005 ◽  
Vol 16 (12) ◽  
pp. 5514-5527 ◽  
Author(s):  
Tarek Y. El Sayegh ◽  
Pamela D. Arora ◽  
Lingzhi Fan ◽  
Carol A. Laschinger ◽  
Peter A. Greer ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Adhesion Strength ◽  
Fluorescence Recovery After Photobleaching ◽  
Kinase Activity ◽  
Intercellular Adhesion ◽  
Wild Type ◽  
Nonreceptor Tyrosine Kinase ◽  
Junction Formation ◽  
Intercellular Adhesions ◽  
Dependent Mechanism

Cortactin regulates the strength of nascent N-cadherin-mediated intercellular adhesions through a tyrosine phosphorylation-dependent mechanism. Currently, the functional significance of cortactin phosphorylation and the kinases responsible for the regulation of adhesion strength are not defined. We show that the nonreceptor tyrosine kinase Fer phosphorylates cadherin-associated cortactin and that this process is involved in mediating intercellular adhesion strength. In wild-type fibroblasts N-cadherin ligation-induced transient phosphorylation of Fer, indicating that junction formation activates Fer kinase. Tyrosine phosphorylation of cortactin after N-cadherin ligation was strongly reduced in fibroblasts expressing only catalytically inactive Fer (D743R), compared with wild-type cells. In wild-type cells, N-cadherin-coated bead pull-off assays induced fourfold greater endogenous N-cadherin association than in D743R cells. Fluorescence recovery after photobleaching showed that GFP-N-cadherin mobility at nascent contacts was 50% faster in wild-type than D743R cells. In shear wash-off assays, nascent intercellular adhesion strength was twofold higher in wild-type than D743R cells. Cortactin recruitment to adhesions was independent of Fer kinase activity, but was impacted by N-cadherin ligation-provoked Rac activation. We conclude that N-cadherin ligation induces Rac-dependent cortactin recruitment and Fer-dependent cortactin phosphorylation, which in turn promotes enhanced mobilization and interaction of surface expressed N-cadherin in contacting cells.

Cumulation and acceleration of ions by TW femtosecond laser impulse

2004 ◽  
Author(s):  
V.A. Balakirev ◽  
A.N. Dovbnya ◽  
M.A. Krasnogolovets ◽  
I.N. Onishchenko ◽  
N.I. Onishchenko ◽  
...  
Keyword(s):  
Femtosecond Laser ◽  
Laser Impulse
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