Kinetics of Cell Adhesion to a Hydrophilic-Hydrophobic Copolymer Model System

1980 ◽  
pp. 667-675 ◽  
Author(s):  
Jonathan J. Rosen ◽  
Michael B. Schway
Keyword(s):  
Cell Adhesion ◽  
Model System ◽  
Kinetics Of

scholarly journals Serine and Threonine Phosphorylation of the Paxillin LIM Domains Regulates Paxillin Focal Adhesion Localization and Cell Adhesion to Fibronectin

1998 ◽  
Vol 9 (7) ◽  
pp. 1803-1816 ◽  
Author(s):  
Michael C. Brown ◽  
Joseph A. Perrotta ◽  
Christopher E. Turner
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion ◽  
Binding Sites ◽  
Protein Localization ◽  
Model System ◽  
Lim Domain ◽  
Amino Terminal ◽  
Lim Domains ◽  
Inside Out

We have previously shown that the LIM domains of paxillin operate as the focal adhesion (FA)-targeting motif of this protein. In the current study, we have identified the capacity of paxillin LIM2 and LIM3 to serve as binding sites for, and substrates of serine/threonine kinases. The activities of the LIM2- and LIM3-associated kinases were stimulated after adhesion of CHO.K1 cells to fibronectin; consequently, a role for LIM domain phosphorylation in regulating the subcellular localization of paxillin after adhesion to fibronectin was investigated. An avian paxillin-CHO.K1 model system was used to explore the role of paxillin phosphorylation in paxillin localization to FAs. We found that mutations of paxillin that mimicked LIM domain phosphorylation accelerated fibronectin-induced localization of paxillin to focal contacts. Further, blocking phosphorylation of the LIM domains reduced cell adhesion to fibronectin, whereas constitutive LIM domain phosphorylation significantly increased the capacity of cells to adhere to fibronectin. The potentiation of FA targeting and cell adhesion to fibronectin was specific to LIM domain phosphorylation as mutation of the amino-terminal tyrosine and serine residues of paxillin that are phosphorylated in response to fibronectin adhesion had no effect on the rate of FA localization or cell adhesion. This represents the first demonstration of the regulation of protein localization through LIM domain phosphorylation and suggests a novel mechanism of regulating LIM domain function. Additionally, these results provide the first evidence that paxillin contributes to “inside-out” integrin-mediated signal transduction.

Reaction kinetics of the metal ion catalyzed .beta.-phenylserine-pyridoxal model system

1978 ◽  
Vol 100 (17) ◽  
pp. 5549-5553 ◽  
Author(s):  
Kuniyasu Tatsumoto ◽  
Arthur E. Martell
Keyword(s):  
Reaction Kinetics ◽  
Metal Ion ◽  
Model System ◽  
Kinetics Of

Kinetics of the Low Salinity Waterflooding Effect Studied in a Model System

2013 ◽  
Author(s):  
Hassan Mahani ◽  
Steffen Berg ◽  
Denis Ilic ◽  
Willem-Bart Bartels ◽  
Vahid Joekar-Niasar
Keyword(s):  
Model System ◽  
Low Salinity ◽  
Low Salinity Waterflooding ◽  
Kinetics Of

Thermal Degradation Kinetics of Bixin in an Aqueous Model System

2005 ◽  
Vol 53 (6) ◽  
pp. 2307-2311 ◽  
Author(s):  
Alessandro de O. Rios ◽  
Claudio D. Borsarelli ◽  
Adriana Z. Mercadante
Keyword(s):  
Thermal Degradation ◽  
Degradation Kinetics ◽  
Model System ◽  
Thermal Degradation Kinetics ◽  
Kinetics Of

Phagocytosis, an alternative model system for the study of cell adhesion

2004 ◽  
Vol 15 (6) ◽  
pp. 679-689 ◽  
Author(s):  
C COUGOULE ◽  
A WIEDEMANN ◽  
J LIM ◽  
E CARON
Keyword(s):  
Cell Adhesion ◽  
Alternative Model ◽  
Model System

Direct insight into the kinetics of the high-pressure step-growth polymerization of DGEBA/aniline model system

Polymer ◽  
2019 ◽  
Vol 172 ◽  
pp. 322-329 ◽  
Author(s):  
Andrzej Dzienia ◽  
Kajetan Koperwas ◽  
Magdalena Tarnacka ◽  
Mirosław Chorążewski ◽  
Eugene B. Postnikov ◽  
...  
Keyword(s):  
High Pressure ◽  
Model System ◽  
Pressure Step ◽  
Step Growth ◽  
Step Growth Polymerization ◽  
Kinetics Of ◽  
Insight Into
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