Phosphospecific Site Tyrosine Phosphorylation of p125FAK and Proline-rich Kinase 2 Is Differentially Regulated by Cholecystokinin Receptor Type A Activation in Pancreatic Acini

The focal adhesion kinases, p125FAK and proline-rich kinase 2 (PYK2), are involved in numerous processes as adhesion, cytoskeletal changes, and growth. These kinases have 45% homology and share three tyrosine phosphorylation (TyrP) sites. Little information exists on the ability of stimulants to cau...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 2003-05, Vol.278 (21), p.19008-19016
Hauptverfasser:	Pace, Andrea, García-Marin, Luis J., Tapia, Jose A., Bragado, María J., Jensen, Robert T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Calcium - metabolism Cholecystokinin - administration & dosage Cholecystokinin - pharmacology Diglycerides - metabolism Dose-Response Relationship, Drug Enzyme Activation Enzyme Inhibitors - pharmacology Focal Adhesion Kinase 1 Focal Adhesion Kinase 2 Focal Adhesion Protein-Tyrosine Kinases Hydrolysis Indoles - pharmacology Inositol Phosphates - metabolism Kinetics Male Maleimides - pharmacology Pancreas - enzymology Phosphatidylinositol 4,5-Diphosphate - metabolism Phosphorylation Phosphotyrosine - metabolism Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Protein-Tyrosine Kinases - chemistry Protein-Tyrosine Kinases - metabolism Rats Rats, Sprague-Dawley Receptors, Cholecystokinin - physiology Sincalide - pharmacology Tetradecanoylphorbol Acetate - pharmacology Thapsigargin - pharmacology Type C Phospholipases - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!