Regulation of cytosolic protein-tyrosine kinase from porcine spleen by polyamines and negative-charged polysaccharides.
In vitro regulation of cytosolic protein-tyrosine kinase from porcine spleen (CPTK-40) by various positive or negative charged compounds was studied. Spermine and spermidine stimulated the activity of CPTK-40 about two-fold using (Val5)angiotensin II as a substrate. This stimulation was not specific for the peptide but was also observed in the case of tubulin phosphorylation indicating a direct effect of these compounds on the enzyme itself. On the contrary, negative-charged polysaccharides were shown to be strong inhibitors of CPTK-40. The possibility of the physiological regulation of CPTK-40 by these compounds is briefly discussed.
D000804:Angiotensin II / Q000378:metabolism; D000818:Animals; D002809:Chondroitin Sulfates / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D010455:Peptides / Q000494:pharmacology*; D010766:Phosphorylation; D011073:Polyamines / Q000494:pharmacology*; D011134:Polysaccharides / Q000494:pharmacology*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity; D013552:Swine; D014404:Tubulin / Q000378:metabolism
D010455:Peptides; D011073:Polyamines; D011134:Polysaccharides; D014404:Tubulin; D000804:Angiotensin II; D002809:Chondroitin Sulfates; D011505:Protein-Tyrosine Kinases