Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.6.1.2 (guanylate cyclase)
 8,497 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cell motility is an important determinant of vascular disease. We examined mechanisms underlying the effect of nitric oxide (NO) on motility in cultured primary aortic smooth muscle cells from newborn rats. The NO donor S-nitroso-N-acetyl-penicillamine (SNAP) increased the activity of protein tyrosine phosphatase 1B (PTP-1B). This effect was mimicked by a cGMP analog and blocked by the guanyl cyclase antagonist 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one, indicating the involvement of cGMP. Treatment of cells with antisense, but not control oligodeoxynucleotide (ODN), against PTP-1B attenuated the inhibitory effect of NO on cell motility. Cell shape and adhesion are important determinants of cell motility. We report that SNAP induced cell rounding and reduced adhesion and caused dissociation of actin stress fibers. Moreover, SNAP reduced phosphotyrosine levels in focal adhesion proteins, paxillin, and focal adhesion kinase. The PTP inhibitor phenylarsine oxide or decrease of PTP-1B protein levels via the use of antisense ODN prevented NO-induced cell-shape change, altered adhesion, and migration. These results indicate that NO regulates cell shape, adhesion, and migration by dephosphorylation of focal adhesion proteins via a mechanism that requires PTP-1B activity.
 ...
PMID:NO alters cell shape and motility in aortic smooth muscle cells via protein tyrosine phosphatase 1B activation. 1048 24

The objective of the present work was to study the effects of erythrocyte proteins phosphorylation in erythrocyte aggregation and deformability. Human whole blood samples were incubated in vitro in absent and in presence of the phosphorylation/dephosphorilation band 3 inhibitors and also with adenylyl cyclase, guanylate cyclase and PI3K inhibitors and the erythrocyte aggregation index (AIE) and deformability were assayed. The results show that when band 3 is phosphorylated in presence of a PTP inhibitor an increase in erythrocyte aggregation index is observed (p<0.0001). A partial dephosphorylation band 3 state, induced by PTK inhibitors, show a decrease in the erythrocyte aggregation index (p<0.002). However both manipulated states induced lower EAI values than blood samples aliquots controls. The guanylate cyclase and PI3-K inhibitors significantly decrease the erythrocyte aggregation index in relation with the control blood samples. Erythrocyte deformability in presence of all the inhibitors did not showed significant changes. PTP and PI3-K inhibitors showed a significantly increase in the plasma potassium concentrations not associated with EAI values. Methehemoglobin levels were increased significantly when guanylate cyclase inhibitor is present in the blood samples. In conclusion, the results suggest that erythrocyte aggregation index is dependent of the phosphorylated/dephosphorylated state of band 3.
 ...
PMID:Modulation of erythrocyte hemorheological properties by band 3 phosphorylation and dephosphorylation. 1736 Oct 21