RGD Reference Report - NO alters cell shape and motility in aortic smooth muscle cells via protein tyrosine phosphatase 1B activation. - Rat Genome Database

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NO alters cell shape and motility in aortic smooth muscle cells via protein tyrosine phosphatase 1B activation.

Authors: Hassid, A  Yao, J  Huang, S 
Citation: Hassid A, etal., Am J Physiol. 1999 Sep;277(3):H1014-26. doi: 10.1152/ajpheart.1999.277.3.H1014.
RGD ID: 401965470
Pubmed: PMID:10484424   (View Abstract at PubMed)
DOI: DOI:10.1152/ajpheart.1999.277.3.H1014   (Journal Full-text)

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.



Gene-Chemical Interaction Annotations    Click to see Annotation Detail View

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PTPN1Human1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one multiple interactionsISOPtpn1 (Rattus norvegicus)ODQ inhibits the reaction [SNAP increases activity of Ptpn1 protein in aortic smooth muscle cells]RGD 
Ptpn1Rat1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one multiple interactionsEXP ODQ inhibits the reaction [SNAP increases activity of Ptpn1 protein in aortic smooth muscle cells]RGD 
Ptpn1Mouse1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one multiple interactionsISOPtpn1 (Rattus norvegicus)ODQ inhibits the reaction [SNAP increases activity of Ptpn1 protein in aortic smooth muscle cells]RGD 
PTPN1HumanS-nitroso-N-acetyl-D-penicillamine increases activityISOPtpn1 (Rattus norvegicus)SNAP increases activity of Ptpn1 protein in aortic smooth muscle cellsRGD 
Ptpn1RatS-nitroso-N-acetyl-D-penicillamine increases activityEXP SNAP increases activity of Ptpn1 protein in aortic smooth muscle cellsRGD 
Ptpn1MouseS-nitroso-N-acetyl-D-penicillamine increases activityISOPtpn1 (Rattus norvegicus)SNAP increases activity of Ptpn1 protein in aortic smooth muscle cellsRGD 

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Ptpn1Ratnegative regulation of cell-substrate adhesion  IMP  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Ptpn1  (protein tyrosine phosphatase, non-receptor type 1)

Genes (Mus musculus)
Ptpn1  (protein tyrosine phosphatase, non-receptor type 1)

Genes (Homo sapiens)
PTPN1  (protein tyrosine phosphatase non-receptor type 1)


Additional Information