TY - JOUR
T1 - A pivotal role of nitric oxide in endothelial cell dysfunction
AU - Goligorsky, Michael S.
AU - Noiri, E.
AU - Tsukahara, H.
AU - Budzikowski, A. S.
AU - Li, H.
PY - 2000
Y1 - 2000
N2 - The functional role of the vascular endothelium is a subject of growing interest and appreciation. Some of the key functions of the endothelium are modulated by the activity and expression of endothelial nitric oxide synthase (eNOS), suggesting a role for this enzyme in endothelial dysfunction. Several well-known angiogenic stimulators exert their effect only in the presence of the functional eNOS. In this setting NO production is responsible for the scalar podokinetic cell motility, which is a prerequisite for the acquisition of vectorial movement when guidance cues are applied. The mode of this NO action appears to lie in the accelerated turnover of focal adhesions through the process of activation/inactivation of protein tyrosine phosphatases. Localization of eNOS to the caveolar domains, in the proximity of clustered β1 integrins, provides an additional level of regulatory complexity through the modulation of caveolar dynamics and the state of caveolin oligomerization. Therefore, eNOS serves various important functions in the endothelium and is a putative target for therapeutic interventions.
AB - The functional role of the vascular endothelium is a subject of growing interest and appreciation. Some of the key functions of the endothelium are modulated by the activity and expression of endothelial nitric oxide synthase (eNOS), suggesting a role for this enzyme in endothelial dysfunction. Several well-known angiogenic stimulators exert their effect only in the presence of the functional eNOS. In this setting NO production is responsible for the scalar podokinetic cell motility, which is a prerequisite for the acquisition of vectorial movement when guidance cues are applied. The mode of this NO action appears to lie in the accelerated turnover of focal adhesions through the process of activation/inactivation of protein tyrosine phosphatases. Localization of eNOS to the caveolar domains, in the proximity of clustered β1 integrins, provides an additional level of regulatory complexity through the modulation of caveolar dynamics and the state of caveolin oligomerization. Therefore, eNOS serves various important functions in the endothelium and is a putative target for therapeutic interventions.
KW - Angiogenesis
KW - Caveolae
KW - Signal transduction
KW - Vasomotion
KW - eNOS
UR - http://www.scopus.com/inward/record.url?scp=0034052195&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034052195&partnerID=8YFLogxK
U2 - 10.1046/j.1365-201X.2000.00636.x
DO - 10.1046/j.1365-201X.2000.00636.x
M3 - Article
C2 - 10691777
AN - SCOPUS:0034052195
VL - 168
SP - 33
EP - 40
JO - Acta Physiologica Scandinavica
JF - Acta Physiologica Scandinavica
SN - 0001-6772
IS - 1
ER -