http://www.cnr.it/ontology/cnr/individuo/prodotto/ID170773
Endothelial nitric oxide synthase is segregated from caveolin-1 and localizes to the leading edge of migrating cells. (Articolo in rivista)
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- Endothelial nitric oxide synthase is segregated from caveolin-1 and localizes to the leading edge of migrating cells. (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.yexcr.2005.12.014 (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Bulotta S; Cerullo A; Barsacchi R; Palma CD; Rotiroti D; Clementi E;Borgese N (literal)
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- http://www.sciencedirect.com/science/article/pii/S0014482705005823 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- Bulotta S: Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro;
Cerullo A: Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro;
Barsacchi R: Stem Cell Research Institute-DIBIT H San Raffaele, Milano; Palma CD: bStem Cell Research Institute-DIBIT H San Raffaele, Milano; Department of Pharmaco-Biology, University of Calabria; Rotiroti D: Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro; Clementi E: Stem Cell Research Institute-DIBIT H San Raffaele, Milano;Department of Preclinical Sciences, University of Milano, and E. Medea Scientific Institute, Bosisio Parini, Italy; Borgese N: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica dell'Università di Mlano; Dipartimento di Scienze farmacobiologiche, Università \"Magna Graecia\" di Catanzaro (literal)
- Titolo
- Endothelial nitric oxide synthase is segregated from caveolin-1 and localizes to the leading edge of migrating cells. (literal)
- Abstract
- The enzyme endothelial Nitric Oxide Synthase (eNOS) is involved in key physiological and pathological processes, including cell motility and apoptosis. It is widely believed that at the cell surface eNOS is localized in caveolae, where caveolin-1 negatively regulates its activity, however, there are still uncertainties on its intracellular distribution. Here, we applied high resolution confocal microscopy to investigate the surface distribution of eNOS in transfected HeLa cells and in human umbilical vein endothelial cells (HUVEC) endogenously expressing the enzyme. In confluent and non-confluent HUVEC and HeLa cells, we failed to detect substantial colocalization between eNOS and caveolin-1 at the cell surface. Instead, in non-confluent cells, eNOS was concentrated in ruffles and at the leading edge of migrating cells, colocalizing with actin filaments and with the raft marker ganglioside G(M1), and well segregated from caveolin-1, which was restricted to the posterior region of the cells. Treatments that disrupted microfilaments caused loss of eNOS from the cell surface and decreased Ca(2+)-stimulated activity, suggesting a role of the cytoskeleton in the localization and function of the enzyme. Our results provide a morphological correlate for the role of eNOS in cell migration and raise questions on the site of interaction between eNOS and caveolin-1. (literal)
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