Abstract | BACKGROUND: METHODS AND RESULTS: Immunoblot showed increased α(1)-, α(8)- and α(v)- integrins, and decreased α(5)-integrin levels in PAs of both models. β(1)- and β(3)-integrins were reduced in PAs of chronic hypoxia and monocrotaline-treated rats, respectively. Integrin expression in aorta was minimally affected. Differential expression of α(1)- and α(5)-integrins induced by chronic hypoxia was further examined. Immunostaining showed that they were expressed on the surface of PA smooth muscle cells (PASMCs), and their distribution was unaltered by chronic hypoxia. Phosphorylation of focal adhesion kinase was augmented in PAs of chronic hypoxia rats, and in chronic hypoxia PASMCs cultured on the α(1)-ligand collagen IV. Moreover, α(1)-integrin binding hexapeptide GRGDTP elicited an enhanced Ca(2+) response, whereas the response to α(5)-integrin binding peptide GRGDNP was reduced in CH-PASMCs. CONCLUSION:
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Authors | Anita Umesh, Omkar Paudel, Yuan-Ning Cao, Allen C Myers, James S K Sham |
Journal | Journal of vascular research
(J Vasc Res)
Vol. 48
Issue 6
Pg. 525-37
( 2011)
ISSN: 1423-0135 [Electronic] Switzerland |
PMID | 21829038
(Publication Type: Journal Article, Research Support, N.I.H., Extramural)
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Copyright | Copyright © 2011 S. Karger AG, Basel. |
Chemical References |
- Integrins
- Monocrotaline
- Focal Adhesion Kinase 1
- Ptk2 protein, rat
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Topics |
- Animals
- Calcium Signaling
(physiology)
- Chronic Disease
- Disease Models, Animal
- Focal Adhesion Kinase 1
(metabolism)
- Hypertension, Pulmonary
(chemically induced, metabolism)
- Hypoxia
(metabolism)
- Integrins
(metabolism)
- Male
- Monocrotaline
(pharmacology)
- Muscle, Smooth, Vascular
(metabolism)
- Phosphorylation
(physiology)
- Pulmonary Artery
(metabolism)
- Rats
- Rats, Wistar
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