caa a22 4500 477120113 CHVBK 20180405111634.0 cr unu---uuuuu 170330e19960401xx s 000 0 eng 10.1007/BF00227887 doi (NATIONALLICENCE)springer-10.1007/BF00227887 Reduction in Gh protein expression is associated with cytodifferentiation of vascular smooth muscle cells [Elektronische Daten] [Elizabeth Vincan, Craig Neylon, Alexander Jacobsen, Elizabeth Woodcock] Gh, a high molecular weight GTP-binding protein that couples α1-adrenoceptors in heart and liver to phosphatidylinositol (Ptdlns)-specific phospholipase C (PLC), has recently been shown to be a tissue transglutaminase type 11. Transglutaminases have been suggested to play a role in the maintenance of blood vessel structure, and therefore it is possible that changes in their expression may accompany pathological states which involve phenotypic modulation of smooth muscle. Hence, we investigated the expression of Gh during differentiation of rat aortic smooth muscle cells in culture. Gh content was reduced markedly in cultured smooth muscle cells compared to freshly isolated cells as determined by Western blotting using a Gh-specific monoclonal antibody. In contrast, the level of Gq, a heterotrimeric G-protein that couples α1-adrenoceptors to PLC, was maintained throughout the culture period. These findings indicate that changes in G, expression accompany phenotypic modulation of vascular smooth muscle cells. These changes in Gh protein expression may be important in the altered responsiveness of vessels in pathological disease states. Kluwer Academic Publishers, 1996 vascular smooth muscle cell nationallicence G-protein nationallicence Gh, transglutaminase nationallicence phosphatidylinositol turnover nationallicence signal transduction nationallicence Vincan Elizabeth Cellular Biochemistry Laboratory, Baker Medical Research Institute, Commercial Road, Prahran, 3181, Victoria, Australia aut Neylon Craig Cell Biology Laboratory, Baker Medical Research Institute, Commercial Road, Prahran (Melbourne), 3141, Victoria, Australia aut Jacobsen Alexander Cellular Biochemistry Laboratory, Baker Medical Research Institute, Commercial Road, Prahran, 3181, Victoria, Australia aut Woodcock Elizabeth Cellular Biochemistry Laboratory, Baker Medical Research Institute, Commercial Road, Prahran, 3181, Victoria, Australia aut Molecular and Cellular Biochemistry Kluwer Academic Publishers 157/1-2(1996-04-01), 107-110 0300-8177 157:1-2<107 1996 157 11010 https://doi.org/10.1007/BF00227887 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00227887 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Vincan Elizabeth Cellular Biochemistry Laboratory, Baker Medical Research Institute, Commercial Road, Prahran, 3181, Victoria, Australia aut NATIONALLICENCE 700 1- Neylon Craig Cell Biology Laboratory, Baker Medical Research Institute, Commercial Road, Prahran (Melbourne), 3141, Victoria, Australia aut NATIONALLICENCE 700 1- Jacobsen Alexander Cellular Biochemistry Laboratory, Baker Medical Research Institute, Commercial Road, Prahran, 3181, Victoria, Australia aut NATIONALLICENCE 700 1- Woodcock Elizabeth Cellular Biochemistry Laboratory, Baker Medical Research Institute, Commercial Road, Prahran, 3181, Victoria, Australia aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers 157/1-2(1996-04-01), 107-110 0300-8177 157:1-2<107 1996 157 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer