Zobrazeno 1 - 10
of 10
pro vyhledávání: '"M E, Fultz"'
Autor:
Gary L. Wright, M. E. Fultz
Publikováno v:
Acta Physiologica Scandinavica. 177:197-205
AIM: Using confocal microscopy and standard immunohistochemical techniques, changes in the structure of alpha-actin and beta-actin as well as the distribution of myosin II were studied in the contracting A7r5 smooth muscle cell. RESULTS: Prior to sti
Publikováno v:
Acta Physiologica Scandinavica. 174:237-246
Reports from numerous laboratories suggest that protein kinase C (PKC) translocation to substrate target sites may vary depending on cell type and experimental conditions. We have proposed that acutely variable targeting of PKC to different substrate
Publikováno v:
Acta Physiologica Scandinavica. 170:87-97
The translocation of protein kinase C (PKC) isozymes from their inactive cell locus to a variety of cytoskeletal, organelle, and plasmalemmal sites is thought to play an important role in their activation and substrate specificity. We have utilized c
Autor:
S Wang, G Wright, J Harrah, R Touchon, W McCumbee, W Geng, M E Fultz, M N Abdul-Jalil, G L Wright
Publikováno v:
Canadian Journal of Physiology and Pharmacology. 78:500-506
The effect of short-term exposure to homocysteine (Hcy) on the contractile characteristics of rat aortic tissue was assessed both in vitro and in vivo. The contractile response of Hcy-treated aortic rings in culture for 1 or 4 days was unchanged from
Autor:
M E, Fultz, G L, Wright
Publikováno v:
Acta physiologica Scandinavica. 177(2)
Using confocal microscopy and standard immunohistochemical techniques, changes in the structure of alpha-actin and beta-actin as well as the distribution of myosin II were studied in the contracting A7r5 smooth muscle cell.Prior to stimulation, each
Publikováno v:
Journal of muscle research and cell motility. 22(6)
Previous work has shown that stimulation of contraction in A7r5 smooth muscle cells with phorbol ester (PDBu) results in the disassembly and remodeling of the alpha-actin component of the cytoskeleton (Fultz et al., 2000, J Mus Res Cell Motil 21: 775
Publikováno v:
Acta physiologica Scandinavica. 174(3)
Reports from numerous laboratories suggest that protein kinase C (PKC) translocation to substrate target sites may vary depending on cell type and experimental conditions. We have proposed that acutely variable targeting of PKC to different substrate
Publikováno v:
Pflugers Archiv : European journal of physiology. 443(1)
The subcellular translocation of PKCalpha was studied in A7r5 cells by confocal microscopy through use of standard immunohistologic staining and PKCalpha-enhanced green fluorescent protein (PKCalpha-EGFP) fusion protein expression. The results from b
Publikováno v:
Acta physiologica Scandinavica. 170(2)
The translocation of protein kinase C (PKC) isozymes from their inactive cell locus to a variety of cytoskeletal, organelle, and plasmalemmal sites is thought to play an important role in their activation and substrate specificity. We have utilized c
Autor:
S, Wang, G, Wright, J, Harrah, R, Touchon, W, McCumbee, W, Geng, M E, Fultz, M N, Abdul-Jalil, G L, Wright
Publikováno v:
Canadian journal of physiology and pharmacology. 78(6)
The effect of short-term exposure to homocysteine (Hcy) on the contractile characteristics of rat aortic tissue was assessed both in vitro and in vivo. The contractile response of Hcy-treated aortic rings in culture for 1 or 4 days was unchanged from