Journal ArticleDOI
Calyculin A and okadaic acid: inhibitors of protein phosphatase activity
H. Ishihara,Bruce L. Martin,David L. Brautigan,Hideaki Karaki,Hiroshi Ozaki,Yukio Kato,Nobuhiro Fusetani,Shugo Watabe,Koichi Hashimoto,Daisuke Uemura,David J. Hartshorne +10 more
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TLDR
The pattern of inhibition for the phosphatase in myosin B is similar to that of the type-1 enzyme, and the effects of both compounds on various phosphatases are screened.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1989-03-31. It has received 999 citations till now. The article focuses on the topics: Okadaic acid & Calyculin.read more
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Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
Masayoshi Uehata,Toshimasa Ishizaki,Hiroyuki Satoh,Takashi Ono,Toshio Kawahara,Tamami Morishita,Hiroki Tamakawa,Keiji Yamagami,Jun Inui,Midori Maekawa,Shuh Narumiya +10 more
TL;DR: Pyridine derivative Y-27632 consistently suppresses Rho-induced, p160ROCK-mediated formation of stress fibres in cultured cells and dramatically corrects hypertension in several hypertensive rat models, suggesting that compounds that inhibit this process might be useful therapeutically.
Journal ArticleDOI
Signaling Mechanisms Regulating Endothelial Permeability
Dolly Mehta,Asrar B. Malik +1 more
TL;DR: This review summarizes and analyzes the recent data from genetic, physiological, cellular, and morphological studies that have addressed the signaling mechanisms involved in the regulation of both the paracellular and transcellular transport pathways.
Journal ArticleDOI
Okadaic acid: a new probe for the study of cellular regulation.
TL;DR: The tumour promoter okadaic acid is a potent and specific inhibitor of protein phosphatases 1 and 2A and is extremely useful for identifying biological processes that are controlled through the reversible phosphorylation of proteins.
Journal ArticleDOI
Sodium-Potassium-Chloride Cotransport
TL;DR: Although the NKCC has been studied for approximately 20 years, it is only beginning to frame the broad outlines of the structure, function, and regulation of this ubiquitous ion transport mechanism.
Journal Article
Calcium Movements, Distribution, and Functions in Smooth Muscle
Hideaki Karaki,Hiroshi Ozaki,Masatoshi Hori,Minori Mitsui-Saito,Ken-ichi Amano,Ken-ichi Harada,Shigeki Miyamoto,Hiroshi Nakazawa,Kyung-Jong Won,Koichi Sato +9 more
TL;DR: Contraction of smooth muscle is regulated by the cytosolic Ca2+ level ([Ca2+]i)b, and the sensitivity of the contractile elements in response to changes in the environment surrounding the cell.
References
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Journal ArticleDOI
Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
Corinna Bialojan,Akira Takai +1 more
TL;DR: Kinetic studies showed that okadaic acid acts as a non-competitive or mixed inhibitor on the okadaIC acid-sensitive enzymes.
Journal ArticleDOI
The role of protein phosphorylation in neural and hormonal control of cellular activity
TL;DR: There is an integrated network of regulatory pathways, mediated by phosphorylation–dephosphorylation, that allows diverse cellular events to be coordinated by neural and hormonal stimuli, and the evidence that supports this concept is reviewed.
Journal ArticleDOI
Okadaic acid, a cytotoxic polyether from two marine sponges of the genus Halichondria
Kazuo Tachibana,Paul J. Scheuer,Yasumasa Tsukitani,Hiroyuki Kikuchi,Donna Van Engen,Jon Clardy,Yalamanchili Gopichand,Francis J. Schmitz +7 more
Journal ArticleDOI
The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities.
TL;DR: Examination of the amino acid sequences around each phosphorylation site does not support the idea that protein phosphatase specificity is determined by the primary structure in the immediate vicinity of the phosphorylated site, and demonstrates that proteinosphatase-1 and protein phosph atase 2A have very broad substrate specificities.
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Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
Corinna Bialojan,Akira Takai +1 more