Smooth muscle biochemical activities

I, 4,5-trisphosphate 3-kinase activity in pig aortic smooth muscle. Biochem. 

Hogaboom, G.K. and Fedan, J.F. (1981). Calmodulin stimulation of calcium uptake and (Ca -Mg )-ATPase activities in microsomes from canine tracheal smooth muscle. Biochem. Biophys. Res. Commun. 99, 737-744. 

Cross RA, Jackson AP, Citi S, Kendrick-Jones J, Bagshaw CR (1988) Active site trapping of nucleotide by smooth and non-muscle myosins. J Mol Biol 203 173-181 Dabrowska R (1994) In Raeburn D, Giembycz MA (eds) Airways smooth muscle biochemical control of contraction and relaxation. Birkhauser, Basle, pp 32-59 Dabrowska R, Goch A, Galazkiewicz B, Osinska H (1985) The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments. Biochim Biophys Acta 842 70-75... 

Ngai PK, Walsh MP (1984) Inhibition of smooth muscle actin-activated myosin Mg -ATPase activity by caldesmon. J Biol Chem 259 13656-13659 Ngai PK, Walsh MP (1987) The effects of phosphorylation of smooth-muscle caldesmon. Biochem J 244 417-425... 

Duarte J, Vizcaino FP, Utrilla P, Jimenez J, Tamargo J, Zarzuelo A. VasodUatory effects of flavonoids in rat aortic smooth muscle. Structure activity relationships. Biochem Pharmacol 1993 24 857-862. 

Wilson DP, Susnjar M, Kiss E, Sutherland C, Walsh MP (2005) Thromboxane A2-induced contraction of rat caudal arterial smooth muscle involves activation of Ca entry and Ca sensitization rho-associated kinase-mediated phosphorylation of MYPTl at Thr-855, but not Thr-697. Biochem J 389 763 774... 

Furchgott and Zawadzki [1] first discovered that endothelial cells release a substance(s) responsible for the relaxation of vascular smooth muscle by acetylcholine this substance was named endothelium-derived relaxing factor (EDRF). This epoch-making discovery answers the question raised for nearly one hundred years by pharmacologists about why vascular smooth muscle is relaxed by acetylcholine, which however elicits contraction of the other smooth muscles. Because of its instability, the true chemical nature of EDRF was not easily identified. Several years later, several research groups independently found that the biological activities and biochemical properties of EDRF were identical... 

The smooth muscle cell does not respond in an all-or-none manner, but instead its contractile state is a variable compromise between diverse regulatory influences. While a vertebrate skeletal muscle fiber is at complete rest unless activated by a motor nerve, regulation of the contractile activity of a smooth muscle cell is more complex. First, the smooth muscle cell typically receives input from many different kinds of nerve fibers. The various cell membrane receptors in turn activate different intracellular signal-transduction pathways which may affect (a) membrane channels, and hence, electrical activity (b) calcium storage or release or (c) the proteins of the contractile machinery. While each have their own biochemically specific ways, the actual mechanisms are for the most part known only in outline. 

Effects of immunosuppressants on receptor activator of NF-kappaB ligand and osteoprotegerin production by human osteoblastic and coronary artery smooth muscle cells. Biochem Biophys Res Commun 280 334-339... 

Abedi H, Zachary I 1998 Cytochalasin D stimulation of tyrosine phosphorylation and phosphotyrosine-associated kinase activity in vascular smooth muscle cells. Biochem Biophys Res Commun 246 646—650... 

Several of the proteins that mediate Ca2+ flow in and out of SR have been identified. Oxalate-facilitated Ca2+ uptake into the SR and in vitro biochemical studies of purified SR identified it as an ATP-driven Ca2+ pump (SERCA pump reviewed in Himpens et al 1995) that is inhibited by thapsigargin and cyclopiazonic acid and regulated, at least in some smooth muscles, by phosphorylation of phospholamban by cyclic nucleotide-activated protein kinase(s) (Karczewski et al 1998). 

Rakhit, S., Conway, A-M., Tate, R., Bower, T, Pyne, N.J. and Pyne, S., 1999, Sphingosine 1-phosphate stimulation of the p42/p44 mitogen-activated protein kinase pathway in airway smooth muscle role of endothelial differentiation gene-1, c-Src tyrosine kinase and phosphoinositide 3-kinase. Biochem. J. 338 643-649. 

The same basic biochemical control mechanism causes contraction of the smooth muscle as well as secretion of aldosterone. The binding of angiotensin to its receptor activates a membrane phospholipase-C. It catalyses the hydrolysis of phosphoinositide phosphatidylinositol bis-phosphate to produce the two intracellular messengers, inositol trisphosphate (IP3) and diacylglycerol (DAG). 

Many of the biochemical and molecular events that are responsible for uterine smooth muscle contraction are the same as those that control other smooth muscle tissues (Fig. 62.1). Once uterine smooth muscle sensitivity has been augmented, actin and myosin must interact for contraction to occur. This interaction depends on the phosphorylation of the contractile proteins by the enzyme myosin light chain kinase (MLCK). This enzyme requires Ca++ and is active only when associated with calmodulin. Activation of the entire muscle contraction... 

Sobieszek, A. Andruchov, O.Y. Nieznanski, K. Kinase-related protein (tel-okin) is phosphorylated by smooth-muscle myosin light-chain kinase and modulates the kinase activity. Biochem. J., 328, 425-430 (1997)... 

Edwards, R.A. Walsh, M.P. Sutherland, C. Vogel, H.J. Activation of calci-neurin and smooth muscle myosin light chain kinase by Met-to-Leu mutants of calmodulin. Biochem. J., 331, 149-152 (1998)... 

Ketotifen is a nonspecific, oral, mast cell stabilizer introduced in 1972 (1). The prominent biochemical-pharmacological activities of ketotifen are H,-receptor antagonism, phosphodiesterase inhibition, inhibition of the formation SRS-A, and inhibition of calcium flux in smooth muscle preparations all these actions are suited to prevent a development of asthmatic conditions. Promising results were obtained in early clinical trials ketotifen was equipotent with disodium cromoglycate in prevention of asthma induced by spontaneous excer-cise or by antigens. Also, ketotifen is more specific than clemastine as a H-,-receptor antagonist. However, more recent, controled trials failed to substantiate the early therapeutic optimism. The beneficial effect of ketotifen in the treatment of asthma is only small it was noted that this effect is associated with pronounced sedation (2). 

Wang G, Siow YL, Karmin O. Homocysteine stimulates nuclear factor kappaB activity and monocyte chemoattractant protein-1 expression in vascular smooth-muscle cells a possible role for protein kinase C. Biochem J 2000 352(Pt 3) 817-826. 

H. Satoh, M. Togo, M. Hara, T. Miyata, K. Han, H. Maekawa, N. Ohno, Y. Hashimoto, K. Kurokawa, and T. Watanabe, Advanced glycation endproducts stimulate mitogen-activated protein kinase and proliferation in rabbit vascular smooth muscle cells, Biochem. Biophys. Res. Comm., 1997, 239, 111-115. 

Bono F, Lamarche I, Herbert JM. Induction of vascular smooth muscle cell growth by selective activation of the proteinase activated receptor-2 (PAR-2). Biochem Biophys Res Commun 1997 241 762-764. 

Ludwig, A., Friedel, B., Metzkow, S., Meiners, S., Stangl, V., Baumann, G., and Stangl, K. (2005). Effect of statins on the proteasomal activity in mammalian endothelial and vascular smooth muscle cells. Biochem Pharmacol 70 520-526. 

A family of actin-binding proteins that exist in various isoforms. As with other protein isoforms or isoenzymes, the expression of the isoforms is tissue-specific. The interaction of calponin with actin inhibits the actomyosin Mg-ATRase activity. See Winder, S. and Walsh, M., Inhibition of the actinomyosin MgATRase by chicken gizzard calponin. Prog. Clin. Biol. Res. 327, 141-148, 1990 Winder, S.J., Sutherland, C., and Walsh, M.R., Biochemical and functional characterization of smooth muscle calponin, Adv. Exp. Med. Biol. 304, 37-51, 1991 Winder, S.J. and Walsh, M.R., Calponin thin filament-linked regulation of smooth muscle contraction. Cell Signal. 5,677-686,1993 el-Mezgueldi, M., Calponin, Int. J. Biochem. 

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