Myosin heavy chain isoforms, expression

Eddinger TJ, Murphy RA (1991) Developmental changes in actin and myosin heavy chain isoform expression in smooth muscle. Arch Biochem Biophys 284 232237 Eddinger TJ, Wolf JA (1993) Expression of four myosin heavy chain isoforms with development iii mouse uterus. Cell Motil Cytoskeleton 25 358368 Edman KA (1980) Depression of mechanical performance by active shortening during twitch and tetanus of vertebrate muscle fibres. Acta Physiologica Scandinavica 109 1526... [Pg.49]

Cavaill F, Fournier T, Dallot E, Dhellemes C, Ferr F (1995) Myosin heavy chain isoform expression in human myometrium. Cell Motil Cytoskel 30 183-193... [Pg.298]

Eddinger TJ, Murphy RA (1991) Developmental changes in actin and myosin heavy chain isoform expression in smooth muscle. Arch Biochem Biophys 284 232-237... [Pg.300]

Kim HS, Aikawa M, Kimura K, Kuro-o M, Nakahara K, Suzuki T, Katoh H, Okamoto E, Yazaki Y, Nagai R (1993) Ductus arteriosus advanced differentiation of smooth muscle cells demonstrated by myosin heavy chain isoform expression in rabbits. Circulation 88 1804-1810... [Pg.317]

Miyata, S., Minobe, W., Bristow, M.R., and Leinwand, L.A. (2000) Myosin heavy chain isoform expression in the failing and nonfailing human heart. Circ. Res. 86, 386-390. [Pg.293]

Hoya K, Asai A, Sasaki T. Expression of myosin heavy chain isoforms by smooth muscle cells in cerebral arteriovenous malformations. Acta Neuropathol. 2003 105 455-461. [Pg.885]

Kuro-o M, Nagai R, Tsuchimochi H, Katoh H, Yazaki Y, Ohkubo A, Takaku F (1989) Developmentally regulated expression of vascular smooth muscle myosin heavy chain isoforms. J Biol Chem 264 18272-18275... [Pg.298]

Kuro-o M, Nagai R, Nakahara K, Katoh H, Tsai RC, Tsuchimochi H, Yazaki YH, Ohkubo H, Takaku F (1991) cDNA cloning of a myosin heavy chain isoform in embryonic smooth muscle and its expression during vascular development and in arteriosclerosis. J Biol Chem 266 3768-3773... [Pg.298]

Eddinger TJ, Wolf JA (1993) Expression of four myosin heavy chain isoforms with development in mouse uterus. Cell Motil Cytoskel 25 358-368... [Pg.298]

Murakami N, Trenkner E, Elzinga M (1993) Changes in expression of nonmuscle myosin heavy chain isoforms during muscle and nonmuscle tissue development. Dev Biol 157 19-27... [Pg.303]

Colbert MC, Kirby ML, Robbins J (1996) Endogeneous retinoic acid signaling colocalizes with advanced expression of the adult smooth muscle myosin heavy chain isoform during development of the ductus arteriosus. Circ Res 78 790-798... [Pg.317]

Chiavegato A, Bochaton-Piallat M-L, D Amore E, Sartore S, Gabbiani G (1995) Expression of myosin heavy chain isoforms in mammary epithelial cells and in myofibroblasts from different fibrotic settings during neoplasia. Virchows Archiv B 426 77-86... [Pg.318]

Lemon, D.D., Papst, P.J., Joly, K., Plato, C.F., and McKinsey, T.A. (2011) A high-performance liquid chromatography assay for quantification of cardiac myosin heavy chain isoform protein expression. Anal. Biochem. 408, 132-135. [Pg.292]

The multiple non-muscle-type myosin heavy chain isoforms can be grouped into two myosin heavy chain A and B types, the latter being predominantly expressed in brain (Sun and Chantler 1992, Takahashi et al. 1992) and the former essentially in muscle and in non-muscle-non-brain tissues (Murakami et al. 1993). [Pg.246]

NFAT proteins are expressed in skeletal, cardiac, and smooth muscle and play important roles in the regulation of the development and differentiation of these tissues. In skeletal muscle, NFAT isoforms are expressed at different stages of development and regulate progression from early muscle cell precursors to mature myocytes. NFAT proteins have also been shown to control the expression of the myosin heavy chain and positively regulate muscle growth [1, 2]. [Pg.849]

Itoh K and Adelstein RS [1995] Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B. J Biol Chem 270 14533-14540... [Pg.366]

Striated muscle myosins. In smooth and non-muscle cells, two different length isoforms of the tailpiece have been identified, that result in 200 kDa (SM2) and 204 kDa (SMI) heavy chain isoforms (Nagai et al 1989, Babij and Periasamy 1989). These iso forms are expressed to the same extent at... [Pg.19]

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