A Ca2+ -sensitive actin regulatory protein from smooth muscle

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A Comparative, semi-quantitative Evaluation of Myofibroblasts Between Mucoepidermoid Carcinoma and Pleomorphic Adenoma Using α -Smooth Muscle Actin Marker

Abstract Introduction: Myofibroblasts are the main stromal components that constitute the desmoplastic reaction of host cells to inductive stimuli exerted by tumor cells. The purpose of this study was to evaluate the score of myofibroblasts using α -smooth muscle actin marker (α–SMA) in mucoepidermoid carcinoma (MEC) in comparison with pleomorphic adenoma (PA)and study the amount presence of t...

متن کامل

Endothelin-induced increases in vascular smooth muscle Ca2+ do not depend on dihydropyridine-sensitive Ca2+ channels.

Endothelin is a potent mammalian vasoconstrictive peptide with structural homology to cation channel-binding insect toxins. We tested the proposal that this peptide directly activates dihydropyridine-sensitive Ca2+ channels in cultured vascular smooth muscle (VSM) cells. First, we found that cell Ca2+ can be altered in VSM by activation of voltage-operated Ca2+ channels. KCl-induced depolarizat...

متن کامل

Ca2+ movements in smooth muscle.

We describe the Ca2+ movements in smooth muscle cells at rest and during activation and relaxation as deduced from transplasmalemmal Ca2+ fluxes and contractile respnses. The general picture which emerges is: the resting cell has a [Ca2+]cyt below 10(-7) M and large gradients are poised across both the cell membrane and intracellular membranes. Excitation opens up Ca2+ channels which are linked...

متن کامل

A myosin-like protein from smooth muscle.

A protein was purified from chicken gizzard smooth muscle. It bound ATP and actin. Actin activated the Mg2(+)-ATPase activity of this protein. The Ca2(+)-ATPase activity was lower than K(+)-EDTA ATPase activity. Thus, it appears that this protein is akin to myosin I rather than to conventional myosin. However, ATPase activities of the protein were much lower than those of myosin I. A protein co...

متن کامل

A Ca2+ insensitive actin-crosslinking protein from Dicytostelium discoideum.

We have isolated a 30,000-dalton protein from Dictyostelium which cosedimented with and affected the low shear viscosity of actin. At low concentrations, this protein increased the low shear viscosity to greater than that of the actin control, whereas higher concentrations decreased viscosity. The viscosity decrease correlated with the formation of actin filament bundles, as seen electron micro...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: FEBS Letters

سال: 1985

ISSN: 0014-5793

DOI: 10.1016/0014-5793(85)80607-4