Is Anti–h-Caldesmon Useful for Distinguishing Smooth Muscle and Myofibroblastic Tumors?
نویسندگان
چکیده
منابع مشابه
Autophosphorylation of smooth-muscle caldesmon.
Caldesmon, a major actin- and calmodulin-binding protein of smooth muscle, has been implicated in regulation of the contractile state of smooth muscle. The isolated protein can be phosphorylated by a co-purifying Ca2+/calmodulin-dependent protein kinase, and phosphorylation blocks inhibition of the actomyosin ATPase by caldesmon [Ngai & Walsh (1987) Biochem. J. 244, 417-425]. We have examined t...
متن کاملPoint: airway smooth muscle is useful.
Some ideas just sit and stare at you. Here is one that has bothered me for a year or so. It is hard for me to regard smooth muscles as vestigial (3, 4) and they can not be solely mean-spirited, so they probably have useful function. With no library and no computer, I just fell back on Intelligent Design Un-Googled. And off I went job hunting on behalf of airway smooth muscles. Do they manage th...
متن کاملThe effects of smooth muscle caldesmon on actin filament motility.
The movement of reconstituted thin filaments over an immobilized surface of thiophosphorylated smooth muscle myosin was examined using an in vitro motility assay. Reconstituted thin filaments contained actin, tropomyosin, and either purified chicken gizzard caldesmon or the purified COOH-terminal actin-binding fragment of caldesmon. Control actin-tropomyosin filaments moved at a velocity of 2.3...
متن کاملPhosphorylation of caldesmon by ERK MAP kinases in smooth muscle.
Phosphorylation of h-caldesmon has been proposed to regulate airway smooth muscle contraction. Both extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases phosphorylate h-caldesmon in vitro. To determine whether both enzymes phosphorylate caldesmon in vivo, phosphorylation-site-selective antibodies were used to assay phosphorylation of MAP kinase consensus s...
متن کاملThree-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments
Caldesmon is known to inhibit actomyosin ATPase and filament sliding in vitro, and may play a role in modulating smooth muscle contraction as well as in diverse cellular processes including cytokinesis and exocytosis. However, the structural basis of caldesmon action has not previously been apparent. We have recorded electron microscope images of negatively stained thin filaments containing cal...
متن کاملذخیره 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: American Journal of Clinical Pathology
سال: 2000
ISSN: 1943-7722,0002-9173
DOI: 10.1309/k5jp-a9en-uwn7-b5gg