Regulation of Catch Muscle by Twitchin Phosphorylation: Effects on Force, ATPase, and Shortening
العنوان: | Regulation of Catch Muscle by Twitchin Phosphorylation: Effects on Force, ATPase, and Shortening |
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المؤلفون: | S. U. Mooers, Chenqing Li, Tom Butler, Marion J. Siegman, Srinivasa Narayan |
المصدر: | Biophysical Journal. 75(4):1904-1914 |
بيانات النشر: | Elsevier BV, 1998. |
سنة النشر: | 1998 |
مصطلحات موضوعية: | medicine.medical_specialty, ATPase, Biophysics, chemistry.chemical_element, Muscle Proteins, Calcium, Biology, In Vitro Techniques, chemistry.chemical_compound, Adenosine Triphosphate, Smooth muscle, Internal medicine, medicine, Cyclic AMP, Atpase activity, Animals, Seawater, Phosphorylation, Caenorhabditis elegans Proteins, Egtazic Acid, Adenosine Triphosphatases, Muscle, Smooth, Calmodulin-binding proteins, Bivalvia, Kinetics, Endocrinology, chemistry, Models, Chemical, biology.protein, Calmodulin-Binding Proteins, Stress, Mechanical, medicine.symptom, Adenosine triphosphate, Muscle contraction, Muscle Contraction, Research Article |
الوصف: | Recent experiments on permeabilized anterior byssus retractor muscle (ABRM) of Mytilus edulis have shown that phosphorylation of twitchin releases catch force at pCa>8 and decreases force at suprabasal but submaximum [Ca2+]. Twitchin phosphorylation decreases force with no detectable change in ATPase activity, and thus increases the energy cost of force maintenance at subsaturating [Ca2+]. Similarly, twitchin phosphorylation causes no change in unloaded shortening velocity (Vo) at any [Ca2+], but when compared at equal submaximum forces, there is a higher Vo when twitchin is phosphorylated. During calcium activation, the force-maintaining structure controlled by twitchin phosphorylation adjusts to a 30% Lo release to maintain force at the shorter length. The data suggest that during both catch and calcium-mediated submaximum contractions, twitchin phosphorylation removes a structure that maintains force with a very low ATPase, but which can slowly cycle during submaximum calcium activation. A quantitative cross-bridge model of catch is presented that is based on modifications of the Hai and Murphy (1988. Am. J. Physiol. 254:C99–C106) latch bridge model for regulation of mammalian smooth muscle. |
تدمد: | 0006-3495 |
DOI: | 10.1016/s0006-3495(98)77631-3 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3f041c30a32b15f5f8d44993d208bff |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....a3f041c30a32b15f5f8d44993d208bff |
قاعدة البيانات: | OpenAIRE |
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