Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretch
about
Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodelingTargeted proteolysis of plectin isoform 1a accounts for hemidesmosome dysfunction in mice mimicking the dominant skin blistering disease EBS-OgnaCalcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases.Calpain3 is expressed in a proteolitically active form in papillomavirus-associated urothelial tumors of the urinary bladder in cattle.Excision of titin's cardiac PEVK spring element abolishes PKCalpha-induced increases in myocardial stiffnessCalpain 3 is important for muscle regeneration: evidence from patients with limb girdle muscular dystrophies.Altered cross-bridge properties in skeletal muscle dystrophiesThe role of proteases in excitation-contraction coupling failure in muscular dystrophy.Altered ubiquitin causes perturbed calcium homeostasis, hyperactivation of calpain, dysregulated differentiation, and cataract.L-arginine supplementation protects exercise performance and structural integrity of muscle fibers after a single bout of eccentric exercise in rats.Absence of Dystrophin Disrupts Skeletal Muscle Signaling: Roles of Ca2+, Reactive Oxygen Species, and Nitric Oxide in the Development of Muscular Dystrophy.What does the membrane K(ATP) channel really do in skeletal muscle?Dysregulation of calcium homeostasis in muscular dystrophies.Characterization of Muscle Ankyrin Repeat Proteins in human skeletal muscle.Activity, abundance and expression of Ca²⁺-activated proteases in skeletal muscle of the aestivating frog, Cyclorana alboguttata.Skeletal muscle atrophy in sedentary Zucker obese rats is not caused by calpain-mediated muscle damage or lipid peroxidation induced by oxidative stress.Sex differences in intracellular Ca(2+) accumulation following eccentric contractions of rat skeletal muscle in vivo.Acute change of titin at mid-sarcomere remains despite 8 wk of plyometric training.Calpain-3 is activated following eccentric exercise.Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans.Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers.CAPN3-mediated processing of C-terminal titin replaced by pathological cleavage in titinopathy.When phosphorylated at Thr148, the β2-subunit of AMP-activated kinase does not associate with glycogen in skeletal muscle.Single fiber analyses of glycogen-related proteins reveal their differential association with glycogen in rat skeletal muscle
P2860
Q24294688-603925D8-13C3-4252-9220-43CA3F89796CQ27335461-1B2395D5-BA9E-4C14-8C09-453C3503C62BQ33506801-9BAAAA73-D5B2-453E-B878-E6F1AA17ECBFQ33565470-4DC6F241-7F8E-4A25-A179-D3C3488C46AFQ33787977-9C78408B-CA04-4529-9DC2-9752A5DFC7EDQ34207404-D52C84D6-B87D-44D1-92D0-8E46A6E3F1F8Q34335939-1B96228E-9742-4AB2-91FD-FC8BD614B115Q34800803-5B79E44B-EA36-4653-A589-6602B105C5DBQ35038062-905F819C-ACA2-42F9-A991-C25DF2EE18A8Q35149368-93311A0E-4AE6-4536-9074-14C17D4E2142Q36422465-B64A93CE-3079-45BB-A080-E4A41A5E9752Q37809623-1D994FF2-D4AE-4E12-A237-22677C469AA1Q38257886-289EB4D3-7580-454C-A50B-ADAF51C1263AQ38725504-06C069BF-F375-4BE5-BB50-63000BE50D6AQ41696195-E1048BB7-6743-4E2A-BD1F-1D236721FA89Q41827896-8E70D896-FCAB-4B9E-B95C-A13EAA7A9636Q42970181-141B6319-4727-4D36-A901-20A1C6F4EA32Q46763944-1246EC2C-9962-42B0-A68C-0216CB10C1E3Q47721953-D6269077-1C54-4CBD-A368-1534435F10CCQ48170243-7C8D51CD-3714-4765-B436-A52EF4C529EEQ51763103-3D44F080-00B6-43DD-A4BE-DF9A38577A38Q52951368-ADCC3936-DCF1-43C3-81BA-B6D1281F4E2CQ53118181-5F07DA51-C8F4-49D2-AF00-E3C0D10F1D22Q57834212-580FED01-42CA-4A5F-B6A6-19081BBEAD79
P2860
Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretch
description
2009 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2009
@ast
im März 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/03/20)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/03/20)
@nl
наукова стаття, опублікована в березні 2009
@uk
name
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@ast
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@en
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@nl
type
label
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@ast
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@en
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@nl
prefLabel
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@ast
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@en
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@nl
P2860
P356
P1476
Endogenous calpain-3 activatio ...... nd is not dependent on stretch
@en
P2093
Graham D Lamb
P2860
P304
P356
10.1074/JBC.M808655200
P407
P577
2009-01-14T00:00:00Z