Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle
Global cooling: Cold acclimation and the expression of soluble proteins in carp skeletal muscle
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DOI：
10.1002/pmic.200601004
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发表时间：
2007-08-01
期刊：
影响因子：
3.4
通讯作者：
Whitfield, Phillip D.
中科院分区：
文献类型：
--
作者：
McLean, Lynn;Young, Iain S.;Whitfield, Phillip D.
普通鲤鱼（Cyprinus carpio）具有良好的能力来改变肌肉特性以响应温度的变化。了解在蛋白质水平上支持这种表型反应的机制可能会为骨骼肌适应性过程的分子基础提供基本的见解。本研究以鲤鱼为材料，采用低温处理，对鲤鱼肌肉匀浆可溶性提取物进行1-D SDS-PAGE和2-DE分离。蛋白质鉴定使用MALDI-TOF-MS和从头肽测序使用LC-MS/MS。2-D凝胶填充有许多蛋白质点，是鲤鱼肌酸激酶（CK）的所有三种肌肉亚型（M1，M2和M3）的片段。当鲤鱼冷却到10 ℃时，CK片段的积累增加。在骨骼肌中观察到的蛋白质的变化进行了比较，在以前的转录本分析研究中描述的变化。编码CK亚型的基因下调，编码泛素-蛋白酶体途径关键蛋白的基因上调。这些发现是一致的一个特定的冷诱导增强CK的蛋白水解。
The common carp (Cyprinus carpio) has a well-developed capacity to modify muscle properties in response to changes in temperature. Understanding the mechanisms underpinning this phenotypic response at the protein level may provide fundamental insights into the molecular basis of adaptive processes in skeletal muscle. In this study, common carp were subjected to a cooling regimen and soluble extracts of muscle homogenates were separated by 1-D SDS-PAGE and 2-DE. Proteins were identified using MALDI-TOF-MS and de novo peptide sequencing using LC-MS/MS. The 2-D gel was populated with numerous protein spots that were fragments of all three muscle isoforms (M1, M2 and M3) of carp creatine kinase (CK). The accumulation of the CK fragments was enhanced when the carp were cooled to 10 degrees C. The protein changes observed in the skeletal muscle of carp subjected to cold acclimation were compared to changes described in a previous transcript analysis study. Genes encoding CK isoforms were downregulated and the genes encoding key proteins of the ubiquitin-proteasome pathway were upregulated. These findings are consistent with a specific cold-induced enhancement of proteolysis of CK.