Will Quantitative Proteomics Redefine Some of the Key Concepts in Skeletal Muscle Physiology?

Proteomes

Agnieszka Gizak¹  Dariusz Rakus²  Jacek R. Wisniewski² 

[1] Department of Animal Molecular Physiology, Wroclaw University, Cybulskiego 30, 50-205 Wroclaw, Poland

关键词: C2C12 cells;    kcat;    glyconeogenesis;    glycolysis regulation;    lysine acetylation;    skeletal muscle;   

DOI  :  10.3390/proteomes4010002

来源: mdpi

【 摘 要 】

Molecular and cellular biology methodology is traditionally based on the reasoning called “the mechanistic explanation”. In practice, this means identifying and selecting correlations between biological processes which result from our manipulation of a biological system. In theory, a successful application of this approach requires precise knowledge about all parameters of a studied system. However, in practice, due to the systems’ complexity, this requirement is rarely, if ever, accomplished. Typically, it is limited to a quantitative or semi-quantitative measurements of selected parameters (e.g., concentrations of some metabolites), and a qualitative or semi-quantitative description of expression/post-translational modifications changes within selected proteins. A quantitative proteomics approach gives a possibility of quantitative characterization of the entire proteome of a biological system, in the context of the titer of proteins as well as their post-translational modifications. This enables not only more accurate testing of novel hypotheses but also provides tools that can be used to verify some of the most fundamental dogmas of modern biology. In this short review, we discuss some of the consequences of using quantitative proteomics to verify several key concepts in skeletal muscle physiology.

【 授权许可】

CC BY   
© 2016 by the authors; licensee MDPI, Basel, Switzerland.