Display options
Share it on

J Proteome Res. 2014 Aug 01;13(8):3802-3809. doi: 10.1021/pr5004642. Epub 2014 Jun 30.

Method Development for the Detection of Human Myostatin by High-Resolution and Targeted Mass Spectrometry.

Journal of proteome research

Hassendrini Nileishika Peiris, Keith Ashman, Kanchan Vaswani, David Kvaskoff, Gregory Edward Rice, Murray David Mitchell

Affiliations

  1. The University of Queensland Centre for Clinical Research, Royal Brisbane and Women's Hospital , Herston, Brisbane QLD 4029, Australia.

PMID: 24949862 DOI: 10.1021/pr5004642

Abstract

Myostatin, a highly conserved secretory protein, negatively regulates muscle development, affecting both the proliferation and differentiation of muscle cells. Proteolytic processing of the myostatin precursor protein generates a myostatin pro-peptide and mature protein. Dimerization of the mature myostatin protein creates the active form of myostatin. Myostatin dimer activity can be inhibited by noncovalent binding of two monomeric myostatin pro-peptides. This ability for myostatin to self-regulate as well as the altered expression of myostatin in states of abnormal health (e.g., muscle wasting) support the need for specific detection of myostatin forms. Current protein detection methods (e.g., Western blot) rely greatly on antibodies and are semiquantitative at best. Tandem mass spectometry (as in this study) provides a highly specific method of detection, enabling the characterization of myostatin protein forms through the analysis of discrete peptides fragments. Utilizing the scheduled high-resolution multiple reaction monitoring paradigm (sMRM

Keywords: GDF-8; Myostatin; mass spectrometry

Publication Types