Format

Send to

Choose Destination
Comp Biochem Physiol B Biochem Mol Biol. 2016 Apr-May;194-195:65-70. doi: 10.1016/j.cbpb.2016.01.010. Epub 2016 Jan 28.

Myostatin inhibitory region of fish (Paralichthys olivaceus) myostatin-1 propeptide.

Author information

1
Department of Marine Molecular Biotechnology, Gangneung-Wonju National University, Gangneung-si, Ganwon-do, 210-702, South Korea; Department of Human Nutrition, Food and Animal Sciences, University of Hawaii, 1955 East-West Rd., Honolulu, HI 96822, USA.
2
Department of Marine Molecular Biotechnology, Gangneung-Wonju National University, Gangneung-si, Ganwon-do, 210-702, South Korea.
3
Department of Marine Molecular Biotechnology, Gangneung-Wonju National University, Gangneung-si, Ganwon-do, 210-702, South Korea. Electronic address: hj-jin@gwnu.ac.kr.
4
Department of Human Nutrition, Food and Animal Sciences, University of Hawaii, 1955 East-West Rd., Honolulu, HI 96822, USA. Electronic address: ykim@hawaii.edu.

Abstract

Myostatin (MSTN) is a potent negative regulator of skeletal muscle growth, and its activity is suppressed by MSTN propeptide (MSTNpro), the N-terminal part of MSTN precursor cleaved during post-translational MSTN processing. The current study examined which region of flatfish (Paralichthys olivaceus) MSTN-1 propeptide (MSTN1pro) is critical for MSTN inhibition. Six different truncated forms of MSTN1pro containing N-terminal maltose binding protein (MBP) as a fusion partner were expressed in Escherichia coli, and partially purified by an affinity chromatography for MSTN-inhibitory activity examination. Peptides covering different regions of flatfish MSTN1pro were also synthesized for MSTN-inhibitory activity examination. A MBP-fused MSTN1pro region consisting of residues 45-100 had the same MSTN-inhibitory potency as the full sequence flatfish MSTN1pro (residues 23-265), indicating that the region of flatfish MSTN1pro consisting of residues 45-100 is sufficient to maintain the full MSTN-inhibitory capacity. A MBP-fused MSTN1pro region consisting of residues 45-80 (Pro45-80) also showed MSTN-inhibitory activity with a lower potency, and the Pro45-80 demonstrated its MSTN binding capacity in a pull-down assay, indicating that the MSTN-inhibitory capacity of Pro45-80 is due to its binding to MSTN. Flatfish MSTN1pro synthetic peptides covering residues 45-65, 45-70, and 45-80 demonstrated MSTN-inhibitory activities, but not the synthetic peptide covering residues 45-54, indicating that residues 45-65 of flatfish MSTN1pro are essential for MSTN inhibition. In conclusion, current study show that like the mammalian MSTNpro, the MSTN-inhibitory region of flatfish MSTN1pro resides near its N-terminus, and imply that smaller sizes of MSTNpro can be effectively used in various applications designed for MSTN inhibition.

KEYWORDS:

Fish myostatin propeptide; Inhibitory region; Myostatin; Myostatin propeptide; Paralichthys olivaceus; Truncated protein

PMID:
26827850
DOI:
10.1016/j.cbpb.2016.01.010
[Indexed for MEDLINE]

Publication types, MeSH terms, Substances

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center