Ontology highlight
ABSTRACT:
SUBMITTER: Shin K
PROVIDER: S-EPMC3821026 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Shin Kyungsoo K Pandey Aditya A Liu Xiang-Qin XQ Anini Younes Y Rainey Jan K JK
FEBS open bio 20130809
The peptide hormone apelin is translated as a 77-residue preproprotein, truncated to the 55-residue proapelin and, subsequently, to 13-36-residue bioactive isoforms named apelin-13 to -36. Proapelin is hypothesized to be cleaved to apelin-36 and then to the shorter isoforms. However, neither the mechanism of proapelin processing nor the endoproteases involved have been determined. We show direct cleavage of proapelin to apelin-13 by proprotein convertase subtilisin/kexin 3 (PCSK3, or furin) in v ...[more]