Prolyl carboxypeptidase purified from human placenta: its characterization and identification as an apelin-cleaving enzyme

Biochim Biophys Acta. 2016 Nov;1864(11):1481-8. doi: 10.1016/j.bbapap.2016.07.004. Epub 2016 Jul 20.
No abstract available

Keywords: (Pyr)-apelin-13; Energy homeostasis; Enzyme kinetics; Prolyl carboxypeptidase; Substrate specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apelin
  • Carboxypeptidases / chemistry*
  • Carboxypeptidases / genetics
  • Carboxypeptidases / isolation & purification
  • Carboxypeptidases / metabolism
  • Colipases / chemistry
  • Colipases / genetics
  • Colipases / metabolism
  • Energy Metabolism / genetics
  • Enzyme Precursors / chemistry
  • Enzyme Precursors / genetics
  • Enzyme Precursors / metabolism
  • Female
  • Gene Expression
  • Ghrelin / chemistry
  • Ghrelin / genetics
  • Ghrelin / metabolism
  • Human Umbilical Vein Endothelial Cells
  • Humans
  • Intercellular Signaling Peptides and Proteins / chemistry*
  • Intercellular Signaling Peptides and Proteins / genetics
  • Intercellular Signaling Peptides and Proteins / metabolism
  • Kinetics
  • Placenta / chemistry*
  • Placenta / enzymology
  • Pregnancy
  • Proteolysis
  • Substrate Specificity
  • alpha-MSH / chemistry*
  • alpha-MSH / genetics
  • alpha-MSH / metabolism

Substances

  • APLN protein, human
  • Apelin
  • Colipases
  • Enzyme Precursors
  • Ghrelin
  • Intercellular Signaling Peptides and Proteins
  • obestatin, human
  • alpha-MSH
  • procolipase
  • Carboxypeptidases