Lysophospholipid acyltransferases: 1-acylglycerol-3-phosphate O-acyltransferases. From discovery to disease

Curr Opin Lipidol. 2012 Aug;23(4):290-302. doi: 10.1097/MOL.0b013e328354fcf4.

Abstract

Purpose of review: Over the past several years, many more isoforms for the same enzymes, specifically for 1-acylglycerol-3-phosphate O-acyltransferases (AGPATs), have been cloned and studied. In this review, we summarize their biochemical features and discuss their functional role.

Recent findings: The most significant role of these AGPATs appeared from our observation of AGPAT2 in the biology of adipose tissue (adipocytes) in humans and mice. Other isoforms are shown to be implicated in lung, reproductive and cardiac muscle function and in the cause of cancer. In-vitro substrate specificities of these AGPATs also suggest the in-vivo role of these AGPATs in remodeling of several of the glycerophospholipids.

Summary: Despite significant progress in understanding the role of these AGPATs, much is still to be discovered in terms of how each of these AGPATs function in the presence or absence of other AGPATs and what their functional role might be.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • 1-Acylglycerol-3-Phosphate O-Acyltransferase* / chemistry
  • 1-Acylglycerol-3-Phosphate O-Acyltransferase* / genetics
  • 1-Acylglycerol-3-Phosphate O-Acyltransferase* / metabolism
  • 1-Acylglycerophosphocholine O-Acyltransferase* / chemistry
  • 1-Acylglycerophosphocholine O-Acyltransferase* / genetics
  • 1-Acylglycerophosphocholine O-Acyltransferase* / metabolism
  • Amino Acid Sequence
  • Animals
  • Disease* / genetics
  • Genome-Wide Association Study
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Molecular Sequence Data

Substances

  • Isoenzymes
  • 1-Acylglycerophosphocholine O-Acyltransferase
  • 1-Acylglycerol-3-Phosphate O-Acyltransferase