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J Lipid Res. 2016 Apr;57(4):538-45. doi: 10.1194/jlr.R063032. Epub 2015 Nov 22.

GPI-AP release in cellular, developmental, and reproductive biology.

Author information

1
Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan.
2
Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan ikawa@biken.osaka-u.ac.jp.

Abstract

Glycosylphosphatidylinositol-anchored proteins (GPI-APs) contain a covalently linked GPI anchor located on outer cell membranes. GPI-APs are ubiquitously conserved from protozoa to vertebrates and are critical for physiological events such as development, immunity, and neurogenesis in vertebrates. Both membrane-anchored and soluble GPI-APs play a role in regulating their protein conformation and functional properties. Several pathways mediate the release of GPI-APs from the plasma membrane by vesiculation or cleavage. Phospholipases and putative substrate-specific GPI-AP-releasing enzymes, such as NOTUM, glycerophosphodiesterase 2, and angiotensin-converting enzyme, have been characterized in mammals. Here, the protein modifications resulting from the cleavage of the GPI anchor are discussed in the context of its physiological functions.

KEYWORDS:

GPIase; IZUMO1 receptor/JUNO; gene expression; genetics; glycosylphosphatidylinositol-anchored protein; glypican; membranes; phospholipases; phospholipids/phosphatidylinositol; reversion-inducing cysteine-rich protein with kazal motifs; testis-expressed gene 101

PMID:
26593072
PMCID:
PMC4808780
DOI:
10.1194/jlr.R063032
[Indexed for MEDLINE]
Free PMC Article

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