Recombinant Human GPI-PLD protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Glycosylphosphatidylinositol specific phospholipase D1 (GPI-PLD) is an enzyme that hydrolyzes glycosylphosphatidylinositol (GPI)-anchored proteins. Also known as GPLD1 it acts by cleaving the inositol phosphate linkage. GPI-PLD possesses a molecular mass of about 110 kDa and is found extensively in the plasma signaling its secretion from the liver. In certain studies researchers occasionally refer to it by its involved function in detaching GPI proteins.

Biological function summary

GPI-PLD participates in remodeling the cell surface by releasing certain GPI-anchored proteins. It impacts cellular events like signal transduction and cell adhesion. GPI-PLD functions independently not as part of a larger complex. Observation of GPI-PLD activities reveals involvement in regulating immune responses as well as interactions with other proteins on cell membranes. Its ability to influence GPI protein release affects how cells communicate and adapt in various biological contexts.

Pathways

The enzyme GPI-PLD plays a role in pathways involving lipid metabolism and the immune system particularly complement system activation. GPI-PLD collaborates with proteins such as phospholipase C in lipid regulatory pathways. Its activity impacts the balance and turnover of lipids which affects the complement cascade by modulating membrane-bound proteins. Through these interactions GPI-PLD participates in refining how immune responses unfold affecting related biological processes.

Research shows that GPI-PLD has connections with conditions like atherosclerosis and diabetes. Changes in its enzymatic activity and expression levels impact lipid metabolism which ties to atherosclerosis development. In diabetes improper regulation of GPI-PLD can alter inflammatory and immune responses. The enzyme's activity further connects with lipoprotein interactions placing emphasis on its link with apolipoprotein AI indicating a broader influence in disorders related to lipid metabolism and inflammation.