Biosynthesis of phosphatidylcholine by human lysophosphatidylcholine acyltransferase 1

Phosphatidylcholine formation by LPCAT1 is regulated by Ca2+ and the redox status of the cell

“…As observed previously [34], we confirmed that substitution of Cys-211 to most other residues greatly reduced activity of LPCAT1, resulting in enzymes with low or no detectable activity (Figure 4). However, one mutant form, C 211 T, could produce as much PC as LPCAT1 (Figure 4A), with an activity rate of about 60% of LPCAT1 (Figure 4B).…”

The expression level of lysophosphatidylcholine acyltransferase 1 (LPCAT1) correlates to the progression of prostate cancer

“…A human homolog of mouse LPCAT1, 1-acylglycerol-3-phosphate-Oacyltransferase isoform 9 (AGPAT9) was cloned and characterized by Agarwal et al AGPAT9 was demonstrated to be able to catalyze the synthesis of phosphatidic acid (PA), however, it failed to show LPCAT activity (10). Subsequently, human LPCAT1 was reported to exhibit activities of both lysophosphatidylcholine acyltransferase (LPCAT) and lysophosphatidylglycerol acyltransferase (LPGAT) by Harayama et al (11). In addition to its significance in production of DPPC (8–9, 12) and in retinal photoreceptor homeostasis (13–14), LPCAT1 was found to be overexpressed in colorectal adenocarcinomas as compared to normal rectal mucosa and shown a weak immunohistochemical signal in prostate cancer (15).…”

Histopathological and ultra-structural characterization of local neuromuscular damage induced by repeated phosphatidylcholine/deoxycholate injection

“…Cell culture studies raised the possibility that PC/DC mixture dissolves local fat deposits in a nonspecific manner (Gupta et al, 2009). DC, being an emulsifier, is implicated in nonspecific fat lysis causing fat dissolution (Harayama et al, 2009). Alternatively, increased PC in cell membranes can accelerate lipolysis by improving sensitivity to insulin (Vance and Vance, 2004).…”