GPAT3

Last update 23 Jan 2025

Basic Info

Synonyms

1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10, 1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9, 1-AGP acyltransferase 9

+ [16]

Introduction

Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone (PubMed:17170135). Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:19318427). Protects cells against lipotoxicity (PubMed:30846318).

100 Clinical Results associated with GPAT3

100 Translational Medicine associated with GPAT3

0 Patents (Medical) associated with GPAT3

1,150

Literatures (Medical) associated with GPAT3

01 Feb 2025·American Journal of Physiology-Renal Physiology

Glycerol-3-phosphate contributes to the increase in FGF23 production in chronic kidney disease

Article

Author: Zhou, Wen ; Cherukuru, Rohan ; Adams, Michael A ; Xie, Han ; Zhang, Qian ; Rhee, Eugene P ; Simic, Petra ; Turner, Mandy E

This study shows that glycerol-3-phosphate, a glycolytic by-product recently implicated in a kidney-to-bone signaling axis that regulates FGF23 production, increases in mice and rats with CKD. Furthermore, mice deficient in a key enzyme that synthesizes glycerol-3-phosphate have attenuated increases in both glycerol-3-phosphate and FGF23 in CKD, along with enhanced cortical bone loss. These studies identify glycerol-3-phosphate as a novel regulator of FGF23 and mineral metabolism in CKD.

01 Jan 2025·International Immunopharmacology

Immunoproteomic analysis and identification of possible allergenic proteins in Artemisia annua pollen

Article

Author: Wang, Mei ; Ma, Jingui ; Yang, Zhigang ; Ma, Fen ; Sa, Yuping ; Wang, Weibiao ; He, Xinmin ; Ma, Xueqin ; Chen, Guoning ; Zhang, Weiman

BACKGROUNDArtemisia annua (A. annua) is a wind-pollinated weed and a major allergen responsible for allergic respiratory diseases in Northern China.METHODSThis study involved the separation of pollen proteins from A. annua utilizing SDS-PAGE and Coomassie Blue staining techniques. The effectiveness of extracting allergens from Artemisia annua pollen (AAP) were confirmed both in vivo and in vitro. A mouse model was established using A. annua pollen (AAP) extracts. In vitro, the interaction between allergenic proteins in the AAP extract and specific IgE antibodies present in patients' sera was analyzed, using IgE-immunoblotting and ELISA methods. Protein bands were subsequently analyzed by mass spectrometry. The recombinant Art an 3 (rArt an 3) protein was obtained via recombination, expression, and purification. Finally, the binding activity of rArt an 3 specific IgE was subsequently examined using Western blot and inhibition ELISA (iELISA).RESULTSThe electrophoretic profiles of AAP showed band patterns ranging from 10 to 70 kDa, with the most prominet IgE-binding pollen proteins detected at approximately 12 kDa. After stimulation of AAP, the sensitized group of mice exhibited significant allergic symptoms compared to the control group. Mass spectrometry analysis identified 7 proteins, including putative aldehyde oxidase Art an 7, Art v 1-like protein, Art an 3.0101 allergen precursor, Art an 3.0102 allergen precursor, Art an 3.0201 allergen precursor, lipid transfer protein 3, and non-specific lipid-transfer protein. The results of immunoblotting and iELISA showed that rArt an 3 could bind to IgE antibodies in the patient sera, and co-incubation of rArt an 3 with serum, the binding serum significantly inhibited IgE binding to the crude AAP.CONCLUSIONSThe Art an 3 is a key allergenic protein in AAP with a high IgE sensitization rate in the studied population sample. These findings enhance our understanding of the sensitization components of AAP and its sensitization characteristics within the Chinese population, thereby promoting the development of precise molecular diagnostics and therapeutic interventions.

01 Jan 2025·Molecular and Cellular Endocrinology

FSH increases lipid droplet content by regulating the expression of genes related to lipid storage in Rat Sertoli cells

Article

Author: Riera, Maria Fernanda ; Meroni, Silvina Beatriz ; Centola, Cecilia Lucia ; Dasso, Marina Ercilia ; Galardo, Maria Noel

Sertoli cells (SCs) are essential for appropriate spermatogenesis. From a metabolic standpoint, they catabolize glucose and provide germ cells with lactate, which is their main energy source. SCs also oxidize fatty acids (FAs), which are stored as triacylglycerides (TAGs) within lipid droplets (LDs), to fulfill their own energy requirements. On the other hand, it has been demonstrated that FSH regulates some of SCs functions, but little is known about its effect on lipid metabolism. In the present study, we aimed to analyze FSH-mediated regulation of (1) lipid storage in LDs and (2) the expression of genes involved in FAs activation and TAG synthesis and storage in SCs. SCs obtained from 20-day-old rats were cultured for different incubation periods with FSH (100 ng/ml). It was observed that FSH increased LD content and TAG levels in SCs. There were also increments in the expression of Plin1, Fabp5, Acsl1, Acsl4, Gpat3, and Dgat1, which suggests that these proteins may mediate the increase in TAGs and LDs elicited by FSH. Regarding the signaling involved in FSH actions, it was observed that dbcAMP increased LD, and H89, a PKA inhibitor, inhibited FSH stimulus. Also, dbcAMP increased Plin2, Fabp5, Acsl1, Acsl4, and Dgat1 mRNA levels, confirming a role of the cAMP/PKA pathway in the regulation of lipid storage in SCs. Altogether, these results suggest that FSH, via the cAMP/PKA pathway, regulates lipid storage in SCs ensuring the availability of substrates to satisfy their energy requirements.

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GPAT3

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