ABHD16B

Last update 08 May 2025

Basic Info

Synonyms

ABHD16B, abhydrolase domain containing 16B, Abhydrolase domain-containing protein 16B

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Introduction

Hydrolyzes the sn-1 position of glycerophospholipids with high specificity towards phosphatidylserine (PS), PS-PLA1 enzyme (PubMed:36841071). Also hydrolyzes the acyl chain of glycerolipids with a preference for the monoacylglycerol (MAG) 1-acylglycerol, MAG lipase (PubMed:36841071). Plays a regulatory role in cellular lipid homeostasis by modulating genes involved in neutral lipid degradation and in phospholipid synthesis and composition (PubMed:37944658).

100 Clinical Results associated with ABHD16B

100 Translational Medicine associated with ABHD16B

0 Patents (Medical) associated with ABHD16B

Literatures (Medical) associated with ABHD16B

01 Jan 2024·Chemistry and Physics of Lipids

Elucidating the functional role of human ABHD16B lipase in regulating triacylglycerol mobilization and membrane lipid synthesis in Saccharomyces cerevisiae

Article

Author: Rajasekharan, Ram ; Usharani, Dandamudi ; Narayanasamy, Raja

Lipids are essential biological macromolecules that play a pivotal role in various physiological processes and cellular homeostasis. ABHD16B, a member of the α/β-hydrolase domain (ABHD) superfamily protein, has emerged as a potential key regulator in lipid metabolism. However, the precise role of human ABHD16B in lipid metabolism remains unclear. In this study, we reported the overexpression of ABHD16B in Saccharomyces cerevisiae to determine its physiological relevance in lipid metabolism. Through in vivo [¹⁴C]acetate labeling experiments, we observed that overexpression of ABHD16B causes a decrease in cellular triacylglycerol (TAG) levels and a concurrent increase in phospholipid synthesis in wild-type cells. Mass spectrometry (LC-MS/MS) analysis further corroborated these findings, showing a significant decrease in TAGs with a carbon chain length of 48 and an increase in major phospholipid species, specifically 34:2, upon overexpression of ABHD16B. Confocal microscopy analysis revealed a reduction in the number of lipid droplets in strains overexpressing ABHD16B, consistent with the observed decrease in neutral lipids. Additionally, qRT-PCR analysis indicated a high phospholipid synthetic activity of ABHD16B and a potential decrease in TAG levels in wild-type yeast, possibly due to upregulation of endogenous TAG hydrolytic enzymes, as confirmed using 3tglsΔ mutant strain. Furthermore, GC-MS analysis revealed significant modifications in fatty acid composition upon ABHD16B overexpression. Collectively, our results underscore the influence of ABHD16B overexpression on TAG levels, phospholipid synthesis, lipid droplet dynamics, and fatty acid composition. These findings reveal a complex interplay between TAG hydrolysis and phospholipid synthesis, highlighting the critical involvement of ABHD16B in lipid homeostasis and providing further insights into its regulatory function in cellular lipid metabolism.

01 May 2023·Biophysical Chemistry

Molecular insights on PS-PLA1 lipase activity of human ABHD16B

Article

Author: Usharani, Dandamudi ; Rajasekharan, Ram ; Narayanasamy, Raja

The human alpha beta hydrolase domain (ABHD) proteins are ubiquitous and regulate the cellular lipids' anabolic and catabolic processes. The structural aspects for specific biochemical function of many ABHD proteins related to physiological disorders and its link to pathological conditions remain unknown. Here putative human ABHD16B protein was overexpressed in Saccharomyces cerevisiae for its biological activity. In-vitro enzymatic assay of the recombinant ABHD16B protein with fluorescently tagged glycerophospholipids revealed that the PLA₁ activity is observed with phosphatidylserine (PS). In addition, it efficiently hydrolyzed monoacylglycerol over triacylglycerols. Further, molecular dynamic simulations and per residue binding free energy decomposition analysis revealed that the origin of PS-specific PLA₁ activity of ABHD16B is due to the electrostatic interaction of the PS head group with K8, R319, and E178, which led to having the hydrogen bond interaction of sn-1 acyl chain ester to the catalytic site residues. Site-directed mutagenesis of the ²⁴⁵GXSXG²⁴⁹ motif of ABHD16B reduced the maximal lipase activity of PS and MAG. In summary, these results revealed that ABHD16B plays a vital role in PS selectivity that in turn, controls the specific subcellular pools of 2-LPS metabolism in the tissues at low pH.

15 Dec 2012·American Journal of Respiratory and Critical Care MedicineQ1 · MEDICINE

Systemic Steroid Exposure Is Associated with Differential Methylation in Chronic Obstructive Pulmonary Disease

Q1 · MEDICINE

Article

Author: Lomas, David A. ; Wan, Emily S. ; Bacherman, Helene ; DeMeo, Dawn L. ; Anderson, Wayne H. ; Carey, Vincent J. ; Qiu, Weiliang ; Rennard, Stephen I. ; Agustí, Alvar ; Baccarelli, Andrea

RATIONALESystemic glucocorticoids are used therapeutically to treat a variety of medical conditions. Epigenetic processes such as DNA methylation may reflect exposure to glucocorticoids and may be involved in mediating the responses and side effects associated with these medications.OBJECTIVESTo test the hypothesis that differences in DNA methylation are associated with current systemic steroid use.METHODSWe obtained DNA methylation data at 27,578 CpG sites in 14,475 genes throughout the genome in two large, independent cohorts: the International COPD Genetics Network (n(discovery) = 1,085) and the Boston Early Onset COPD study (n(replication) = 369). Sites were tested for association with current systemic steroid use using generalized linear mixed models.MEASUREMENTS AND MAIN RESULTSA total of 511 sites demonstrated significant differential methylation by systemic corticosteroid use in all three of our primary models. Pyrosequencing validation confirmed robust differential methylation at CpG sites annotated to genes such as SLC22A18, LRP3, HIPK3, SCNN1A, FXYD1, IRF7, AZU1, SIT1, GPR97, ABHD16B, and RABGEF1. Functional annotation clustering demonstrated significant enrichment in intrinsic membrane components, hemostasis and coagulation, cellular ion homeostasis, leukocyte and lymphocyte activation and chemotaxis, protein transport, and responses to nutrients.CONCLUSIONSOur analyses suggest that systemic steroid use is associated with site-specific differential methylation throughout the genome. Differentially methylated CpG sites were found in biologically plausible and previously unsuspected pathways; these genes and pathways may be relevant in the development of novel targeted therapies.

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ABHD16B

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