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Literature summary for 2.3.1.23 extracted from

  • Taniguchi, K.; Hikiji, H.; Okinaga, T.; Hashidate-Yoshida, T.; Shindou, H.; Ariyoshi, W.; Shimizu, T.; Tominaga, K.; Nishihara, T.
    Essential role of lysophosphatidylcholine acyltransferase 3 in the induction of macrophage polarization in PMA-treated U937 cells (2015), J. Cell. Biochem., 116, 2840-2848.
    View publication on PubMed

Application

Application Comment Organism
pharmacology the enzyme is a potential therapeutic targets for the regulation of immune and inflammatory disorders Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
gene LPCAT3, quantitative real-time RT-PCR enzyme expression analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information LPCAT3 isozyme knockdown to about 25% activity in U-937 cells by siRNA. LPCAT3 siRNA-transfected cells show a spindle-shaped. morphology similar to that of M1-polarized macrophages, whereas control siRNAtransfected cells show a rounded morphology typical ofM2-polarized macrophages. Knockdown of LPCAT3 in phorbol ester-treated U-937 cells decreases LPCAT activity toward linoleoyl-CoA and arachidonoyl-CoA Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
lipopolysaccharide suppresses the enzyme activity of isozyme LPCAT3 toward linoleoyl-CoA and arachidonoyl-CoA in phorbol 12-myristate 13-acetate-treated U-937 cells Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine Homo sapiens
-
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q6P1A2 LPCAT3, one of four isozymes, gene LPCAT3
-

Source Tissue

Source Tissue Comment Organism Textmining
leukemia cell
-
Homo sapiens
-
macrophage
-
Homo sapiens
-
monocyte
-
Homo sapiens
-
U-937 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
-
Homo sapiens CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
arachidonoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
-
Homo sapiens CoA + 1-acyl-2-arachidonoyl-sn-glycero-3-phosphocholine
-
?
linoleoyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
-
Homo sapiens CoA + 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine
-
?

Synonyms

Synonyms Comment Organism
LPCAT3
-
Homo sapiens
lysophosphatidylcholine acyltransferase 3
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

Expression

Organism Comment Expression
Homo sapiens lipopolysaccharide significantly downregulates the mRNA expression of isozyme LPCAT3 down

General Information

General Information Comment Organism
malfunction LPCAT3 knockdown induces a spindle-shaped morphology typical of M1-polarized macrophages, increases the secretion of CXCL10, and decreases the levels of CD206 in interleukin-4-activated U-937 cells. Knockdown of LPCAT3 shifts the differentiation of phorbol ester-treated U-937 cells to M1-polarized macrophages. Decrease in the content of phosphatidylcholine containing linoleic acid or arachidonic acid in biological membranes caused by the suppression of LPCAT3 may influencemembrane fluidity, curvature and function Homo sapiens
physiological function lysophospholipid acyltransferases (LPLATs) regulate the diversification of fatty acid composition in biological membranes. Lysophosphatidylcholine acyltransferases (LPCATs) are members of the LPLATs that play a role in inflammatory responses. LPCAT3 is reported to be a major contributor to increase polyunsaturated fatty acids, including linoleic acid and arachidonic acid, and is associated with inflammatory responses in human primary macrophages, and the enzyme LPCAT3 plays an important role in M1/M2-macrophage polarization, analysis of the underlying mechanism Homo sapiens