| Autor: |
Yaginuma S; Faculty of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan., Kawana H; Faculty of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan., Aoki J; Faculty of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan. |
| Jazyk: |
angličtina |
| Zdroj: |
Molecules (Basel, Switzerland) [Molecules] 2022 Apr 12; Vol. 27 (8). Date of Electronic Publication: 2022 Apr 12. |
| DOI: |
10.3390/molecules27082487 |
| Abstrakt: |
Phospholipase A 1 (PLA 1 ) is an enzyme that cleaves an ester bond at the sn -1 position of glycerophospholipids, producing a free fatty acid and a lysophospholipid. PLA 1 activities have been detected both extracellularly and intracellularly, which are well conserved in higher eukaryotes, including fish and mammals. All extracellular PLA 1 s belong to the lipase family. In addition to PLA 1 activity, most mammalian extracellular PLA 1 s exhibit lipase activity to hydrolyze triacylglycerol, cleaving the fatty acid and contributing to its absorption into the intestinal tract and tissues. Some extracellular PLA 1 s exhibit PLA 1 activities specific to phosphatidic acid (PA) or phosphatidylserine (PS) and serve to produce lysophospholipid mediators such as lysophosphatidic acid (LPA) and lysophosphatidylserine (LysoPS). A high level of PLA 1 activity has been detected in the cytosol fractions, where PA-PLA 1 /DDHD1/iPLA 1 was responsible for the activity. Many homologs of PA-PLA 1 and PLA 2 have been shown to exhibit PLA 1 activity. Although much has been learned about the pathophysiological roles of PLA 1 molecules through studies of knockout mice and human genetic diseases, many questions regarding their biochemical properties, including their genuine in vivo substrate, remain elusive. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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