Role of fatty acid transport protein 4 in metabolic tissues: insights into obesity and fatty liver disease.
acyl CoA synthetase
fatty acid transport protein 4
fatty acids
lipidomics
phospholipids
triglycerides
Journal
Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797
Informations de publication
Date de publication:
30 06 2022
30 06 2022
Historique:
received:
20
10
2021
revised:
16
05
2022
accepted:
17
05
2022
pubmed:
19
5
2022
medline:
3
6
2022
entrez:
18
5
2022
Statut:
ppublish
Résumé
Fatty acid (FA) metabolism is a series of processes that provide structural substances, signalling molecules and energy. Ample evidence has shown that FA uptake is mediated by plasma membrane transporters including FA transport proteins (FATPs), caveolin-1, fatty-acid translocase (FAT)/CD36, and fatty-acid binding proteins. Unlike other FA transporters, the functions of FATPs have been controversial because they contain both motifs of FA transport and fatty acyl-CoA synthetase (ACS). The widely distributed FATP4 is not a direct FA transporter but plays a predominant function as an ACS. FATP4 deficiency causes ichthyosis premature syndrome in mice and humans associated with suppression of polar lipids but an increase in neutral lipids including triglycerides (TGs). Such a shift has been extensively characterized in enterocyte-, hepatocyte-, and adipocyte-specific Fatp4-deficient mice. The mutants under obese and non-obese fatty livers induced by different diets persistently show an increase in blood non-esterified free fatty acids and glycerol indicating the lipolysis of TGs. This review also focuses on FATP4 role on regulatory networks and factors that modulate FATP4 expression in metabolic tissues including intestine, liver, muscle, and adipose tissues. Metabolic disorders especially regarding blood lipids by FATP4 deficiency in different cell types are herein discussed. Our results may be applicable to not only patients with FATP4 mutations but also represent a model of dysregulated lipid homeostasis, thus providing mechanistic insights into obesity and development of fatty liver disease.
Identifiants
pubmed: 35583196
pii: 231317
doi: 10.1042/BSR20211854
pmc: PMC9160530
pii:
doi:
Substances chimiques
CD36 Antigens
0
Fatty Acid Transport Proteins
0
Fatty Acid-Binding Proteins
0
Fatty Acids
0
Lipids
0
Membrane Transport Proteins
0
Triglycerides
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2022 The Author(s).
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