Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

Distinct roles of adipose triglyceride lipase and hormone-sensitive lipase in the catabolism of triacylglycerol estolides

K. Brejchova, FPW. Radner, L. Balas, V. Paluchova, T. Cajka, H. Chodounska, E. Kudova, M. Schratter, R. Schreiber, T. Durand, R. Zechner, O. Kuda

. 2021 ; 118 (2) : . [pub] 20210112

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc21019454
E-zdroje Online Plný text

NLK Free Medical Journals od 1915 do Před 6 měsíci
Freely Accessible Science Journals od 1915 do Před 6 měsíci
PubMed Central od 1915 do Před 6 měsíci
Europe PubMed Central od 1915 do Před 6 měsíci
Open Access Digital Library od 1915-01-01
Open Access Digital Library od 1915-01-15

Branched esters of palmitic acid and hydroxy stearic acid are antiinflammatory and antidiabetic lipokines that belong to a family of fatty acid (FA) esters of hydroxy fatty acids (HFAs) called FAHFAs. FAHFAs themselves belong to oligomeric FA esters, known as estolides. Glycerol-bound FAHFAs in triacylglycerols (TAGs), named TAG estolides, serve as metabolite reservoir of FAHFAs mobilized by lipases upon demand. Here, we characterized the involvement of two major metabolic lipases, adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL), in TAG estolide and FAHFA degradation. We synthesized a library of 20 TAG estolide isomers with FAHFAs varying in branching position, chain length, saturation grade, and position on the glycerol backbone and developed an in silico mass spectra library of all predicted catabolic intermediates. We found that ATGL alone or coactivated by comparative gene identification-58 efficiently liberated FAHFAs from TAG estolides with a preference for more compact substrates where the estolide branching point is located near the glycerol ester bond. ATGL was further involved in transesterification and remodeling reactions leading to the formation of TAG estolides with alternative acyl compositions. HSL represented a much more potent estolide bond hydrolase for both TAG estolides and free FAHFAs. FAHFA and TAG estolide accumulation in white adipose tissue of mice lacking HSL argued for a functional role of HSL in estolide catabolism in vivo. Our data show that ATGL and HSL participate in the metabolism of estolides and TAG estolides in distinct manners and are likely to affect the lipokine function of FAHFAs.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc21019454
003      
CZ-PrNML
005      
20210830101024.0
007      
ta
008      
210728s2021 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1073/pnas.2020999118 $2 doi
035    __
$a (PubMed)33372146
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Brejchova, Kristyna $u Institute of Physiology, Czech Academy of Sciences, 142 20 Prague 4, Czech Republic
245    10
$a Distinct roles of adipose triglyceride lipase and hormone-sensitive lipase in the catabolism of triacylglycerol estolides / $c K. Brejchova, FPW. Radner, L. Balas, V. Paluchova, T. Cajka, H. Chodounska, E. Kudova, M. Schratter, R. Schreiber, T. Durand, R. Zechner, O. Kuda
520    9_
$a Branched esters of palmitic acid and hydroxy stearic acid are antiinflammatory and antidiabetic lipokines that belong to a family of fatty acid (FA) esters of hydroxy fatty acids (HFAs) called FAHFAs. FAHFAs themselves belong to oligomeric FA esters, known as estolides. Glycerol-bound FAHFAs in triacylglycerols (TAGs), named TAG estolides, serve as metabolite reservoir of FAHFAs mobilized by lipases upon demand. Here, we characterized the involvement of two major metabolic lipases, adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL), in TAG estolide and FAHFA degradation. We synthesized a library of 20 TAG estolide isomers with FAHFAs varying in branching position, chain length, saturation grade, and position on the glycerol backbone and developed an in silico mass spectra library of all predicted catabolic intermediates. We found that ATGL alone or coactivated by comparative gene identification-58 efficiently liberated FAHFAs from TAG estolides with a preference for more compact substrates where the estolide branching point is located near the glycerol ester bond. ATGL was further involved in transesterification and remodeling reactions leading to the formation of TAG estolides with alternative acyl compositions. HSL represented a much more potent estolide bond hydrolase for both TAG estolides and free FAHFAs. FAHFA and TAG estolide accumulation in white adipose tissue of mice lacking HSL argued for a functional role of HSL in estolide catabolism in vivo. Our data show that ATGL and HSL participate in the metabolism of estolides and TAG estolides in distinct manners and are likely to affect the lipokine function of FAHFAs.
650    _2
$a tuková tkáň $x metabolismus $7 D000273
650    _2
$a bílá tuková tkáň $x metabolismus $7 D052436
650    _2
$a zvířata $7 D000818
650    _2
$a estery $x chemie $7 D004952
650    _2
$a mastné kyseliny $x metabolismus $7 D005227
650    _2
$a ženské pohlaví $7 D005260
650    _2
$a HEK293 buňky $7 D057809
650    _2
$a lidé $7 D006801
650    _2
$a lipasa $x metabolismus $7 D008049
650    _2
$a lipolýza $x fyziologie $7 D008066
650    _2
$a metabolismus $x fyziologie $7 D008660
650    _2
$a myši $7 D051379
650    _2
$a myši knockoutované $7 D018345
650    _2
$a kyselina palmitová $x metabolismus $7 D019308
650    _2
$a kyseliny stearové $x metabolismus $7 D013229
650    _2
$a sterolesterasa $x metabolismus $7 D002787
650    _2
$a triglyceridy $x metabolismus $7 D014280
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Radner, Franz Peter Walter $u Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria
700    1_
$a Balas, Laurence $u Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, École Nationale Supérieure de Chimie de Montpellier, Faculté de Pharmacie, Université de Montpellier, 34093 Montpellier, France
700    1_
$a Paluchova, Veronika $u Institute of Physiology, Czech Academy of Sciences, 142 20 Prague 4, Czech Republic
700    1_
$a Cajka, Tomas $u Institute of Physiology, Czech Academy of Sciences, 142 20 Prague 4, Czech Republic
700    1_
$a Chodounska, Hana $u Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 166 10 Prague 6, Czech Republic
700    1_
$a Kudova, Eva $u Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 166 10 Prague 6, Czech Republic
700    1_
$a Schratter, Margarita $u Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria
700    1_
$a Schreiber, Renate $u Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria
700    1_
$a Durand, Thierry $u Institut des Biomolécules Max Mousseron, UMR 5247, CNRS, École Nationale Supérieure de Chimie de Montpellier, Faculté de Pharmacie, Université de Montpellier, 34093 Montpellier, France
700    1_
$a Zechner, Rudolf $u Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria; rudolf.zechner@uni-graz.at ondrej.kuda@fgu.cas.cz $u BioTechMed-Graz, 8010 Graz, Austria
700    1_
$a Kuda, Ondrej $u Institute of Physiology, Czech Academy of Sciences, 142 20 Prague 4, Czech Republic; rudolf.zechner@uni-graz.at ondrej.kuda@fgu.cas.cz
773    0_
$w MED00010472 $t Proceedings of the National Academy of Sciences of the United States of America $x 1091-6490 $g Roč. 118, č. 2 (2021)
856    41
$u https://pubmed.ncbi.nlm.nih.gov/33372146 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y p $z 0
990    __
$a 20210728 $b ABA008
991    __
$a 20210830101024 $b ABA008
999    __
$a ok $b bmc $g 1690304 $s 1139900
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2021 $b 118 $c 2 $e 20210112 $i 1091-6490 $m Proceedings of the National Academy of Sciences of the United States of America $n Proc Natl Acad Sci U S A $x MED00010472
LZP    __
$a Pubmed-20210728

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...