PMID- 24113382
OWN - NLM
STAT- MEDLINE
DCOM- 20140214
LR  - 20211021
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 440
IP  - 4
DP  - 2013 Nov 1
TI  - Overexpression of human fatty acid transport protein 2/very long chain acyl-CoA 
      synthetase 1 (FATP2/Acsvl1) reveals distinct patterns of trafficking of exogenous 
      fatty acids.
PG  - 743-8
LID - S0006-291X(13)01642-2 [pii]
LID - 10.1016/j.bbrc.2013.09.137 [doi]
AB  - In mammals, the fatty acid transport proteins (FATP1 through FATP6) are members 
      of a highly conserved family of proteins, which function in fatty acid transport 
      proceeding through vectorial acylation and in the activation of very long chain 
      fatty acids, branched chain fatty acids and secondary bile acids. FATP1, 2 and 4, 
      for example directly function in fatty acid transport and very long chain fatty 
      acids activation while FATP5 does not function in fatty acid transport but 
      activates secondary bile acids. In the present work, we have used stable 
      isotopically labeled fatty acids differing in carbon length and saturation in 
      cells expressing FATP2 to gain further insights into how this protein functions 
      in fatty acid transport and intracellular fatty acid trafficking. Our previous 
      studies showed the expression of FATP2 modestly increased C16:0-CoA and C20:4-CoA 
      and significantly increased C18:3-CoA and C22:6-CoA after 4h. The increases in 
      C16:0-CoA and C18:3-CoA suggest FATP2 must necessarily partner with a long chain 
      acyl CoA synthetase (Acsl) to generate C16:0-CoA and C18:3-CoA through vectorial 
      acylation. The very long chain acyl CoA synthetase activity of FATP2 is 
      consistent in the generation of C20:4-CoA and C22:6-CoA coincident with transport 
      from their respective exogenous fatty acids. The trafficking of exogenous fatty 
      acids into phosphatidic acid (PA) and into the major classes of phospholipids 
      (phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylinositol 
      (PI), and phosphatidyserine (PS)) resulted in distinctive profiles, which changed 
      with the expression of FATP2. The trafficking of exogenous C16:0 and C22:6 into 
      PA was significant where there was 6.9- and 5.3-fold increased incorporation, 
      respectively, over the control; C18:3 and C20:4 also trended to increase in the 
      PA pool while there were no changes for C18:1 and C18:2. The trafficking of C18:3 
      into PC and PI trended higher and approached significance. In the case of C20:4, 
      expression of FATP2 resulted in increases in all four classes of phospholipid, 
      indicating little selectivity. In the case of C22:6, there were significant 
      increases of this exogenous fatty acids being trafficking into PC and PI. 
      Collectively, these data support the conclusion that FATP2 has a dual function in 
      the pathways linking the transport and activation of exogenous fatty acids. We 
      discuss the differential roles of FATP2 and its role in both fatty acid transport 
      and fatty acid activation in the context of lipid homeostasis.
CI  - Copyright (c) 2013 Elsevier Inc. All rights reserved.
FAU - Melton, Elaina M
AU  - Melton EM
AD  - Department of Biochemistry, University of Nebraska, Lincoln, NE, United States; 
      Center for Cardiovascular Sciences, Albany Medical College, Albany, NY, United 
      States.
FAU - Cerny, Ronald L
AU  - Cerny RL
FAU - DiRusso, Concetta C
AU  - DiRusso CC
FAU - Black, Paul N
AU  - Black PN
LA  - eng
GR  - R01-GM56850/GM/NIGMS NIH HHS/United States
GR  - F31 DK085961/DK/NIDDK NIH HHS/United States
GR  - R01-DK07076/DK/NIDDK NIH HHS/United States
GR  - 1F31-DK085961/DK/NIDDK NIH HHS/United States
GR  - R01 GM056840/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20131008
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Fatty Acids)
RN  - 0 (Phosphatidic Acids)
RN  - EC 6.2.1.- (Coenzyme A Ligases)
RN  - EC 6.2.1.3 (long-chain-fatty-acid-CoA ligase)
SB  - IM
MH  - Biological Transport
MH  - Coenzyme A Ligases/genetics/*physiology
MH  - Fatty Acids/*metabolism
MH  - HEK293 Cells
MH  - Humans
MH  - Lipid Metabolism
MH  - Phosphatidic Acids/metabolism
PMC - PMC4665974
MID - NIHMS531280
OTO - NOTNLM
OT  - FATP2
OT  - Fatty acid activation
OT  - Fatty acid trafficking
OT  - Fatty acid transport protein 2
OT  - Lipid synthesis
EDAT- 2013/10/12 06:00
MHDA- 2014/02/15 06:00
PMCR- 2015/12/01
CRDT- 2013/10/12 06:00
PHST- 2013/09/25 00:00 [received]
PHST- 2013/09/30 00:00 [accepted]
PHST- 2013/10/12 06:00 [entrez]
PHST- 2013/10/12 06:00 [pubmed]
PHST- 2014/02/15 06:00 [medline]
PHST- 2015/12/01 00:00 [pmc-release]
AID - S0006-291X(13)01642-2 [pii]
AID - 10.1016/j.bbrc.2013.09.137 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2013 Nov 1;440(4):743-8. doi: 
      10.1016/j.bbrc.2013.09.137. Epub 2013 Oct 8.