PMID- 26635907
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20200929
IS  - 1871-5222 (Print)
IS  - 1875-6115 (Electronic)
IS  - 1871-5222 (Linking)
VI  - 9
IP  - 1
DP  - 2009 Sep
TI  - Targeting the fatty acid transport proteins (FATP) to understand the mechanisms 
      linking fatty acid transport to metabolism.
PG  - 11-17
AB  - One principal process driving fatty acid transport is vectorial acylation, where 
      fatty acids traverse the membrane concomitant with activation to CoA thioesters. 
      Current evidence is consistent with the proposal that specific fatty acid 
      transport (FATP) isoforms alone or in concert with specific long chain acyl CoA 
      synthetase (Acsl) isoforms function to drive this energy-dependent process. 
      Understanding the details of vectorial acylation is of particular importance as 
      disturbances in lipid metabolism many times leads to elevated levels of 
      circulating free fatty acids, which in turn increases fatty acid internalization 
      and ectopic accumulation of triglycerides. This is associated with changes in 
      fatty acid oxidation rates, accumulation of reactive oxygen species, the 
      synthesis of ceramide and ER stress. The correlation between chronically elevated 
      plasma free fatty acids and triglycerides with the development of obesity, 
      insulin resistance and cardiovascular disease has led to the hypothesis that 
      decreases in pancreatic insulin production, cardiac failure, arrhythmias, and 
      hypertrophy are due to aberrant accumulation of lipids in these tissues. To this 
      end, a detailed understanding of how fatty acids traverse the plasma membrane, 
      become activated and trafficked into downstream metabolic pools and the precise 
      roles provided by the different FATP and Acsl isoforms are especially important 
      questions. We review our current understanding of vectorial acylation and the 
      contributions by specific FATP and Acsl isoforms and the identification of small 
      molecule inhibitors from high throughput screens that inhibit this process and 
      thus provide new insights into the underlying mechanistic basis of this process.
FAU - Black, Paul N
AU  - Black PN
AD  - Department of Biochemistry, University of Nebraska, Lincoln, NE 68583, USA.
FAU - Sandoval, Angel
AU  - Sandoval A
AD  - Department of Biochemistry, University of Nebraska, Lincoln, NE 68583, USA.
FAU - Arias-Barrau, Elsa
AU  - Arias-Barrau E
AD  - Department of Biochemistry, University of Nebraska, Lincoln, NE 68583, USA.
FAU - DiRusso, Concetta C
AU  - DiRusso CC
AD  - Department of Nutrition and Health Sciences, University of Nebraska, Lincoln, NE 
      68583, USA ; Department of Biochemistry, University of Nebraska, Lincoln, NE 
      68583, USA.
LA  - eng
GR  - R01 DK071076/DK/NIDDK NIH HHS/United States
GR  - R01 GM056840/GM/NIGMS NIH HHS/United States
GR  - R01 GM056840-02/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PL  - United Arab Emirates
TA  - Immunol Endocr Metab Agents Med Chem
JT  - Immunology, endocrine & metabolic agents in medicinal chemistry
JID - 101269161
PMC - PMC4665979
MID - NIHMS223078
EDAT- 2009/09/01 00:00
MHDA- 2009/09/01 00:01
PMCR- 2015/12/01
CRDT- 2015/12/05 06:00
PHST- 2015/12/05 06:00 [entrez]
PHST- 2009/09/01 00:00 [pubmed]
PHST- 2009/09/01 00:01 [medline]
PHST- 2015/12/01 00:00 [pmc-release]
AID - 10.2174/187152209788009850 [doi]
PST - ppublish
SO  - Immunol Endocr Metab Agents Med Chem. 2009 Sep;9(1):11-17. doi: 
      10.2174/187152209788009850.