PMID- 10318917
OWN - NLM
STAT- MEDLINE
DCOM- 19990617
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 10
DP  - 1999 May 11
TI  - Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein.
PG  - 5528-32
AB  - Hormone-sensitive lipase (HSL) is a cytosolic neutral lipase that functions as
      the rate-limiting enzyme for the mobilization of free fatty acids in adipose
      tissue. By using the yeast two-hybrid system to examine the potential interaction
      of HSL with other cellular proteins, evidence is provided to demonstrate a direct
      interaction of HSL with adipocyte lipid-binding protein (ALBP), a member of the
      family of intracellular lipid-binding proteins that binds fatty acids, retinoids,
      and other hydrophobic ligands. The interaction was demonstrated in vitro by the
      binding of ALBP to HSL translated in vitro, to HSL in extracts of HSL
      overexpressing Chinese hamster ovary (CHO) cells, and to HSL in extracts of rat
      adipose tissue. Finally, the presence of ALBP was documented in immune complexes 
      from rat adipose tissue immunoprecipitated with anti-HSL antibodies. The HSL-ALBP
      interaction was mapped to an N-terminal 300-aa region of HSL that is distinct
      from the C-terminal catalytic domain. These results suggest that HSL-derived
      fatty acids are bound by ALBP to facilitate intracellular trafficking of
      hydrophobic lipids.
FAU - Shen, W J
AU  - Shen WJ
AD  - Division of Endocrinology, Department of Medicine, Stanford University, Stanford,
      CA 94305-5103, USA.
FAU - Sridhar, K
AU  - Sridhar K
FAU - Bernlohr, D A
AU  - Bernlohr DA
FAU - Kraemer, F B
AU  - Kraemer FB
LA  - eng
SI  - GENBANK/AF144756
GR  - R01 DK046942/DK/NIDDK NIH HHS/United States
GR  - DK 49705/DK/NIDDK NIH HHS/United States
GR  - DK 46942/DK/NIDDK NIH HHS/United States
GR  - DK 07217/DK/NIDDK NIH HHS/United States
GR  - T32 DK007217/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Carrier Proteins)
RN  - 0 (FABP4 protein, rat)
RN  - 0 (Fabp7 protein, rat)
RN  - 0 (Fatty Acid-Binding Protein 7)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Fatty Acids)
RN  - 0 (Myelin P2 Protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.1.1.13 (Sterol Esterase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - CHO Cells
MH  - Carrier Proteins/*metabolism
MH  - Cricetinae
MH  - Fatty Acid-Binding Protein 7
MH  - Fatty Acid-Binding Proteins/*metabolism
MH  - Fatty Acids/metabolism
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Myelin P2 Protein/*metabolism
MH  - *Neoplasm Proteins
MH  - *Nerve Tissue Proteins
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - Rats
MH  - Recombinant Proteins/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Sterol Esterase/genetics/*metabolism
MH  - Yeasts
PMC - PMC21893
EDAT- 1999/05/13 00:00
MHDA- 1999/05/13 00:01
CRDT- 1999/05/13 00:00
PHST- 1999/05/13 00:00 [pubmed]
PHST- 1999/05/13 00:01 [medline]
PHST- 1999/05/13 00:00 [entrez]
AID - 10.1073/pnas.96.10.5528 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 May 11;96(10):5528-32. doi:
      10.1073/pnas.96.10.5528.