PMID- 10318835
OWN - NLM
STAT- MEDLINE
DCOM- 19990617
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 20
DP  - 1999 May 14
TI  - Cloning of a unique lipase from endothelial cells extends the lipase gene family.
PG  - 14170-5
AB  - A new lipoprotein lipase-like gene has been cloned from endothelial cells through
      a subtraction methodology aimed at characterizing genes that are expressed with
      in vitro differentiation of this cell type. The conceptual endothelial
      cell-derived lipase protein contains 500 amino acids, including an 18-amino acid 
      hydrophobic signal sequence, and is 44% identical to lipoprotein lipase and 41%
      identical to hepatic lipase. Comparison of primary sequence to that of
      lipoprotein and hepatic lipase reveals conservation of the serine, aspartic acid,
      and histidine catalytic residues as well as the 10 cysteine residues involved in 
      disulfide bond formation. Expression was identified in cultured human umbilical
      vein endothelial cells, human coronary artery endothelial cells, and murine
      endothelial-like yolk sac cells by Northern blot. In addition, Northern blot and 
      in situ hybridization analysis revealed expression of the endothelial-derived
      lipase in placenta, liver, lung, ovary, thyroid gland, and testis. A c-Myc-tagged
      protein secreted from transfected COS7 cells had phospholipase A1 activity but no
      triglyceride lipase activity. Its tissue-restricted pattern of expression and its
      ability to be expressed by endothelial cells, suggests that endothelial
      cell-derived lipase may have unique functions in lipoprotein metabolism and in
      vascular disease.
FAU - Hirata, K
AU  - Hirata K
AD  - Division of Cardiology, Stanford University Medical School, Stanford, California,
      94305, USA.
FAU - Dichek, H L
AU  - Dichek HL
FAU - Cioffi, J A
AU  - Cioffi JA
FAU - Choi, S Y
AU  - Choi SY
FAU - Leeper, N J
AU  - Leeper NJ
FAU - Quintana, L
AU  - Quintana L
FAU - Kronmal, G S
AU  - Kronmal GS
FAU - Cooper, A D
AU  - Cooper AD
FAU - Quertermous, T
AU  - Quertermous T
LA  - eng
SI  - GENBANK/AF118767
SI  - GENBANK/AF118768
GR  - KO8 HL 03865 01/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 3.1.1.3 (LIPG protein, human)
RN  - EC 3.1.1.3 (Lipase)
RN  - EC 3.1.1.3 (Lipg protein, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Blotting, Northern
MH  - COS Cells
MH  - Catalytic Domain
MH  - Cloning, Molecular
MH  - Endothelium, Vascular/*enzymology
MH  - Humans
MH  - In Situ Hybridization
MH  - Lipase/*genetics/metabolism
MH  - Liver/enzymology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Transfection
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 - 10.1074/jbc.274.20.14170 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 May 14;274(20):14170-5. doi: 10.1074/jbc.274.20.14170.