Lipase H, a new member of the triglyceride lipase family synthesized by the intestine.
We report here the molecular cloning of a novel member of the triglyceride lipase family, a 2.4-kb cDNA encoding human lipase H (LIPH) and the mouse ortholog (Liph). The human LIPH cDNA encodes a 451-amino-acid protein with a lipase domain. Mouse Liph shows 85% amino acid identity and 75% nucleotide identity to human LIPH. Human LIPH exhibits 47% identity with phosphatidylserine-specific phospholipase A1 (PS-PLA1) and 46% identity with endothelial lipase (LIPG) and lipoprotein lipase (LPL). LIPH is localized on human chromosome 3q27-q28. Northern blot analysis revealed specific expression of LIPH mRNA in intestine, lung, and pancreas. Lipase H protein was also detected in human intestine. Lipase H is a secreted protein with an apparent molecular weight of 63 kDa. Although several lipid substrates were tested, the lipid substrate of LIPG was not identified. Like the other members of this gene family, LIPH may be involved in lipid and energy metabolism.
Jin
Weijun
W
Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
Broedl
Uli C
UC
Monajemi
Houshang
H
Glick
Jane M
JM
Rader
Daniel J
DJ
D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D019143:Evolution, Molecular; D020224:Expressed Sequence Tags; D006801:Humans; D015850:Interleukin-6; D007413:Intestinal Mucosa / Q000378:metabolism*; D053605:Leukemia Inhibitory Factor; D051379:Mice; D018832:Molecular Chaperones / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D010802:Phylogeny; D011506:Proteins; D016415:Sequence Alignment
D015850:Interleukin-6; C507837:LIF protein, human; D053605:Leukemia Inhibitory Factor; C507838:Lif protein, mouse; D018832:Molecular Chaperones; D011506:Proteins