Cai_1989_Biochemistry_28_8966

Reference

Title : Structure of the human hepatic triglyceride lipase gene - Cai_1989_Biochemistry_28_8966
Author(s) : Cai SJ , Wong DM , Chen SH , Chan L
Ref : Biochemistry , 28 :8966 , 1989
Abstract :

The structure of the human hepatic triglyceride lipase gene was determined from multiple cosmid clones. All the exons, exon-intron junctions, and 845 bp of the 5' and 254 bp of the 3' flanking DNA were sequenced. Comparison of the exon sequences to three previously published cDNA sequences revealed differences in the sequence of the codons for residues 133, 193, 202, and 234 that may represent sequence polymorphisms. By primer extension, hepatic lipase mRNA initiates at an adenine 77 bases upstream of the translation initiation site. The hepatic lipase gene spans over 60 kb containing 9 exons and 8 introns, the latter being all located within the region encoding the mature protein. The exons are all of average size (118-234 bp). Exon 1 encodes the signal peptide, exon 4, a region that binds to the lipoprotein substrate, and exon 5, an evolutionarily highly conserved region of potential catalytic function, and exons 6 and 9 encode sequences rich in basic amino acids thought to be important in anchoring the enzyme to the endothelial surface by interacting with acidic domains of the surface glycosaminoglycans. The human lipoprotein lipase gene has been recently reported to have an identical exon-intron organization containing the analogous structural domains [Deeb & Peng (1989) Biochemistry 28, 4131-4135]. Our observations strongly support the common evolutionary origin of these two lipolytic enzymes.

PubMedSearch : Cai_1989_Biochemistry_28_8966
PubMedID: 2605236
Gene_locus related to this paper: human-LIPC

Related information

Citations formats

Cai SJ, Wong DM, Chen SH, Chan L (1989)
Structure of the human hepatic triglyceride lipase gene
Biochemistry 28 :8966

Cai SJ, Wong DM, Chen SH, Chan L (1989)
Biochemistry 28 :8966