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Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies.

ABSTRACT: Hepatic lipase (gene: LIPC; enzyme: HL; E.C.3.1.1.3) is one of three members of the triglyceride lipase family that contributes to vascular lipoprotein degradation and serves a dual role in triglyceride hydrolysis and in facilitating receptor-mediated lipoprotein uptake into the liver. Amino acid sequences, protein structures, and gene locations for vertebrate LIPC (or Lipc for mouse and rat) genes and proteins were sourced from previous reports and vertebrate genome databases. Lipc was distinct from other neutral lipase genes (Lipg encoding endothelial lipase and Lpl encoding lipoprotein lipase [LPL]) and was located on mouse chromosome 9 with nine coding exons on the negative strand. Exon 9 of human LIPC and mouse and rat Lipc genes contained "stop codons" in different positions, causing changes in C-termini length. Vertebrate HL protein subunits shared 58%-97% sequence identities, including active, signal peptide, disulfide bond, and N-glycosylation sites, as well as proprotein convertase ("hinge") and heparin binding regions. Predicted secondary and tertiary structures revealed similarities with the three-dimensional structure reported for horse and human pancreatic lipases. Potential sites for regulating LIPC gene expression included CpG islands near the 5?-untranslated regions of the mouse and rat LIPC genes. Phylogenetic analyses examined the relationships and potential evolutionary origins of the vertebrate LIPC gene family with other neutral triglyceride lipase gene families (LIPG and LPL). We conclude that the triglyceride lipase ancestral gene for vertebrate neutral lipase genes (LIPC, LIPG, and LPL) predated the appearance of fish during vertebrate evolution.

SUBMITTER: Holmes RS

PROVIDER: S-EPMC3298411 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies.

Holmes Roger S RS Vandeberg John L JL Cox Laura A LA

Open access bioinformatics 20110401 3

Hepatic lipase (gene: LIPC; enzyme: HL; E.C.3.1.1.3) is one of three members of the triglyceride lipase family that contributes to vascular lipoprotein degradation and serves a dual role in triglyceride hydrolysis and in facilitating receptor-mediated lipoprotein uptake into the liver. Amino acid sequences, protein structures, and gene locations for vertebrate LIPC (or Lipc for mouse and rat) genes and proteins were sourced from previous reports and vertebrate genome databases. Lipc was distinct ...[more]

PMID: 22408368

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Project description:Endothelial lipase (gene: LIPG; enzyme: EL) is one of three members of the triglyceride lipase family that contributes to lipoprotein degradation within the circulation system and plays a major role in HDL metabolism in the body. In this study, in silico methods were used to predict the amino acid sequences, secondary and tertiary structures, and gene locations for LIPG genes and encoded proteins using data from several vertebrate genome projects. LIPG is located on human chromosome 18 and is distinct from other human 'neutral lipase' genes, hepatic lipase (gene: LIPC; enzyme: HL) and lipoprotein lipase (gene: LPL; enzyme: LPL) examined. Vertebrate LIPG genes usually contained 10 coding exons located on the positive strand for most primates, as well as for horse, bovine, opossum, platypus and frog genomes. The rat LIPG gene however contained only 9 coding exons apparently due to the presence of a 'stop' codon' within exon 9. Vertebrate EL protein subunits shared 58-97% sequence identity as compared with 38-45% sequence identities with human HL and LPL. Four previously reported human EL N-glycosylation sites were predominantly conserved among the 10 potential N-glycosylation sites observed for the vertebrate EL sequences examined. Sequence alignments and identities for key EL amino acid residues were observed as well as conservation of predicted secondary and tertiary structures with those previously reported for horse pancreatic lipase (PL) (Bourne et al. 1994). Several potential sites for regulating LIPG gene expression were observed including CpG islands near the LIPG gene promoter and a predicted microRNA binding site near the 3'-untranslated region. Promoter regions containing functional polymorphisms that regulate HDL cholesterol in baboons were conserved among primates but not retained between primates and rodents. Phylogenetic analyses examined the relationships and potential evolutionary origins of the vertebrate LIPG gene subfamily with other neutral triglyceride lipase gene families, LIPC and LPL. It is apparent that the triglyceride lipase ancestral gene for the vertebrate LIPG gene predated the appearance of fish during vertebrate evolution >500 million years ago.

Project description:Lipase H (LIPH) is a membrane-bound phospholipase generating 2-acyl lysophosphatidic acid (LPA) in the body. LPA is a lipid mediator required for maintaining homeostasis of diverse biological functions and in activating cell surface receptors such as P2Y5, which plays an essential role in hair growth. Bioinformatic methods were used to predict the amino acid sequences, secondary and tertiary structures, and gene locations for LIPH genes and encoded proteins using data from several vertebrate genome projects. Vertebrate LIPH genes contained ten coding exons transcribed on either the positive or negative DNA strands. Evidence is presented for duplicated LIPH genes for the chicken and zebra fish genomes. Vertebrate LIPH protein subunits shared 56–97 % sequence identities and exhibited sequence alignments and identities for key LIPH amino acid residues as well as extensive conservation of predicted secondary and tertiary structures with those previously reported for horse pancreatic lipase (LIPP), with ‘N-signal peptide’, ‘lipase,’ and ‘plat’ structural domains. Comparative studies of vertebrate LIPH sequences with other phospholipase A1-like lipases (LIPI and PS-PLA1), as well as vascular and pancreatic lipases, confirmed predictions for LIPH N-terminal signal peptides (residues 1–18); a conserved vertebrate LIPH N-glycosylation site (66NVT for human LIPH); active site ‘triad’ residues (Ser 154; Asp 178; His 248); disulfide bond residues (233–246; 270–281; 284–292; 427–446), and a ‘short’ 12 residue ‘active site lid’, which is comparable to other phospholipases examined. Phylogenetic analyses demonstrated the relationships and potential evolutionary origins of the vertebrate LIPH family of genes related to, but distinct from other phospholipase A1-like genes (LIPI and PS-PLA1), and from vascular lipase and pancreatic lipase gene families. Electronic supplementary material The online version of this article (doi:10.1007/s13205-012-0087-z) contains supplementary material, which is available to authorized users.

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Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies.

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Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies.

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