Comparative studies of vertebrate lipoprotein lipase: A key enzyme of very low density lipoprotein metabolism

Holmes, Roger S.; VandeBerg, John L.; Cox, Laura A.

doi:10.1016/j.cbd.2011.04.003

Cited by 17 publications

(18 citation statements)

References 109 publications

(132 reference statements)

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“…In addition, the phylogram suggested a sequence of gene duplication events for an ancestral PTLlike gene during vertebrate evolution (see Figure 7): (1) an ancestral PTL gene duplication generating the PTL/PLR1 and PLR2 precursor genes; (2) duplication of the vertebrate PTL/PLR1 precursor gene to form the PTL and PLR1 genes; and (3) duplication of the PLR2 gene prior to primate evolution to form the PLR2 and PLR3 genes, currently observed in primate genomes. It is also apparent that vertebrate neutral lipase genes (HL; EL; and LPL) have been generated during vertebrate evolution from a distinct ancestral gene, which is consistent with previous studies on the enzymes and genes [33][34][35][36][37].…”

Section: Phylogeny and Divergence Of Ptl-like Sequencessupporting

confidence: 87%

“…The bioinformatic methodologies used in this investigation of pancreatic lipase-like genes and proteins may be also readily applied to other pancreatic proteins as well as other gene families encoding enzymes and proteins, including neutral lipases [35][36][37], acid lipases [66], carboxylesterases [67], enolases [68] and other gene families [69][70][71].…”

Section: Discussionmentioning

confidence: 99%

“…Evolutionary studies of vertebrate PTL-like genes and proteins have been largely restricted to structural and genomic comparisons with other members of the neutral lipase gene superfamily, including lipoprotein lipases (LPL), hepatic lipases (HL), endothelial lipases (EL) and phospholipases A1 [5,10,[33][34][35][36][37]. This paper reports predicted gene structures and amino acid sequences for several vertebrate pancreatic lipase (PTL) and related protein (PLR1, PLR2 and PLR3) genes and enzymes not previously reported.…”

Section: Introductionmentioning

confidence: 99%

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Bioinformatics and Evolution of Vertebrate Pancreatic Lipase and Related Proteins and Genes

Holmes¹,

Cox²

2012

JDMGP

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Background: Pancreatic lipase (PTL) functions in the presence of colipase in the hydrolysis of emulsified fats in the small intestine following secretion from the pancreas. Pancreatic lipase related protein 1 (PLR1) is also found in pancreatic secretions and may perform a regulatory role in lipolysis; PLR2 catalyses pancreatic triglyceride and galactolipase reactions while PLR3 may serve a related but unknown lipase function. Comparative PTL, PLR1, PLR2 and PLR3 amino acid sequences and structures and gene locations and sequences were examined using data from several vertebrate genome projects. Methods:Sequence alignments and conserved predicted secondary and tertiary structures were studied and key amino acid residues and domains identified based on previous reports on human and pig PTL. Comparative analyses of vertebrate PTL-like genes were conducted using the UC Santa Cruz Genome Browser. Phylogeny studies investigated the evolution of these vertebrate PTL-like genes.Data: Human and mouse PTL sequences shared 78% identities but only 64-68% identities with human and mouse PLR1 and PLR2 sequences. Several vertebrate PTL and PTL-like protein domains were predicted using bioinformatics including an N-signal peptide; N-glycosylation site(s); an α/β hydrolase fold region containing a catalytic triad; a 'lid' region for the active site; a 'hinge' separating the lipase and PLAT regions; and a C-terminal PLAT region. Eutherian mammalian PLR1 sequences retained residues (196Val/198Ala) responsible for the loss of triacylglycerol lipase activity whereas lower vertebrate PLR1 sequences retained the 'active' lipase residues. In contrast, mammalian PTL, PLR2 and PLR3 sequences exhibited lipase 'active' residues (196Ala/198Pro); chicken and frog PLR1 sequences retained the lipase 'active' residues; and opossum and platypus PLR1 sequences exhibited 196Ala/Ser198 and 196Ser/198Pro residues. A phylogenetic tree analysis provided evidence for four distinct vertebrate PTL-like gene families. Conclusions:Pancreatic lipase (PTL) and related genes and proteins (PLR1 and PLR2) are present in all vertebrate genomes examined whereas PLR3 is found only in primate genomes. The 'inactive' form of vertebrate PLR1 is restricted to eutherian mammals. Vertebrate PTL-like genes apparently originated in a vertebrate ancestor following gene duplication events of an ancestral PTL-like ancestral gene. Two separate lines of PTL-like gene evolution are proposed in lower vertebrates (PTL/PLR1 and PLR2), with a further gene duplication event (PLR2/PLR3) for primate genomes.

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Section: Phylogeny and Divergence Of Ptl-like Sequencessupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Bioinformatics and Evolution of Vertebrate Pancreatic Lipase and Related Proteins and Genes

Holmes¹,

Cox²

2012

JDMGP

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“…As one of three members of the TG lipase family, LPL could contribute to the process of TG-rich CMs and VLDLs (Holmes et al, 2011), and in the removal of lipoproteins from the circulatory system (Murthy et al, 1996). In adult sheep, Pethick and Dunshea (1993) found that about 55-60% of the total amount of free fatty acids originate from hydrolysis of circulating triacylglycerols by LPL.…”

Section: Discussionmentioning

confidence: 99%

“…The bovine LPL gene maps to chromosome 8 and its coding region consists of 10 exons, which are highly expressed in skeletal muscle and adipose tissue (Holmes et al, 2011). Wang et al (2012) identified two polymorphisms (T355420C and A355427T) of the LPL gene that were associated with growth traits in Xiangxi cattle.…”

Section: Introductionmentioning

confidence: 99%

Polymorphisms in the LPL gene and their association with growth traits in Jiaxian cattle

et al. 2016

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ABSTRACT. Previous studies showed that the lipoprotein lipase (LPL) gene was involved in metabolism and transport of lipids, suggesting that the LPL is a potential candidate gene affecting growth traits in animals. The aim of this study was to identify polymorphism in the bovine LPL gene and analyze its possible association with growth traits in 218 randomly selected Jiaxian cattle. We used DNA sequencing to identify single nucleotide polymorphisms (SNPs) in the LPL gene. A sequence analysis revealed three SNPs: two in intron 5 (C18306T and C18341T) and one in exon 6 (G18362A). G18362A is a missense mutation leading to a change of the 325th glycine to serine. Based on c 2 tests, the genotypic distributions of C18306T were in agreement with the Hardy-Weinberg equilibrium (P > 0.05), whereas the other two mutations were not (0.05 > P > 0.01). Association analyses showed that the C18341T SNP was significantly associated with several growth traits (P < 0.01 or P < 0.05), and the G18362A was associated with withers height (P < 0.05). Our results suggest that LPL gene variation may be considered molecular markers for growth traits in Jiaxian cattle.

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Comparative structures and evolution of vertebrate lipase H (LIPH) genes and proteins: a relative of the phospholipase A1 gene families

Holmes

Cox

2012

3 Biotech

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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 materialThe 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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Comparative studies of vertebrate lipoprotein lipase: A key enzyme of very low density lipoprotein metabolism

Cited by 17 publications

References 109 publications

Bioinformatics and Evolution of Vertebrate Pancreatic Lipase and Related Proteins and Genes

Bioinformatics and Evolution of Vertebrate Pancreatic Lipase and Related Proteins and Genes

Polymorphisms in the LPL gene and their association with growth traits in Jiaxian cattle

Comparative structures and evolution of vertebrate lipase H (LIPH) genes and proteins: a relative of the phospholipase A1 gene families

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