Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
Comparison of the cDNA and amino acid sequences of lipoprotein lipase in eight species☆
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Cited by (33)
Characterization of two lipid metabolism-associated genes and their expression profiles under different feeding conditions in Acipenser dabryanus
2021, Aquaculture ReportsCitation Excerpt :The catalytic triad containing Ser-Asp-His, present in A. dabryanus, is essential for triacylglycerol hydrolysis. Ser is essential for catalytic activity and is linked by hydrogen bonds to the other two members of the catalytic triad, Asp and His (Raisonnier et al., 1995), and this active site is conserved in vertebrates. Other motifs, such as potential N-glycosylation sites NXS/T (X can be any amino acid except P), the lipid binding site that plays a vital function in the binding of LPL to lipoproteins and the heparin-binding region that plays an essential role in LPL catalytic function (Hata et al., 1993), are all conserved in A. dabryanus LPL.
Lipoprotein lipase: Biosynthesis, regulatory factors, and its role in atherosclerosis and other diseases
2018, Clinica Chimica ActaMolecular cloning and expression analysis on LPL of Coilia nasus
2016, GeneCitation Excerpt :LPL of C. nasus has PLAT domain from 353 to 477 amino acids; its main function is to mediate interaction with lipids or membrane bound proteins. LPL was N-linked glycoprotein; C. nasus LPL had four glycosylation sites (Asn–X–Ser/Thr) and six cysteines sites to make function in heparin binding process (Raisonnier A et al., 1995; Sendak R et al., 1998). At C-terminus, there was conserved heparin-binding site to make function in heparin releasing into blood.
Molecular characterization of lipoprotein lipase from blunt snout bream Megalobrama amblycephala and the regulation of its activity and expression by dietary lipid levels
2013, AquacultureCitation Excerpt :In human, tryptophan clusters at Trp417, Trp420 and Trp421 play an important role in binding to lipid substrates and lipoprotein. The Lys434 is a site for interaction with low-density lipoprotein receptor-related protein (Raisonier et al., 1995). All of these residues are conserved in all species including M. amblycephala (Trp432, Trp434 and Trp435, Lys448).
Differences in lipid distribution and expression of peroxisome proliferator-activated receptor gamma and lipoprotein lipase genes in torafugu and red seabream
2013, General and Comparative EndocrinologyCitation Excerpt :Similar analysis using the predicted amino acid sequences of the genes on scaffolds 50 and 14 revealed a monophyletic relationship with the endothelial lipase (EL) and hepatic lipase (HL) clades, respectively. The deduced amino acid sequence of the torafugu LPLs contained putative signal peptides, N-glycosylation sites, and several other functional features assigned by comparison to the human LPL (Raisonnier et al., 1995), including sites corresponding to cofactor activation, catalytic triads, heparin binding sites, lipid binding sites, and conserved cysteine residues involved in the formation of disulfide bridges (Fig. 4). Interestingly, the LPL2s from torafugu and red seabream had more amino acid substitutions in their cofactor activation sites and heparin binding sites than LPL1s.
Comparative studies of vertebrate lipoprotein lipase: A key enzyme of very low density lipoprotein metabolism
2011, Comparative Biochemistry and Physiology - Part D: Genomics and ProteomicsCitation Excerpt :Tree topology was reexamined by the boot-strap method (100 bootstraps were applied) of resampling and only values that were highly significant (≥ 90) are shown (Felsenstein, 1985). The deduced amino acid sequences for opossum (M. domestica), frog (X. tropicalis) and stickleback (G. aculeatus) LPL are shown in Fig. 1 together with previously reported sequences for human (Wion et al., 1987; Dichek et al., 1991), mouse (Zechner et al., 1991), chicken LPL (Cooper et al., 1992; Raisonnier et al., 1995), horse pancreatic lipase (LIPP) (Bourne et al., 1994), human pancreatic lipase related protein 1 (LPR1) and human pancreatic lipase related protein 2 (LPR2) (Giller et al., 1992) (Table 1 and Supplementary Table). Alignments of human and other vertebrate LPL sequences examined showed between 58 and 99% identities, suggesting that these are products of the same family of genes, whereas comparisons of sequence identities of vertebrate LPL proteins with human and mouse HL and EL, horse LIPP, human PLR1 and PLR2 exhibited lower levels of sequence identities: HL (41% and 44% respectively); EL (44% and 45% respectively); LIPP (24%); PLR1 (26%); and PLR2 (24%) indicating that these are members of distinct lipase families (Table 2).
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These results were presented in part at the 62nd congress of the European Atherosclerosis Society, Jerusalem, Israel, 5–9 September 1993 (Etienne et al., 1993).