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The lecithin cholesterol acyltransferase gene (LCAT) plays an important role in lipoprotein metabolism, especially in the process termed 'reverse cholesterol transport'. In this study, we obtained the 1,434 bp mRNA sequence of porcine LCAT including the full coding region and encoding a protein of 472 amino acids. The sequence was deposited into the GenBank under the accession no. EU717835. The genomic sequence of this gene which contains six exons and five introns, is 3,712 bp in length (GQ379050). Bioinformatic analysis of the 5' regulatory region has revealed that some transcription factor Sp1, AP-1, AP-2 and NF-kappaB were represented in this region. Tissue expression analysis showed that the porcine LCAT gene is ubiquitously expressed in all examined tissues. Phylogenetic tree was constructed by aligning the amino acid sequences of different species. Moreover, we found a single nucleotide polymorphism (SNP, C/G266) in intron 1 of the LCAT gene and association analysis showed that it was significantly associated with ratio of lean to fat (P < 0.05), caul fat weight (P < 0.01), leaf fat weight (P < 0.05), carcass length (P < 0.05) and bone percentage (P < 0.05). Our study will lay the groundwork for the further investigations on the detailed physiological function of LCAT in pig models.
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http://dx.doi.org/10.1007/s11033-009-9709-x | DOI Listing |
Oxid Med Cell Longev
March 2022
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Agro-Product Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, China.
The liver is the center for uptake, synthesis, packaging, and secretion of lipids and lipoproteins. The research on lipid metabolism in pigs is limited. The objective of the present study is to identify the genes related to lipid metabolism and oxidative stress in pigs by using transcriptomic analysis.
View Article and Find Full Text PDFProtein Expr Purif
November 2021
Department of Biochemistry and Structural Biology, Lund University, P O Box 124, SE22100, Lund, Sweden. Electronic address:
Apolipoprotein A-I (ApoA-I) is the major protein constituent of high-density lipoprotein particles, and as such is involved in cholesterol transport and activation of LCAT (the lecithin:cholesterol acyltransferase). It may also form amyloidal deposits in the body, showing the multifaceted interactions of ApoA-I. In order to facilitate the study of ApoA-I in various systems, we have developed a protocol based on recombinant expression in E.
View Article and Find Full Text PDFMol Biol Rep
June 2010
Key Laboratory of Pig Genetics and Breeding of Ministry of Agriculture & Key Laboratory of Agricultural Animal Genetics, Breeding and Reproduction of Ministry of Education, Huazhong Agricultural University, 430070, Wuhan, People's Republic of China.
The lecithin cholesterol acyltransferase gene (LCAT) plays an important role in lipoprotein metabolism, especially in the process termed 'reverse cholesterol transport'. In this study, we obtained the 1,434 bp mRNA sequence of porcine LCAT including the full coding region and encoding a protein of 472 amino acids. The sequence was deposited into the GenBank under the accession no.
View Article and Find Full Text PDFJ Mol Med (Berl)
August 1999
Institut für Arterioskleroseforschung an der Universität Münster, Germany.
ApoA-I(R151)Paris is a natural apolipoprotein (apo) A-I variant that is associated with low levels of high-density lipoprotein cholesterol (HDL-cholesterol) and the partial deficiency of lecithin:cholesterol acyl-transferase (LCAT) in the plasma of heterozygous carriers. We compared the abilities of recombinant normal apoA-I and recombinant apoA-I(R151C)Paris to clear an emulsion of dimyristoylphosphatidylcholine (DMPC), to form reconstituted lipoproteins with dipalmitoylphosphatidylcholine (DPPC), to activate LCAT, and to promote efflux of biosynthetic cholesterol from porcine aortic smooth muscle cells (SMCs) or of exogenous cholesterol from lipid-loaded mouse peritoneal macrophages. Recombinant apoA-I(R151C)Paris occurred in monomeric and dimeric forms at a ratio of 60:40.
View Article and Find Full Text PDFJ Lipid Res
March 1999
Institut für Arterioskleroseforschung an der Universität Münster, Domagkstrasse 3, D-48149 Münster, Germany.
ApoA-I(R160L)Oslo and apoA-I(P165R) are naturally occurring apolipoprotein (apo) A-I variants that are associated with low HDL-cholesterol in heterozygous carriers. We characterized the capacity of these variants to bind lipid, to activate lecithin:cholesterol acyltransferase (LCAT), and to promote efflux of biosynthetic cholesterol from porcine aortic smooth muscle cells (SMCs) or exogenous cholesterol from lipid-loaded mouse peritoneal macrophages. During cholate dialysis, normal apoA-I and both variants associated completely with dipalmitoylphosphatidylcholine (DPPC) and formed rLpA-I of identical size.
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