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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-4-11
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pubmed:databankReference | |
pubmed:abstractText |
Apolipoprotein (apo) A-1 cDNA was amplified by the reverse-transcriptase-polymerase chain reaction (RT-PCR). Primers were synthesized according to the nucleotide sequence of chicken apo A-1, and the identity of apo A-1 cDNA was confirmed by comparing with the N-terminal amino acid sequence. The open reading frame of apo A-1 cDNA consists of 795 nucleotides, and it is capable of coding a polypeptide of 264 amino acids. A comparison between quail and chicken apo A-1 revealed 94.5% homology in the nucleotide sequence and 91.7% homology in the amino acid sequence. There was a similar 11- or 22-amino acid repeat in quail apo A-1 as was the case for chicken apo A-1. Apo A-1 mRNA was evaluated to be 1.4 k in length and was expressed in various tissues of Japanese quail: the liver, small intestine, lung, kidney, heart, and muscle. A quantitative evaluation, however, revealed that the liver and small intestine were the major organs for apo A-1 synthesis, accounting for more than 90% of the total expression of apo A-1 mRNA. Besides apo A-1 mRNA (1.4 k in length), a transcript of 4.1 k was detected in all the tissues examined, with a magnitude ranging from 5 to 10% of the apo A-1 mRNA level. The effect of cholesterol level on the expression of apo A-1 mRNA was studied to address the physiological significance of apo A-1 in the liver, small intestine, and muscle. The level of cholesterol in the liver and breast muscle was increased by feeding with cholesterol and reached a saturation level at day 7. There was also a temporal rise of cholesterol level at day 7 in the small intestine. Dietary cholesterol increased the expression of apo A-1 mRNA two fold in both the liver and small intestine. This was not the case for breast muscle, in which the expression of apo A-1 mRNA was not modulated by the cholesterol level.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0916-8451
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
286-90
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:9058967-Amino Acid Sequence,
pubmed-meshheading:9058967-Animals,
pubmed-meshheading:9058967-Apolipoprotein A-I,
pubmed-meshheading:9058967-Base Sequence,
pubmed-meshheading:9058967-Blotting, Northern,
pubmed-meshheading:9058967-Cholesterol, Dietary,
pubmed-meshheading:9058967-Coturnix,
pubmed-meshheading:9058967-DNA, Complementary,
pubmed-meshheading:9058967-Gene Expression Regulation,
pubmed-meshheading:9058967-Molecular Sequence Data,
pubmed-meshheading:9058967-RNA, Messenger
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pubmed:year |
1997
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pubmed:articleTitle |
Apolipoprotein A-1 of Japanese quail: cDNA sequence and modulation of tissue expression by cholesterol feeding.
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pubmed:affiliation |
Laboratory of Applied Biochemistry, Faculty of Agriculture, University of The Ryukyus, Okinawa, Japan.
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pubmed:publicationType |
Journal Article
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