A Description of U—n G—

Fielding, Henry; Miller, Henry Knight

doi:10.1093/oseo/instance.00058123

Cited by 10 publications

(11 citation statements)

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“…In any given plasma, HDLA are better substrates than HDLE. This could be related to the lower cholesterol-to-phospholipid ratio and to the higher apoA-I concentration found in HDLA compared to HDLE, because these two factors have been shown to be important determinants for the reactivity of LCATase substrates (35,36). However both HDLA and HDLE from LCATasedeficient patients are better substrates than the corresponding lipoproteins from normal plasma.…”

Section: Resultsmentioning

confidence: 99%

Heterogeneity of human high density lipoprotein: Presence of lipoproteins with and without apoE and their roles as substrates for lecithin:cholesterol acyltransferase reaction

Marcel

Vézina

Emond

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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By affinity chromatography on heparinSepharose, two classes of lipoproteins were separated from high density li'proteins (HDL) isolated from patients with primary or seconda lecithin:cholesterol acyltransferase (LCATase; EC 2.3.1.43) deficiency and from normal subjects. The unretained fraction, HDLA, was characterized by having apoA-I as a major apoprotein; it also contained apoA-II, -GCII, and -CIII but it contained only traces of immunodetectable apoE and no apoB. The retained fraction, HDLE, had apoE as the major apoprotein; it also contained apoA-I, -A-II, -B, -GII, and -ICI. The relative concentration of apoA-I increased with increasing density in the HDLE subclass. Compared to HDLA, HDLE had a significantly higher cholesterol content and a lower protein concentration. HDLE was mainly (90%) contained within the EIDL1 subfraction. Contamination of HDLE by low density lipoproteins (LDL) or Lp(a) was minimal on the basis of pre-p-electrophoretic mobility and absence of albumin, respectively. Contamination by LDL or Lp(a) could be resolved in part by application of HDLE to concanavalin A-Sepharose or to heparinSepharose with a shallow gradient. When evaluated as substrates for a highly purified LCATase preparation, the initial reaction rates and Vm. obtained with HDLA were always higher than those obtained with HDLE in any given plasma. However, both HDL subclasses from LCATase-deficient subjects were better substrates than the corresponding HDL subclasses from normal plasma. Also, both HDL3A and HDL3E isolated from normal HDL3 were better substrates than the corresponding subclasses isolated from normal HDL2. The recognition of this compositional and functional heterogeneity within HDL will allow a better understanding of the metabolism of this lipoprotein class.

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Section: Resultsmentioning

confidence: 99%

Heterogeneity of human high density lipoprotein: Presence of lipoproteins with and without apoE and their roles as substrates for lecithin:cholesterol acyltransferase reaction

Marcel

Vézina

Emond

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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“…Identical amino acids in apo A-I sequences are enclosed in boxes 30 ( (2) resembles the classical 'TATA' box, was found 22 nucleotides upstream from the start of pRBA-502. (2) 90 ( 1 ) Q…”

Section: N a Sequence Analysis Of Prba-502 And Deduced Amino Acid Smentioning

confidence: 99%

Rabbit apolipoprotein A‐I mRNA and gene

Pan

Hao

Yamin

et al. 1987

European Journal of Biochemistry

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In order to study the tissue‐specific expression of rabbit apolipoprotein (apo) A‐I, a 923‐base‐pair clone, pRBA‐502, complementary to rabbit apo A‐I mRNA was identified from a rabbit intestinal cDNA library by hybrid‐select translation and immunoprecipitation methods. Northern blot and dot‐blot hybridization, utilizing 32P‐labeled pRBA‐502, revealed that the rabbit apo A‐I gene is expressed in the intestine, not in the liver and that rabbit apo A‐I mRNA is about 950 nucleotides in length. The entire nucleotide sequence of pRBA‐502 has been determined and the complete amino acid sequence of the corresponding apo A‐I has been deduced. The mRNA codes for a protein comprising 265 amino acids. Amino acids 1–18 and 19–24 of the primary translation product represent the presegment and prosegment, respectively, of apo A‐I. Matured rabbit apo A‐I contains 241 amino acids and has a molecular mass of 27612 Da. Using pRBA‐502 as a probe, a 15.5‐kb genomic fragment, which contains the entire apo A‐I gene, was isolated from a rabbit liver genomic library. Sequence analysis of the gene shows that the 200 base pairs of the 5′ upstream flanking region of the rabbit and human apo A‐I genes showed 78% sequence homology. Like the human apo A‐I gene, the rabbit apo A‐I gene is interrupted by three intervening sequences. Except for two nucleotides in the fourth exon, the coding sequence of the rabbit liver apo A‐I gene is identical to that of pRBA‐502. Our data showed that the lack of expression of apo A‐I gene in rabbit liver is not due to the alternation of rabbit liver apo A‐I gene sequence and suggest that the expression of apo A‐I gene in rabbit liver is regulated by a trans‐acting regulating element(s).

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“…Apolipoprotein A-I (apoA-]) is the major apolipoprotein of plasma high-density lipoproteins (HDL) and a cofactor of lecithin cholesterol acyltransferase which esterifies cholesterol to form cholesteryl esters (1,2). In most mammalian systems apoA-I is synthesized in both liver and intestine and plays an important role in lipoprotein metabolism (3)(4)(5).…”

Section: Introductionmentioning

confidence: 99%

Repetitive elements in the third intron of murine apolipoprotein A‐I gene

Chiang¹,

Fan²,

Shaw³

et al. 1997

IUBMB Life

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Genomic DNAs containing the gene encoding apolipoprotein A-I (apoA-1) from four strains of mice and three strains of rats have been sequenced. Some peculiar repetitive sequences were found in the third intron of apoA-1 of the murine species. The striking features include regular tandem repeats of C(A)4 and C(A)6 in mice and long A-tracts in rats. Not completely identical but very similar motifs were found in mice or rats belonging to the same species while repetitive elements from different species show some variation from their speciesspecific consensus sequences. These repetitive motifs are very similar to the sequences flanking human Alu and rodent B 1 repetitive elements, although no evidence for the existence of Alu or B 1 was found near the peculiar repetitive DNA sequences in apoA-1 gene. BIOCHEMISTRY and MOLECULAR BIOLOGY INTERNATIONALMice and rats are useful experimental models for studying the genetic factors that may be

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A Description of U—n G—

Cited by 10 publications

References 0 publications

Heterogeneity of human high density lipoprotein: Presence of lipoproteins with and without apoE and their roles as substrates for lecithin:cholesterol acyltransferase reaction

Heterogeneity of human high density lipoprotein: Presence of lipoproteins with and without apoE and their roles as substrates for lecithin:cholesterol acyltransferase reaction

Rabbit apolipoprotein A‐I mRNA and gene

Repetitive elements in the third intron of murine apolipoprotein A‐I gene

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