A partial cDNA clone for human apolipoprotein B.

Deeb, Samir S.; Motulsky, Arno G.; Albers, John J.

doi:10.1073/pnas.82.15.4983

Cited by 60 publications

(28 citation statements)

References 25 publications

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“…The results of our sequence studies established that the apoB-100 mRNA is 14.1 kb long encoding a plasma B-100 apolipoprotein of 4536 amino acid residues with an amino acid molecular weight of 512,723. The completed sequence of apoB-100 mRNA is in good agreement with the published partial sequences of apoB-100 (8)(9)(10)(11)(12)(13)(14)(15)(16), except for the 3'-untranslated region that is different from that reported by Knott et al (10) in many places. Computer analysis of the nucleic acid and derived amino acid sequence revealed several interesting features of apoB-100.…”

Section: Resultssupporting

confidence: 79%

“…The heterogeneity in apoB-100 molecular size has been attributed to the propensity of delipidated apoB-100 to aggregate and to the reported sensitivity of apoB-100 to protease cleavage (3,4,7). We (8,9) and others (10)(11)(12)(13)(14)(15)(16) have reported the partial sequence of human and rat (17) liver apoB-100 cDNA. We now report the complete nucleotide sequence of apoB-100 mRNA and its derived amino acid sequence.…”

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confidence: 99%

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Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence.

Law¹,

Grant²,

Higuchi³

et al. 1986

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

160

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Human apolipoprotein B-100 (apoB-100), the ligand on low density lipoproteins that interacts with the low density lipoprotein receptor and initiates receptor-mediated endocytosis and low density lipoprotein catabolism, has been cloned, and the complete nucleic acid and derived amino acid sequences have been determined. ApoB-100 cDNAs were isolated from normal human liver cDNA libraries utilizing immunoscreening as well as filter hybridization with radiolabeled apoB-100 oligodeoxynucleotides. The apoB-100 mRNA is 14.1 kilobases long encoding a mature apoB-100 protein of 4536 amino acids with a calculated amino acid molecular weight of 512,723. ApoB-100 contains 20 potential glycosylation sites, and 12 of a total of 25 cysteine residues are located in the amino-terminal region of the apolipoprotein providing a potential globular structure of the amino terminus of the protein. ApoB-100 contains relatively few regions of amphipathic helices, but compared to other human apolipoproteins it is enriched in beta-structure. The delineation of the entire human apoB-100 sequence will now permit a detailed analysis of the conformation of the protein, the low density lipoprotein receptor binding domain(s), and the structural relationship between apoB-100 and apoB-48 and will provide the basis for the study of genetic defects in apoB-100 in patients with dyslipoproteinemias.

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Section: Resultssupporting

confidence: 79%

mentioning

confidence: 99%

Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence.

Law¹,

Grant²,

Higuchi³

et al. 1986

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

160

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“…If this were the case, one would have to postulate that such a defect in the apo B-37 allele also blocked the formation of apo B-100, in that studies presented in the following article (18) indicate that apo B-37 is the sole product of one of the apo B alleles. Knowledge of the complementary DNA (cDNA) sequence and the deduced amino acid sequence of normal apo B-100 is now emerging from several laboratories (31,32,(36)(37)(38). Studies to determine the molecular basis of the abnormality in the allele encoding for apo B-37 are currently underway.…”

Section: Discussionmentioning

confidence: 99%

Characterization of an abnormal species of apolipoprotein B, apolipoprotein B-37, associated with familial hypobetalipoproteinemia.

Young¹,

Bertics²,

Curtiss³

et al. 1987

J. Clin. Invest.

114

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Steinberg and colleagues have previously described a unique kindred with normotriglyceridemic hypobetalipoproteinemia (1979. J. Clin. Invest. 64:292-301). In a reexamination of this kindred, we found an abnormal apolipoprotein (apo) B species, apo B-37 (203,000 mol wt), in the plasma lipoproteins of multiple members of the kindred. In affected individuals apo B-37 was found in very low density lipoproteins, along with the normal apo B species, apo B-100 and apo B-48. High density lipoproteins (HDL) also contained apo B-37, but no other apo B species. The first 13 amino-terminal amino acids of apo B-37 were identical to those of normal apo B-100. We utilized a panel of 18 different apo B-specific monoclonal antibodies and polyclonal antisera specific for apo B-37 and the thrombin cleavage products of apo B-100 to map apo B-37 in relation to apo B-100, apo B-48, and the thrombin cleavage products of apo B-100. The results of those immunochemical studies indicated that apo B-37 contains only amino-terminal domains of apo B-100.In affected individuals, the majority of apo B-37 in plasma was contained in the HDL density fraction. Within that fraction apo B-37 was found on discrete lipoprotein particles, termed Lp-B37, that had properties distinct from normal HDL particles containing apo A-I.This report documents for the first time the existence of an abnormal apo B species in humans. Further study of apo B-37 and lipoprotein particles containing apo B-37 should lead to an improved understanding of apo B structure and function.

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“…[16][17][18][19], FCRs for autologous and homologous LDLs were not different (0.213+0.028 vs. 0.195±0.041 pools/d, respectively). For the markedly obese woman (No.…”

Section: Methodsmentioning

confidence: 99%

In vivo evidence for reduced binding of low density lipoproteins to receptors as a cause of primary moderate hypercholesterolemia.

Vega¹,

Grundy²

1986

J. Clin. Invest.

193

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The causes of primary moderate hypercholesterolemia are not understood, but some patients have reduced fractional clearance rates (FCRs) for low density lipoproteins (LDL). This could be due to either decreased activity of LDL receptors or to a defect in structure (or composition) of LDL that reduces its affinity for receptors. To distinguish between these causes, simultaneous turnover rates of autologous and normal homologous LDL were determined in 15 patients with primary moderate hypercholesterolemia. In 10, turnover rates of both types of LDL were indistinguishable, which indicated that autologous LDL was cleared as efficiently as normal homologous LDL. In five others, FCRs for autologous LDL were significantly lower than for homologous LDL. Two of the latter five were treated with mevinolin, and although FCRs for both types of LDL rose during treatment, differences in FCRs between the two types of LDL persisted. In these five patients, autologous LDL appeared to be a poor ligand for LDL receptors.

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A partial cDNA clone for human apolipoprotein B.

Cited by 60 publications

References 25 publications

Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence.

Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence.

Characterization of an abnormal species of apolipoprotein B, apolipoprotein B-37, associated with familial hypobetalipoproteinemia.

In vivo evidence for reduced binding of low density lipoproteins to receptors as a cause of primary moderate hypercholesterolemia.

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