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

Law, Simon W.; Grant, Susan; Higuchi, Kayoko; Hospattankar, Ashok; Lackner, Karl J.; Lee, N; Brewer, H. Bryan

doi:10.1073/pnas.83.21.8142

Cited by 160 publications

(56 citation statements)

References 30 publications

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“…This sequence was obtained later than the other sequences and is probably most accurate. The sequence by Law et al 8 is least similar, while that by Chen et al 5 is most similar to the sequence by Ludwig et al 49 …”

mentioning

confidence: 65%

“…Acetonitrile, methanol, and other solvents for high-performance liquid chromatography (HPLC) were from Burdick and Jackson (Muskegon, Ml). Vydac C, 8 , Hypersil ODS, and Spherisorb ODS columns were from Cel Associates (Houston, TX). Reagents and solvents for the automatic gas phase sequencer were the products of Applied Biosystems (Foster City, CA).…”

Section: Methodsmentioning

confidence: 99%

“…Reference Chen et al 5 Knott et al°L aw et al 8 Cladaras et al 9 Ludwig et al 40 Carlson et al 53 Hardman et al 52 Protter et al M Chen et al …”

Section: Table 3 Number Of Nucleotlde Differences Per Nonsynonymous mentioning

confidence: 99%

“…However, in some cases, there is circumstantial evidence that suggests sequencing errors. At codon 766, Law et al 8 observed CGA, whereas all other authors observed CAG; at codon 1391, Cladaras et al 9 observed TCT, whereas all others observed TTC; at codon 2298, Hardman et al 50 observed TAT, whereas all others observed ATT; at codon 2906, Law et al 8 observed TCG, whereas all others observed TGC; at codon 3264, Carlson et al 51 observed CTG, whereas all others observed CGT; at codon 3404, Law et al 8 observed CCG, whereas all others observed GCC; and at codon 3797, Cladaras et al 9 observed CGA, whereas all others observed CAG. In each of these cases, the differences involve the rearrangement of two or three nucleotides, a situation that is unlikely to have arisen by point mutation.…”

Section: Variations Among Apoproteln B-100 Sequences From Different Lmentioning

confidence: 99%

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Structure of apolipoprotein B-100 of human low density lipoproteins.

et al. 1989

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We have analyzed low density lipoproteins (LDL) apolipoprotein (apo) B structure by direct sequence analysis of LDL apo B-100 tryptlc peptides. Native LDL were digested with trypsin, and the products were fractionated on a Sephadex G-50 column. The partially digested apo B-100 still associated with liplds was recovered In the void volume (designated trypsln-nonreleasable, TN, peptides). The released peptides (designated trypsln-releasable, TR, peptides) in subsequent peaks were repurifled on two successive high-performance liquid chromatogaphy (HPLC) columns. The TN peak was dellpidated and redigested with trypsin, and the resulting peptides were purified on two successive HPLC columns. Using this approach, we sequenced over 88% of LDL apo B-100, extending and refining our previous study (Nature 1986;323:738-742) which covered 52% of the protein. TN peptides made up 31%, and the TR peptides, 34% of the apo B-100 sequence; 23.7% were found under both TN and TR categories. Based on its differential trypsin releasabllity, apo B-100 can be divided into five domains: 1) residues 1-1000, largely TR; 2) residues 1001-1700, alternating TR and TN; 3) residues 1701-3070, largely TN; 4) residues 3071-4100, mainly TR and mixed; and 5) residues 4101-4536, almost exclusively TN. Domain 1 contained 14 of the 25 Cys residues In apo B. Domain 4 encompassed seven N-glycosylatIon sites, and contained the putative receptor binding domains. All 19 potential N-glycosylatlon sites were directly sequenced: 16 were found to be glycosylated and three were not Three pairs of dlsurfide bridges were also mapped. Finally, a combination of cDNA sequencing, direct mRNA sequencing, and comparison of published apo B-100 sequences allowed us to Identify specific amino acid residues within apo B-100 that seem to represent bona fide allellc variations. Our study provides information on LDL apo B-100 structure that will be important to our understanding of its conformation and metabolism. (Arteriosclerosis 9:96-108, January/February 1989) L ow density lipoproteins (LDL) are the major carriers of cholesterol in plasma, and their increased concentration in circulation is correlated with the development of atherosclerosis. 12 In normal individuals, very low density lipoproteins (VLDL) are the major precursor lipoproteins of plasma LDL. LDL are removed from the circulation by both high-affinity receptor-mediated 3 and receptor-independent 4 pathways, the liver being the major organ responsible for LDL clearance. Apoprotein (apo) B-100 is the major protein constituent in LDL and is the ligand recognized by the LDL receptor.The complete sequence of apo B-100 has been recently deduced from its cDNA sequence. 5 -8 It is one of the largest monomeric proteins known, with a calculated

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mentioning

confidence: 65%

Section: Methodsmentioning

confidence: 99%

“…Reference Chen et al 5 Knott et al°L aw et al 8 Cladaras et al 9 Ludwig et al 40 Carlson et al 53 Hardman et al 52 Protter et al M Chen et al …”

Section: Table 3 Number Of Nucleotlde Differences Per Nonsynonymous mentioning

confidence: 99%

Section: Variations Among Apoproteln B-100 Sequences From Different Lmentioning

confidence: 99%

See 2 more Smart Citations

Structure of apolipoprotein B-100 of human low density lipoproteins.

et al. 1989

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“…The MRT of VLDL-apoB-100 indicates the average time that the VLDL particle remains in the circulation after being secreted by the liver. A molecular mass of 512,723 g/mol for apoB-100 was used for unit conversions (33).…”

Section: Calculationsmentioning

confidence: 99%

Reproducibility of stable isotope-labeled tracer measures of VLDL-triglyceride and VLDL-apolipoprotein B-100 kinetics

Magkos

Patterson

Mittendorfer

2007

Journal of Lipid Research

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Apolipoprotein B-100 Hopkins (Arginine4019 [unk] Tryptophan)

Ladias

Kwiterovich²,

Smith

et al. 1989

JAMA

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A 43-year-old woman with severe coronary artery disease and hyperapobetalipoproteinemia was heterozygous for an abnormal Msp I apolipoprotein B (APOB) gene fragment because of the absence of the MspI site around codon 4046 in exon 29 of the APOB gene. Using the polymerase chain reaction technique, 134 base pairs containing the mutant Msp I site were amplified, cloned, and sequenced. The mutation was a C to T transition, substituting tryptophan for arginine at amino acid position 4019 of the mature ApoB-100 protein. Seven relatives of the proband had the same mutation, which has been called "ApoB-100 Hopkins." Only three of seven relatives with the mutation had hyperapobetalipoproteinemia; one was borderline while two other relatives without the mutation had hyperapobetalipoproteinemia. Mutant low-density lipoprotein (LDL) was bound and degraded to a greater extent than normal LDL in cultured human fibroblasts. In conclusion, a new mutation, ApoB-100 Hopkins, was not linked to the hyperapobetalipoproteinemia phenotype, which also was segregating in this family. The increased affinity of this mutant LDL for the LDL receptor may be due to a specific effect of ApoB-100 Hopkins or to altered LDL size and composition.

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

Cited by 160 publications

References 30 publications

Structure of apolipoprotein B-100 of human low density lipoproteins.

Structure of apolipoprotein B-100 of human low density lipoproteins.

Reproducibility of stable isotope-labeled tracer measures of VLDL-triglyceride and VLDL-apolipoprotein B-100 kinetics

Apolipoprotein B-100 Hopkins (Arginine4019 [unk] Tryptophan)

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