ArticleProceedings of the National Academy of Sciences of the United States of America1989
Expression of apolipoprotein B mRNAs encoding higher- and lower-molecular weight isoproteins in rat liver and intestine.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 61 citations in OpenAlex.
- RNA-DNA sequence differences in Saccharomyces cerevisiae.Genome research · 2016Article
- Apolipoprotein B48, the Structural Component of Chylomicrons, Is Sufficient to Antagonize Staphylococcus aureus Quorum-Sensing.PloS one · 2015Article
- Flow-cytometric visualization of C>U mRNA editing reveals the dynamics of the process in live cells.RNA biology · 2015Article
- Intracellular trafficking and secretion of VLDL.Arteriosclerosis, thrombosis, and vascular biology · 2012Review
- Recent progress in understanding protein and lipid factors affecting hepatic VLDL assembly and secretion.Nutrition & metabolism · 2010Article
- Lipoproteins, cholesterol homeostasis and cardiac health.International journal of biological sciences · 2009Review
- Insulin promotes the biosynthesis and secretion of apolipoprotein B-48 by altering apolipoprotein B mRNA editing.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Lipid and apolipoprotein B48 transport in mesenteric lymph and the effect of hyperphagia on the clearance of chylomicron-like emulsions in insulin-deficient rats.Diabetologia · 1994Article
- Transgenic mice expressing high plasma concentrations of human apolipoprotein B100 and lipoprotein(a).The Journal of clinical investigation · 1993Article
- Differential expression of mutant and normal beta T3 receptor alleles in kindreds with generalized resistance to thyroid hormone.The Journal of clinical investigation · 1993Article
- Plasma lipoprotein metabolism in transgenic mice overexpressing apolipoprotein E. Accelerated clearance of lipoproteins containing apolipoprotein B.The Journal of clinical investigation · 1992Article
- In vitro apolipoprotein B mRNA editing: identification of a 27S editing complex.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- A base mutation of the C-erbA beta thyroid hormone receptor in a kindred with generalized thyroid hormone resistance. Molecular heterogeneity in two other kindreds.The Journal of clinical investigation · 1990Article
- Article
- Review
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two B apolipoproteins (apo) are present in human plasma, designated apoB-100 and apoB-48, and represent translational products from mature apoB mRNAs that differ by a single base. Either the glutamine codon encoded by the single-copy apoB gene at nucleotide 6666 is transcribed and translated to produce apoB-100 or an RNA-editing mechanism substitutes a uracil for cytosine, altering this glutamine codon (CAA) to a stop codon (UAA), prematurely terminating translation to produce apoB-48. In the present report, editing of rat apoB transcripts was evaluated by amplification of RNA with the polymerase chain reaction by use of primers based on the apoB cDNA cloned from a rat liver cDNA library. The combined results of this study show that (i) a single copy of the apoB gene exists in the rat; (ii) the rat apoB gene encodes only the glutamine codon for the synthesis of apoB of higher molecular weight (apoBH); (iii) rat apoB transcripts undergo RNA editing; (iv) apoBH and apoB of lower molecular weight (apoBL) in the rat represent structural equivalents of apoB-100 and apoB-48 in humans, respectively; (v) RNA editing occurs in both the liver and intestine of the rat; (vi) rat hepatic apoB RNA is more extensively edited than is human hepatic apoB RNA, which is consistent with the marked increase in apoBL secretion by the rat liver when compared with human; and (vii) the definitive identification of apoBH mRNA as well as apoBL mRNA in the rat intestine provides a mechanism for the biosynthesis of both apoBH and apoBL by the rat intestine.
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