BIOMAT Database Logo BIOMAT Database Logo

The molecular biology of human apoA-I, apoA-II, apoC-II and apoB. 1986

S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer

The application of molecular biology techniques has enabled us to determine the gene sequence, organization, transcription and processing of apolipoprotein genes. Consequently, new insights have been gained in the biosynthesis and processing of these proteins. In addition to apoA-I, apoA-II and apoC-III reported here, other apolipoprotein genes such as apoC-II and apoE genes were found to share common intron-exon organizations. The results suggest that these genes most probably arise from a common ancestral gene. Utilizing cDNA as hybridization probes, we have localized apoA-I, apoA-II, apoC-II, apoC-III, apoE and apoB to specific locations of individual chromosomes (for review, see ref. 6). There is no clear relationship between currently known physiological function and the organization of the apolipoproteins in the chromosomes with the exception of the LDL receptor and its ligand, apoE which are localized to chromosome 19. However, apoB-100, the major ligand for the LDL receptor is on chromosome 2 and not in synteny with the apoE and the LDL receptor genes. The cloning of the major human apolipoprotein genes have also allowed us to initiate studies on the molecular defects leading to various dyslipoproteinemias including Tangier disease and abetalipoproteinemia. Undoubtedly, information derived from these studies will provide the basis for future in vitro and in vivo studies on patients with dyslipoproteinemia and premature atherosclerosis.

UI MeSH Term Description Entries
D008076 Cholesterol, HDL Cholesterol which is contained in or bound to high-density lipoproteins (HDL), including CHOLESTEROL ESTERS and free cholesterol. High Density Lipoprotein Cholesterol,Cholesterol, HDL2,Cholesterol, HDL3,HDL Cholesterol,HDL(2) Cholesterol,HDL(3) Cholesterol,HDL2 Cholesterol,HDL3 Cholesterol,alpha-Lipoprotein Cholesterol,Cholesterol, alpha-Lipoprotein,alpha Lipoprotein Cholesterol
D008967 Molecular Biology A discipline concerned with studying biological phenomena in terms of the chemical and physical interactions of molecules. Biochemical Genetics,Biology, Molecular,Genetics, Biochemical,Genetics, Molecular,Molecular Genetics,Biochemical Genetic,Genetic, Biochemical,Genetic, Molecular,Molecular Genetic
D009693 Nucleic Acid Hybridization Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503) Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D005786 Gene Expression Regulation Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation. Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001054 Apolipoproteins A Structural proteins of the alpha-lipoproteins (HIGH DENSITY LIPOPROTEINS), including APOLIPOPROTEIN A-I and APOLIPOPROTEIN A-II. They can modulate the activity of LECITHIN CHOLESTEROL ACYLTRANSFERASE. These apolipoproteins are low in atherosclerotic patients. They are either absent or present in extremely low plasma concentration in TANGIER DISEASE. Apo-A,ApoA
D001055 Apolipoproteins B Major structural proteins of triacylglycerol-rich LIPOPROTEINS. There are two forms, apolipoprotein B-100 and apolipoprotein B-48, both derived from a single gene. ApoB-100 expressed in the liver is found in low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). ApoB-48 expressed in the intestine is found in CHYLOMICRONS. They are important in the biosynthesis, transport, and metabolism of triacylglycerol-rich lipoproteins. Plasma Apo-B levels are high in atherosclerotic patients but non-detectable in ABETALIPOPROTEINEMIA. Apo-B,Apo B,ApoB,Apoprotein (B),Apoproteins B
D001056 Apolipoproteins C A group of apolipoproteins that can readily exchange among the various classes of lipoproteins (HDL; VLDL; CHYLOMICRONS). After lipolysis of TRIGLYCERIDES on VLDL and chylomicrons, Apo-C proteins are normally transferred to HDL. The subtypes can modulate remnant binding to receptors, LECITHIN CHOLESTEROL ACYLTRANSFERASE, or LIPOPROTEIN LIPASE. Apo-C,Apo C,ApoC,Apoprotein (C),Apoproteins C

Related Publications

S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
[Molecular biology research on ApoA-I].
January 1989, Sheng li ke xue jin zhan [Progress in physiology],
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
Differential tissue-specific expression of human apoA-I and apoA-II.
May 1991, Journal of lipid research,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
Plasma turnover of HDL apoC-I, apoC-III, and apoE in humans: in vivo evidence for a link between HDL apoC-III and apoA-I metabolism.
October 2003, Journal of lipid research,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
ApoA-I deficiency causes both hypertriglyceridemia and increased atherosclerosis in human apoB transgenic mice.
February 1998, Journal of lipid research,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
Secretion of apoB- and apoA-I-containing lipoproteins by chick kidney.
April 1998, Journal of lipid research,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
On the structural similarity of ApoA-I and ApoA-II of human high density lipoproteins.
January 1978, Biochemical and biophysical research communications,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
ApoA-I/A-II-HDL positively associates with apoB-lipoproteins as a potential atherogenic indicator.
November 2017, Lipids in health and disease,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
Synthesis of reconstituted high density lipoprotein (rHDL) containing apoA-I and apoC-III: the functional role of apoC-III in rHDL.
March 2009, Molecules and cells,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
Overexpression of SR-BI by adenoviral vector promotes clearance of apoA-I, but not apoB, in human apoB transgenic mice.
September 2002, Journal of lipid research,
S W Law, and K J Lackner, and S S Fojo, and A Hospattankar, and J C Monge, and H B Brewer
Identification of an apoC-II variant (apoC-IIBethesda) in a kindred with apoC-II deficiency and type I hyperlipoproteinemia.
March 1988, Journal of lipid research,
Copied contents to your clipboard!