Cited by 353Cholesterol and Lipid MetabolismClusterin in disease pathologyProtein Structure and Dynamics

Apolipoprotein J: structure and tissue distribution

De Silva, Harshini V., Harmony, Judith A. K., Stuart, William D., Gil, Cleris M., Robbins, Jeffrey·1990·Biochemistry

Abstract

The primary structure of apolipoprotein J (apoJ) was deduced by the combined strategies of protein sequencing and cDNA cloning and sequencing. ApoJ, an apolipoprotein associated with discrete subclasses of high-density lipoproteins, is encoded by a single gene in both the human and mouse genomes. ApoJ is synthesized as a 427 amino acid polypeptide that is posttranslationally cleaved at an internal bond between Arg-205 and Ser-206. The subunits of apoJ are designated apoJ alpha, corresponding to residues 1-205, and apoJ beta, corresponding to resides 206-427. The subunits are associated through disulfide bonds. Analysis of the primary structure of apoJ predicts the existence of amphiphilic helices, which may account for the association of apoJ with lipoproteins, and heparin-binding motifs in both subunits. ApoJ appears to be the human analogue of a rat protein present in high concentrations in the testis, sulfated glycoprotein 2. ApoJ mRNA (1.9 kb) is expressed in all but one tissue examined. The mRNA is present in relatively high levels in brain, ovary, testis, and liver, is less abundant in heart, spleen, lung, and breast, and is absent in T-lymphocytes. ApoJ is unique among previously characterized human apolipoproteins in its structure and tissue distribution.

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Crossref · 10.1021/bi00474a025

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Authors
De Silva, H. V., Harmony, J. A. K., Stuart, W. D., Gil, C. M., & Robbins, J.
Venue
Biochemistry
Published
1990-06-05
Volume
29
Issue
22
Pages
5380-5389
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2071064041
Cited by
353
References
43
Citations by year
2026: 1 · 2025: 5 · 2024: 5 · 2023: 9 · 2022: 7 · 2021: 7 · 2020: 17 · 2019: 6 · 2018: 5 · 2017: 9 · 2016: 9 · 2015: 11 · 2014: 11 · 2013: 8 · 2012: 17
FWCI
26.40
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01hd013225-09, 5r01hl030999-08)
  • National Heart, Lung, and Blood Institute (P01HL041496, HL 30999, HL41496)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD13225)
Topics
  • Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
  • Health Sciences › Medicine › Oncology › Clusterin in disease pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
clusterin, apolipoprotein A-I, high-density lipoprotein, primary structure, post-translational cleavage, disulfide bonds, tissue distribution, mRNA expression, sulfated glycoprotein-2
MeSH terms
Amino Acid Sequence, Animals, Apolipoproteins, Base Sequence, Cell Line, Cloning, Molecular, Gene Expression Regulation, Glycoproteins, Heparin, Humans, Lipoproteins, HDL, Molecular Sequence Data, Organ Specificity, Poly A, Protein Conformation, Protein Processing, Post-Translational, RNA, Messenger, Sequence Homology, Nucleic Acid, Protein Biosynthesis, Genomic Library, Molecular Chaperones, Macromolecular Substances, Lipid Metabolism, Clusterin, Mice

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