Cited by 170Angiogenesis and VEGF in CancerLiver physiology and pathologyDevelopmental Biology and Gene Regulation

Identification of a mammalian angiopoietin-related protein expressed specifically in liver

Conklin, Darrell, Gilbertson, Debra, Taft, David W., Maurer, Mark F., Whitmore, Theodore E., Smith, Deborah L., Walker, Kathleen M., Chen, Lennie H. +3 more·1999·Genomics

Abstract

Based on searches of EST databases for signal sequences and amphipathic helices, we have identified and cloned an angiopoietin-like gene, ANGPTL3. Multiple tissue Northern blots show that ANGPTL3 is expressed principally in the liver. ANGPTL3 is expressed early during liver development, and expression is maintained in adult liver. Human ANGPTL3 is a 460-amino-acid polypeptide with the characteristic structure of angiopoietins: a signal peptide, an extended helical domain predicted to form dimeric or trimeric coiled-coils, a short linker peptide, and a globular fibrinogen homology domain (FHD). Murine ANGPTL3 is a 455-acid polypeptide encoded by seven exons on mouse chromosome 4, spanning about 11 kb of DNA. ANGPTL3 contains the four conserved cysteines implicated in the intramolecular disulfide bonds within the FHD, but it does not contain two other cysteines that are found within the FHD of angiopoietins 1, 2, and 4. ANGPTL3 also does not contain the characteristic calcium binding motif found in the other angiopoietins. By radiation hybrid mapping and the use of surrounding genes, human ANGPTL3 maps to the 1p31 region.

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Registry

Crossref · 10.1006/geno.1999.6041

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  • ANGPTL3 is exclusively expressed and secreted by the liver and is an important regulator of plasma triglyceride levels due to its inhibition of LPL in oxidative tissues.

    “ANGPTL3 is exclusively expressed and secreted by the liver and has emerged as an important regulator of plasma triglyceride levels due to its inhibition of LPL in oxidative tissues [34] (Figure 3).”

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Authors
Conklin, D., Gilbertson, D., Taft, D. W., Maurer, M. F., Whitmore, T. E., Smith, D. L., Walker, K. M., Chen, L. H., Wattler, S., Nehls, M., & Lewis, K. B.
Corresponding author
Conklin, Darrell
Venue
Genomics
Publisher
Elsevier BV
Published
1999-12
Volume
62
Issue
3
Pages
477-482
ISSN
0888-7543 (ISSN-L)
OpenAlex
W2033200911
Cited by
169
References
24
Citations by year
2026: 8 · 2025: 11 · 2024: 11 · 2023: 13 · 2022: 12 · 2021: 14 · 2020: 11 · 2019: 8 · 2018: 5 · 2017: 5 · 2016: 2 · 2015: 8 · 2014: 3 · 2013: 7 · 2012: 3
FWCI
1.27
Type
journal article
Language
en
Open access
closed
Locations
  • Genomics (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
  • Health Sciences › Medicine › Hepatology › Liver physiology and pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords
ANGPTL3, angiopoietin-like proteins, liver-specific gene expression, angiopoietins, coiled-coil domain, signal peptide, gene cloning, mouse chromosome 4, radiation hybrid mapping, liver development, cysteine disulfide bonds
MeSH terms
Angiopoietin-like Proteins, Angiopoietin-Like Protein 3, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Chromosomes, Human, Pair 1, Glycosylation, Growth Substances, Humans, Liver, Membrane Glycoproteins, Molecular Sequence Data, Organ Specificity, Proteins, RNA, Messenger, Blotting, Northern, Sequence Homology, Amino Acid, Sequence Analysis, DNA, Physical Chromosome Mapping, Amino Acid Motifs, Intercellular Signaling Peptides and Proteins, Angiopoietins, Angiopoietin-1, Angiopoietin-2, Mice

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