The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Interaction of Lp(a) and of apo(a) with liver cells.
Abstract
Lipoprotein(a) (Lp[a]) is a lipoprotein of high atherogenicity with unknown function. Although it binds in vitro to the low-density lipoprotein (LDL) receptor, it is not clear whether this mechanism also operates in vivo. We studied the interaction of Lp(a) and of apoprotein(a) (apo[a]) with hepatoma cells (HepG2 and Hep3B) with the following results. (1) HepG2 cells exhibited saturable high-affinity binding of LDLs, whereas the majority of Lp(a) binding was of low affinity and nonsaturable. Preincubation of HepG2 cells with LDL markedly reduced cholesterol biosynthesis, but Lp(a) had a much lower effect. (2) When HepG2 cells were preincubated for 48 to 72 hours with Lp(a) or apo(a), 125I-LDL binding was increased by a factor of > 2. During this time, up to approximately 1 microgram of apo(a) per 1 milligram cell protein was found to be cell associated in an undegraded form. Monoclonal antibodies against the LDL receptor did not prevent the increase in LDL binding stimulated by apo(a). (3) Coincubation with LDL caused a significant increase of Lp(a) degradation by HepG2 cells that was probably caused by an increase of Lp(a) uptake in a "hitchhiking"-like process.
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“Other studies have also demonstrated reduced Lp(a) cellular binding relative to LDL for primary human hepatocytes, HepG2, and Hep3B cells82,83, with the caveat that each study varied in its particular experimental conditions.”
From Functional interrogation of cellular Lp(a) uptake by genome-scale CRISPR screening (2025) · cites this paper as [82]
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Cites
cDNA sequence of human apolipoprotein(a) is homologous to plasminogen
McLean, J. W., Tomlinson, J. E., Kuang, W.-J., Eaton, D. L., Chen, E. Y., Fless, G. M., Scanu, A. M., & Lawn, R. M. (1987) · Nature · doi:10.1038/330132a0 · Cited by 1,886 · cited 1×
“Cloning of apo(a) cDNA revealed an unexpected striking homology of the apo(a) structure with plasminogen.(7) In addition to the kringle-5 and the protease domains of plasminogen, from 17 to 34 kringle4—like domains are also present in apo(a), depending on the size of the particular isoform.”
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Functional interrogation of cellular Lp(a) uptake by genome-scale CRISPR screening
Khan, T. G., Bragazzi Cunha, J., Raut, C., Burroughs, M., Vyas, H. S., Leix, K., Goonewardena, S. N., Smrcka, A. V., Speliotes, E. K., & Emmer, B. T. (2025) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2025.119174 · Cited by 6
Metadata
- Authors
- Kostner, G. M.
- Affiliations
- Institute of Medical Biochemistry, University of Graz, Austria.
- Venue
- Arteriosclerosis and Thrombosis: A Journal of Vascular Biology
- Published
- 1993-07
- Volume
- 13
- Issue
- 7
- Pages
- 1101-1109
- ISSN
- 1049-8834
- Cited by
- 28
- References
- 1
- Language
- en
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