ArticleThe Journal of clinical investigation1993
Rhesus monkey lipoprotein(a) binds to lysine Sepharose and U937 monocytoid cells less efficiently than human lipoprotein(a). Evidence for the dominant role of kringle 4(37).
Article in The Journal of clinical investigation, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 79 citations in OpenAlex.
- Oxidized phospholipids in cardiovascular disease.Nature reviews. Cardiology · 2024Review
- Lipoprotein(a) beyond the kringle IV repeat polymorphism: The complexity of genetic variation in the LPA gene.Atherosclerosis · 2022Review
- Mechanistic insights into Lp(a)-induced IL-8 expression: a role for oxidized phospholipid modification of apo(a).Journal of lipid research · 2015Article
- Determinants of binding of oxidized phospholipids on apolipoprotein (a) and lipoprotein (a).Journal of lipid research · 2013Article
- Plasma homocysteine and lipoprotein (a) levels in Turkish patients with metabolic syndrome.Heart and vessels · 2005Article
- High-resolution crystal structure of apolipoprotein(a) kringle IV type 7: insights into ligand binding.Protein science : a publication of the Protein Society · 2001Article
- Oxidation of apolipoprotein(a) inhibits kringle-associated lysine binding: the loss of intrinsic protein fluorescence suggests a role for tryptophan residues in the lysine binding site.Protein science : a publication of the Protein Society · 1997Article
- Lipoprotein(a) vascular accumulation in mice. In vivo analysis of the role of lysine binding sites using recombinant adenovirus.The Journal of clinical investigation · 1997Article
- Kringle-containing fragments of apolipoprotein(a) circulate in human plasma and are excreted into the urine.The Journal of clinical investigation · 1996Article
- Evidence that the fibrinogen binding domain of Apo(a) is outside the lysine binding site of kringle IV-10: a study involving naturally occurring lysine binding defective lipoprotein(a) phenotypes.The Journal of clinical investigation · 1996Article
- Sequence polymorphism in kringle IV 37 in linkage disequilibrium with the apolipoprotein (a) size polymorphism.Human genetics · 1995Article
- Interactions of a fluorescently labeled peptide with kringle domains in proteins.Journal of protein chemistry · 1993Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Rhesus lipoprotein(a) (Lp[a]) binds less efficiently than human Lp(a) to lysine-Sepharose and to cultured U937 cells. Studies using elastase-derived plasminogen fragments indicated that neither kringle 5 nor the protease domain of Lp(a) are required in these interactions pointing at an involvement of the K4 region. Comparative structural analyses of both the human and simian apo(a) K4 domain, together with molecular modeling studies, supported the conclusion that K4(37) plays a dominant role in the lysine binding function of apo(a) and that the presence of arginine 72 rather than tryptophan in this kringle can account for the functional deficiency observed with rhesus Lp(a). These in vitro results suggest that rhesus Lp(a) may be less thrombogenic than human Lp(a).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.