The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Effect of the number of apolipoprotein(a) kringle 4 domains on immunochemical measurements of lipoprotein(a)
Abstract
Lipoprotein(a) [Lp(a)] has been measured in numerous clinical and epidemiological studies by a variety of immunochemical methods. However, little, if any, consideration has been given to the confounding effect of the size heterogeneity of apolipoprotein(a) [apo(a)] on the measurement of Lp(a). We developed three direct-binding enzyme-linked immunosorbent assays (ELISAs) with detecting antibodies of different specificities to evaluate the effect of apo(a) size on Lp(a) measurement. The three assays used the same monoclonal antibody to capture the apo(a)-containing particles and were calibrated (in nanomoles per liter) with a serum containing apo(a) with 21 kringle 4 domains. Using all three ELISAs, we measured Lp(a) in a group of 723 subjects selected to have a single apo(a) band, as determined by a high-resolution phenotyping system. Essentially identical results were obtained by the two methods that measured Lp(a) by use of either a polyclonal antibody against apo B or a monoclonal antibody against apo(a) that does not recognize the kringle 4 type 2 repeats. In contrast, the ELISA using a monoclonal antibody specific for apo(a) kringle 4 type 2 repeats overestimated Lp(a) concentration in samples containing apo(a) with more than 21 kringle 4 domains and underestimated Lp(a) samples containing apo(a) with fewer than 21 kringle 4 domains. Thus, these differences in Lp(a) values varied as a function of apo(a) size. We conclude that antibody specificity and apo(a) size heterogeneity can significantly affect Lp(a) measurements.
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Citations
Cites
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,385
THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
Scatchard, G. (1949) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1949.tb27297.x · Cited by 19,778
A new technique for the assay of infectivity of human adenovirus 5 DNA
Graham, F. L., & van der Eb, A. J. (1973) · Virology · doi:10.1016/0042-6822(73)90341-3 · Cited by 9,451
Characteristics of a human cell line transformed by DNA from human adenovirus type 5
Graham, F. L., Russell, W. C., Smiley, J., & Nairn, R. (1977) · Journal of General Virology · doi:10.1099/0022-1317-36-1-59 · Cited by 4,793
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 2×
“Calculation of the molar concentration of Lp(a) was based on the concentrations of alanine, aspartic acid, glutamic acid, leucine, lysine, and phenylalanine, and the combined amino acid composition of apo(a) and apo B-100 obtained from the published protein sequences for apo B-100 (21) and apo(a) (2).”
BackgroundMethodA Parathyroid Hormone-Related Protein Implicated in Malignant Hypercalcemia: Cloning and Expression
Suva, L. J., Winslow, G. A., Wettenhall, R. E. H., Hammonds, R. G., Moseley, J. M., Diefenbach-Jagger, H., Rodda, C. P., Kemp, B. E., Rodriguez, H., Chen, E. Y., et al. (1987) · Science · doi:10.1126/science.3616618 · Cited by 1,293
Chait, A., Brazg, R. L., Tribble, D. L., & Krauss, R. M. (1993) · The American Journal of Medicine · doi:10.1016/0002-9343(93)90144-e · Cited by 554
Molecular definition of the extreme size polymorphism in apolipoprotein(a)
Lackner, C., Cohen, J. C., & Hobbs, H. H. (1993) · Human Molecular Genetics · doi:10.1093/hmg/2.7.933 · Cited by 319
Fless, G. M., ZumMallen, M. E., & Scanu, A. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84439-3 · Cited by 274
Marcovina, S. M., Zhang, Z. H., Gaur, V. P., & Albers, J. J. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1343 · Cited by 225
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Cited by
(2009) · JAMA · doi:10.1001/jama.2009.1063 · Cited by 1,753
Cohen, J., Pertsemlidis, A., Kotowski, I. K., Graham, R., Garcia, C. K., & Hobbs, H. H. (2005) · Nature Genetics · doi:10.1038/ng1509 · Cited by 1,381
A Test in Context: Lipoprotein(a)
Tsimikas, S. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2016.11.042 · Cited by 1,137
“Within populations, there is extensive apo(a) protein size heterogeneity, with >40 different isoforms, and thus, >40 different sizes of Lp(a) particles, which is a unique occurrence unlike other circulating proteins, which usually have 1 defined mass (5).”
BackgroundReyes-Soffer, G., Ginsberg, H. N., Berglund, L., Duell, P. B., Heffron, S. P., Kamstrup, P. R., Lloyd-Jones, D. M., Marcovina, S. M., Yeang, C., Koschinsky, M. L., et al. (2022) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atv.0000000000000147 · Cited by 836
Self-citationNordestgaard, B. G., & Langsted, A. (2016) · Journal of Lipid Research · doi:10.1194/jlr.r071233 · Cited by 575
Metadata
- Authors
- Marcovina, S. M., Albers, J. J., Gabel, B., Koschinsky, M. L., & Gaur, V. P.
- Venue
- Clinical Chemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 1995-02-01
- Volume
- 41
- Issue
- 2
- Pages
- 246-255
- ISSN
- 0009-9147 (ISSN-L)
- 1530-8561
- OpenAlex
- W1907534963
- Cited by
- 354
- References
- 19
- FWCI
- 23.74
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Effect of the number of apolipoprotein(a) kringle 4 domains on immunochemical measurements of lipoprotein(a). https://app.cochat.ai/papers/10.1093/clinchem/41.2.246
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- Marcovina, S. M., Albers, J. J., Gabel, B., Koschinsky, M. L., & Gaur, V. P. (1995). Effect of the number of apolipoprotein(a) kringle 4 domains on immunochemical measurements of lipoprotein(a). Clinical Chemistry. https://doi.org/10.1093/clinchem/41.2.246
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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