What question did this study set out to answer?

To determine why rhesus monkey lipoprotein(a) binds less efficiently to lysine-Sepharose and monocytoid cells than human lipoprotein(a), identifying the specific structural domains responsible.

January 1, 1993Journal of Clinical InvestigationOpen Access

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).

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Why the study?

Does rhesus Lp(a) bind less efficiently to lysine and cells compared to human Lp(a)?

Population

17 rhesus monkeys and human subjects (n=11 for plasma, n=3 for purified Lp)

Comparison

Rhesus monkey lipoprotein(a) (Lp[a]) vs Human lipoprotein(a) (Lp[a])

Design

Preclinical

Authors

ASA M ScanuCenter for Rheumatology LMLindsey A. MilesScripps Research Institute GFG M FlessUniversity of Chicago

Discussion

Member takes

Implication

Rhesus Lp(a) may be less thrombogenic; leaves open whether kringle variants affect human Lp(a) risk.

Key Points

To determine why rhesus monkey lipoprotein(a) binds less efficiently to lysine-Sepharose and monocytoid cells than human lipoprotein(a), identifying the specific structural domains responsible.
Evaluated the binding affinity of human and rhesus lipoprotein(a) to lysine-Sepharose and cultured U937 monocytoid cells using elastase-derived plasminogen fragments.
Conducted comparative sequence analysis and molecular modeling of human and simian apolipoprotein(a) kringle 4 domains.
Rhesus lipoprotein(a) exhibited impaired binding to lysine-Sepharose and U937 cells compared to human lipoprotein(a), with interactions localized to the kringle 4 region rather than kringle 5 or the protease domain.
Kringle 4(37) was identified as dominant in lysine binding, with an arginine 72 substitution in rhesus lipoprotein(a) replacing tryptophan in human lipoprotein(a) to cause the functional binding deficiency.

Structured PICO

Does rhesus Lp(a) bind less efficiently to lysine and cells compared to human Lp(a)?

Population

17 rhesus monkeys (13 from a pedigree with/without LDL receptor deficiency, 4 unrelated) and human subjects (n=11 for plasma, n=3 for purified Lp(a))

Intervention

Rhesus monkey lipoprotein(a) (Lp[a])

Comparator

Human lipoprotein(a) (Lp[a])

Outcome

Binding efficiency to lysine-Sepharose and cultured U937 monocytoid cellssurrogate

Rhesus Lp(a) binds less efficiently to lysine and cells than human Lp(a) due to an arginine substitution in kringle 4(37), suggesting it may be less thrombogenic.

Cite This Study

Scanu et al. (1993) studied this question.

synapsesocial.com/papers/6a8381fcaf1ae4bfdd7211c8 https://doi.org/10.1172/jci116182

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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).

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

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).

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

Also Consider

Also Consider