Lipoprotein(a) and atherosclerosis: New perspectives on the mechanism of action of an enigmatic lipoprotein |
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Authors: | Marlys L Koschinsky |
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Institution: | (1) Department of Biochemistry, Queen’s University, A208 Botterell Hall, K7L 3N6 Kingston, ON, Canada |
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Abstract: | Although elevated plasma concentrations of lipoprotein(a) (Lp(a)) have been identified as a risk factor for coronary heart
disease, the pathophysiologic and physiologic roles of Lp(a) continue to elude basic researchers and clinicians alike. Lp(a)
is a challenging lipoprotein to study because it has a complex structure consisting of a low-density lipoprotein-like moiety
to which is covalently attached the unique glycoprotein apolipoprotein(a) (apo(a)). Apo(a) contains multiply repeated kringle
domains that are similar to a sequence found in the fibrinolytic proenzyme plasminogen; differing numbers of kringle sequences
in apo(a) give rise to Lp(a) isoform size heterogeneity. In addition to elevated plasma concentrations of Lp(a), apo(a) isoform
size has been identified as a risk factor for coronary heart disease, although studies addressing this relationship have been
limited. The similarity of Lp(a) to low-density lipoprotein and plasminogen provides an enticing link between the processes
of atherosclerosis and thrombosis, although a clear demonstration of this association in vivo has not been provided. Clearly,
Lp(a) is a risk factor for both atherothrombotic and purely thrombotic events; a plethora of mechanisms to explain these clinical
findings has been provided by both in vitro studies as well as animal models for Lp(a). |
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