Abstract
Lipoprotein (a) (Lp (a)) may be pro-thrombotic in humans due to its apolipoprotein (a) (apo(a))-mediated decreases in fibrinolysis. Such decreased fibrinolysis arises putatively from interference with plasminogen conversion to plasmin due to the considerable homology between apolipoprotein (a) and plasminogen. However, in vitro, most studies have shown that human Lp (a) decreases agonist-stimulated platelet aggregation while in vivo it appears to decrease aggregation as implied by increased bleeding times with higher blood serum concentrations of Lp(a). Lp (a) binding to platelets mediated by apo (a) increases platelet intracellular c-AMP levels in resting platelets, and decreases platelet production of thromboxane A2 and fibrinogen binding to platelets all of which reduce platelet aggregation. One, though not the only, explanation of these conflicting data may be that Lp(a) self-regulates its interference with fibrinolysis by reducing platelet aggregation and platelet binding of fibrinogen and hence the degree of requirement for fibrinolysis. However, it is concluded more in vivo work needs to be done to fully understand whether, if at all, Lp(a) in varying concentrations and isoforms, favours reduced platelet aggregation or fibrinolysis.
Keywords: Lipoprotein (a), platelet aggregation, fibrinolysis, fibrinogen, cyclic adenosine monophosphate, thromboxane A2
Protein & Peptide Letters
Title: The Molecular Nature and Consequences of Lipoprotein (A)s Association with Platelets
Volume: 14 Issue: 9
Author(s): D. E. Barre
Affiliation:
Keywords: Lipoprotein (a), platelet aggregation, fibrinolysis, fibrinogen, cyclic adenosine monophosphate, thromboxane A2
Abstract: Lipoprotein (a) (Lp (a)) may be pro-thrombotic in humans due to its apolipoprotein (a) (apo(a))-mediated decreases in fibrinolysis. Such decreased fibrinolysis arises putatively from interference with plasminogen conversion to plasmin due to the considerable homology between apolipoprotein (a) and plasminogen. However, in vitro, most studies have shown that human Lp (a) decreases agonist-stimulated platelet aggregation while in vivo it appears to decrease aggregation as implied by increased bleeding times with higher blood serum concentrations of Lp(a). Lp (a) binding to platelets mediated by apo (a) increases platelet intracellular c-AMP levels in resting platelets, and decreases platelet production of thromboxane A2 and fibrinogen binding to platelets all of which reduce platelet aggregation. One, though not the only, explanation of these conflicting data may be that Lp(a) self-regulates its interference with fibrinolysis by reducing platelet aggregation and platelet binding of fibrinogen and hence the degree of requirement for fibrinolysis. However, it is concluded more in vivo work needs to be done to fully understand whether, if at all, Lp(a) in varying concentrations and isoforms, favours reduced platelet aggregation or fibrinolysis.
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Cite this article as:
Barre E. D., The Molecular Nature and Consequences of Lipoprotein (A)s Association with Platelets, Protein & Peptide Letters 2007; 14 (9) . https://dx.doi.org/10.2174/092986607782110202
DOI https://dx.doi.org/10.2174/092986607782110202 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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