PubMed · 8042579
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C F Arkin. 1994. Coagulation screening tests.. https://doi.org/10.1093/ajcp%2F102.2.150
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Heparin-induced thrombocytopenia (HIT) is an immunologic complication of drug therapy with potentially serious venous and arterial thrombotic sequelae. Recent studies have provided insight into the molecular and cellular basis of HIT underlying the diagnosis and treatment of this syndrome. Because various approaches to HIT treatment have resulted in mixed success, the use of heparin substitutes, other anticoagulant agents, and adjunctive therapy needs to be clarified. For patients with pre-existing conditions such as deep venous thrombosis or pulmonary embolism, new understanding of the clinicopathologic syndrome of HIT offers the promise of improved antithrombotic therapy. The participation of thrombin in HIT suggests that specific (hirudin and argatroban) thrombin inhibitors may be ideal agents for treating acute HIT.
Elucidation of the mechanism of formation of insoluble protein aggregates is essential to resolve problems such as protein folding diseases. In this study the effects of various types of biomolecules on the aggregation of denatured proteins were investigated. Denatured alpha-lactalbumin, an acidic protein, was found to be precipitated by lactoferricin, a basic peptide derived from lactoferrin. Denatured lysozyme, a basic protein, by itself showed aggregation, which was promoted by addition of native alpha-lactalbumin. Heparin and nucleic acids caused almost instant aggregation of denatured lysozyme. Native lactoferricin was also found to aggregate with heparin or nucleic acids. The results show that denatured/misfolded proteins as well as peptides are highly reactive with other cellular components to form insoluble aggregates and suggest a possible mechanism by which protein folding diseases progress. Most of the above aggregation reactions were inhibited by lactoferrin, which could form soluble complexes with denatured alpha-lactalbumin, heparin, and nucleic acids.