Discovery and development of direct Xa inhibitors Xa was identified as a promising target for the development of new anticoagulants in the early 1980s. In 1987 the first factor Xa inhibitor, the naturally occurring compound antistasin, was isolated from the salivary glands of the Mexican leech "Haementeria officinalis". Antistasin is a polypeptide and a potent Xa inhibitor. In 1990 another naturally occurring Xa inhibitor was isolated, tick anticoagulant peptide (TAP) from extracts of the tick "Ornithodoros moubata". TAP and antistasin were used to estimate factor Xa as a drug target. Blood coagulation is a complex process by which the blood forms clots. It is an essential part
Formyl peptide receptor 3 derived from the N-terminal sequence of heme-binding protein 1 by cathepsin D cleavage that potently stimulates chemotaxis through FPR3 in monocytes and monocyte-derived dendritic cells. F2L thereby may be a pro-inflammatory stimulus for FPR3. Similar to FPR2 (see FPR2 section), FPR3 is activated by humanin and thereby may be involved in inhibiting the inflammation occurring in and perhaps contributing to Alzheimer's disease. Formyl peptide receptor 3 N-formyl peptide receptor 3 (FPR3) is a receptor protein that in humans is encoded by the "FPR3" gene. Confusingly, there are two nomenclatures for FPR receptors and their genes, the first one used, FPR,