[6] The gene SELP encoding P-selectin is located on chromosome 1q21-q24, spans > 50 kb and contains 17 exons in humans.

[9] When megakaryocytes and endothelial cells are activated by agonists such as thrombin, P-selectin is rapidly translocated to the plasma membrane from granules.

[10] Secondly, increased levels of P-selectin mRNA and protein are induced by inflammatory mediators such as tumor necrosis factor-a (TNF-a), LPS, and interleukin-4 (IL-4).

[11][12][13] The elevated synthesis of P-selectin may play an important role in the delivery of protein to the cell surface.

The number of CRP repeats is the major feature differentiating the type of selectin in extracellular region.

[17] P-selectin plays an essential role in the initial recruitment of leukocytes (white blood cells) to the site of injury during inflammation.

[22] Moreover, platelets facilitate tumor metastasis by forming complexes with tumour cells and leukocytes in the vasculature, thus preventing recognition by macrophages.

[23] In vivo mice experiments have shown that a reduction in circulating platelets could reduce cancer metastasis.

[26] Selective removal of mucin results in reduced interaction between P-selectin and platelets in vivo and in vitro.

[23] Heparin has long been known to represent antiheparanase activity that is to keep an endoglycosidase from degrading heparan sulfate, one of the glycosaminoglycans, and to effectively inhibit P-selectin.