PubMed · 14383148
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K SIMON. 1955-03-31. [New fields for using heparin].. https://pubmed.ncbi.nlm.nih.gov/14383148/
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Heparins and low-molecular-weight heparins (LMWHs) have been the mainstay for the prevention and management of venous and arterial thromboembolic disease. In particular, the LMWHs have become well established in the past 15 years for the prevention of thrombosis in medium- and high-risk surgical and medical patients and in the initial management of venous thromboembolism (VTE). They have also been widely evaluated and adopted in clinical practice in the management of patients with acute coronary syndromes. More recently, a variety of heparin-like drugs have been evaluated as potential antithrombotic agents, and the synthetic pentasaccharide (fondaparinux) has been developed and evaluated for the prevention and treatment of VTE.
Thrombospondin 1 (TSP1) was first recognized as a thrombin-sensitive protein associated with platelet membranes. It is secreted by numerous cell types and its expression is predominant in areas of active tissue remodeling. Thrombospondins 1 and 2 are large, trimeric, matricellular proteins, composed of multiple structural motifs which interact with a diverse array of receptors and molecules. Thrombospondin's capacity to bind multiple receptors renders it multifunctional. The functions of its isolated domains can be overlapping or contradictory. In this review, we focus on the N-terminus of the molecule, first recognized for its strong heparin binding properties and characterized by its susceptibility to proteolytic cleavage from the stalk region of thrombospondin. The N-terminus, called the heparin binding domain (HBD), interacts with a variety of macromolecules including heparan sulfate proteoglycans at the membrane and in the matrix, LDL receptor-related protein (LRP), sulfated glycolipids, calreticulin, and integrins. The HBD mediates endocytosis of thrombospondin. It functions both as a soluble and an insoluble modulator of cell adhesion and motility. In contrast to thrombospondin, the HBD has pro-angiogenic activity. We propose that the HBD of thrombospondins 1 and 2 are found primarily in the cellular microenvironment in conditions of cellular injury, stress and tissue remodeling and that the HBD conveys multiple signals involved in cellular adaptation to injury.