Thrombospondin

Thrombospondin is a type of glycoprotein that is secreted into the extracellular matrix. It is a part of the Thrombospondin family, which is a group of proteins that have been identified in various species ranging from humans to simple multicellular organisms. Thrombospondin plays a crucial role in cell adhesion, cell migration, and angiogenesis.

Function

Thrombospondin is involved in a variety of biological processes. It plays a significant role in cell-to-cell and cell-to-matrix interactions. This includes the regulation of cell growth, cell differentiation, and apoptosis. Thrombospondin also has a role in platelet aggregation, which is a crucial step in the process of blood clotting.

Structure

Thrombospondin is a large trimeric glycoprotein with a molecular weight of approximately 450,000 Daltons. It is composed of three identical subunits, each of which is heavily glycosylated. The protein has a complex structure, with multiple domains that are involved in its various functions.

Clinical significance

Alterations in the expression of thrombospondin have been associated with a variety of diseases, including cancer, cardiovascular disease, and neurodegenerative disease. In cancer, thrombospondin can act as a tumor suppressor by inhibiting angiogenesis. In cardiovascular disease, it has been implicated in the regulation of inflammation and fibrosis. In neurodegenerative disease, thrombospondin is involved in the regulation of synaptic plasticity.

See also

• Thrombospondin family
• Glycoprotein
• Extracellular matrix
• Cell adhesion
• Cell migration
• Angiogenesis

Thrombospondin Resources
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