Beta-Thromboglobulin
Beta-Thromboglobulin (also known as β-Thromboglobulin or β-TG) is a protein that is released from platelets during platelet activation. It is a member of the CXC chemokine family and is also known as Platelet factor 4 variant 1 (PF4V1).
Structure[edit | edit source]
Beta-Thromboglobulin is a small cytokine belonging to the CXC chemokine family. It is approximately 7.8 kilodaltons in size and is composed of 70 amino acid residues. The protein has a four-stranded antiparallel beta-sheet conformation.
Function[edit | edit source]
Beta-Thromboglobulin is stored in the alpha-granules of platelets and is released upon platelet activation. It plays a role in inflammation and wound healing by promoting neutrophil recruitment and angiogenesis. It also has chemotactic properties, attracting monocytes and lymphocytes to the site of injury.
Clinical significance[edit | edit source]
Levels of Beta-Thromboglobulin in the blood can be measured as a marker of platelet activation. Elevated levels of Beta-Thromboglobulin have been associated with various thrombotic conditions, including myocardial infarction, stroke, and deep vein thrombosis. It may also be elevated in conditions associated with increased platelet turnover, such as immune thrombocytopenic purpura and myeloproliferative disorders.
See also[edit | edit source]
References[edit | edit source]
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