Vitronectin

Vitronectin is a glycoprotein present in the extracellular matrix and in serum. It promotes cell adhesion and spreading, inhibits the membrane-damaging effect of the terminal cytolytic complement pathway, and binds to several serum proteins including the anticoagulant, protein S.

Structure

Vitronectin is a large, multi-functional glycoprotein. It is composed of a single chain of 459 amino acids and has a molecular weight of approximately 75 kDa. The protein is rich in cysteine residues, which form multiple disulfide bonds that contribute to the stability of the protein's structure.

Function

Vitronectin plays a key role in a variety of important biological processes. It is involved in hemostasis, the process that causes bleeding to stop, and it also plays a role in cell migration and tissue repair. In addition, vitronectin has been found to inhibit apoptosis, or programmed cell death, and to promote cell proliferation and differentiation.

Clinical significance

Abnormal levels of vitronectin have been associated with a variety of diseases. Elevated levels of vitronectin have been found in the blood of patients with liver cirrhosis and lung cancer, and decreased levels have been observed in patients with sepsis. In addition, mutations in the vitronectin gene have been linked to age-related macular degeneration, a common cause of blindness in older adults.

See also

• Extracellular matrix
• Glycoprotein
• Cell adhesion
• Protein S

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