Update of the human and mouse SERPIN gene superfamily

Claire Heit, Brian C. Jackson, Monica McAndrews, Mathew W. Wright, David C. Thompson, Gary A. Silverman, Daniel W. Nebert, Vasilis Vasiliou

Research output: Contribution to journalArticlepeer-review

111 Scopus citations

Abstract

The serpin family comprises a structurally similar, yet functionally diverse, set of proteins. Named originally for their function as serine proteinase inhibitors, many of its members are not inhibitors but rather chaperones, involved in storage, transport, and other roles. Serpins are found in genomes of all kingdoms, with 36 human protein-coding genes and five pseudogenes. The mouse has 60 Serpin functional genes, many of which are orthologous to human SERPIN genes and some of which have expanded into multiple paralogous genes. Serpins are found in tissues throughout the body; whereas most are extracellular, there is a class of intracellular serpins. Serpins appear to have roles in inflammation, immune function, tumorigenesis, blood clotting, dementia, and cancer metastasis. Further characterization of these proteins will likely reveal potential biomarkers and therapeutic targets for disease.

Original languageEnglish
Article number22
JournalHuman genomics
Volume7
Issue number1
DOIs
StatePublished - 2013
Externally publishedYes

Keywords

  • Blood clotting
  • Cell death
  • Chaperone
  • Complement
  • Metastatic cancer
  • Serine protease inhibitor
  • Serpins
  • Thrombolysis

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