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SERPINB3 and B4: From biochemistry to biology

  1. Author:
    Sun, Y.
    Sheshadri, Namratha
    Zong, W. X.

  2. Author Address

    Department of Chemical Biology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, NJ 08854, United States. National Cancer Institute, Center for Cancer Research, Frederick, MD 21702, United States. Department of Chemical Biology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, NJ 08854, United States; Rutgers Cancer Institute of New Jersey, New Brunswick, NJ 08903, United States. Electronic address: weixing.zong@pharmacy.rutgers.edu.
    1. Year: 2017
    2. Date: Feb
    3. Epub Date: 9/18/2016
  2. Journal: Seminars in Cell & Developmental Biology
    1. 62
    2. Pages: 170-177
  4. Type of Article: Article
  5. ISSN: 1084-9521
  1. Abstract:

    Human SERPINB3 and SERPINB4 are evolutionary duplicated serine/cysteine protease inhibitors. Genomic analysis indicates that these paralogous genes were encoded from independent loci arising from tandem gene duplication. Although the two molecules share 92% identity of their amino acid sequences, they are distinct in the Reactive Center Loop (RCL) including a hinge region and catalytic sequences which accounts for altered substrate specificity. Elevated expression of the two molecules has been reported to contribute to numerous pathological conditions such as inflammatory diseases and cancer. In this review, we focus on summarizing the biochemical features of SERPINB3/B4 and discussing the mechanistic basis for their biological functions and implications in human diseases.

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External Sources

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  2. DOI: 10.1016/j.semcdb.2016.09.005
  3. PMID: 27637160
  4. View record in Web of Science®
  5. WOS: 000395504100018

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