Using C. elegans to identify the protease targets of serpins in vivo

Sangeeta R. Bhatia, Mark T. Miedel, Cavita K. Chotoo, Nathan J. Graf, Brian L. Hood, Thomas P. Conrads, Gary A. Silverman, Cliff J. Luke

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

5 Scopus citations

Abstract

Most serpins inhibit serine and/or cysteine proteases, and their inhibitory activities are usually defined in vitro. However, the physiological protease targets of most serpins are unknown despite many years of research. This may be due to the rapid degradation of the inactive serpin:protease complexes and/or the conditions under which the serpin inhibits the protease. The model organism Caenorhabditis elegans is an ideal system for identifying protease targets due to powerful forward and reverse genetics, as well as the ease of creating transgenic animals. Using combinatorial approaches of genetics and biochemistry in C. elegans, the true in vivo protease targets of the endogenous serpins can be elucidated.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages283-299
Number of pages17
DOIs
StatePublished - 2011
Externally publishedYes

Publication series

NameMethods in Enzymology
Volume499
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Caenorhabditis elegans
  • Mass spectrometry
  • RNAi
  • Serpin
  • Tandem affinity purification

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