Polyglutamine domains are substrates of tissue transglutaminase: does transglutaminase play a role in expanded CAG/poly-Q neurodegenerative diseases?

Published

Journal Article

Huntington's disease and six other neurodegenerative diseases are associated with abnormal gene products containing expanded polyglutamine (poly-Q; Qn) domains (n > or = 40). In the present work, we show that glutathione S-transferase (GST) fusion proteins containing a small, physiological-length poly-Q domain (GSTQ10) or a large, pathological-length poly-Q domain (GSTQ62) are excellent substrates of guinea pig liver (tissue) transglutaminase and that both GSTQ10 and GSTQ62 are activators of tissue transglutaminase-catalyzed hydroxaminolysis of N-alpha-carbobenzoxyglutaminylglycine. The present findings have implications for understanding the pathophysiological mechanisms of expanded CAG/poly-Q domain diseases.

Full Text

Duke Authors

Cited Authors

  • Cooper, AJ; Sheu, KF; Burke, JR; Onodera, O; Strittmatter, WJ; Roses, AD; Blass, JP

Published Date

  • July 1997

Published In

Volume / Issue

  • 69 / 1

Start / End Page

  • 431 - 434

PubMed ID

  • 9202340

Pubmed Central ID

  • 9202340

International Standard Serial Number (ISSN)

  • 0022-3042

Digital Object Identifier (DOI)

  • 10.1046/j.1471-4159.1997.69010431.x

Language

  • eng

Conference Location

  • England