Literature DB >> 2872082

Ca2+-dependent inactivation of acetylcholine receptors by an endogenous transglutaminase.

F Hucho, G Bandini.   

Abstract

The nicotinic acetylcholine receptor (nAChR) from Torpedo californica and T. marmorata electric tissue polymerises irreversibly when DTE and Ca2+ are added to receptor-rich membranes. The polymerisation is time-dependent and complete within 3 h at 30 degrees C. It can be completely prevented by EGTA or the transglutaminase inhibitor cystamine. Transglutaminase activity can also be monitored with the exogenous substrates [3H]putrescine and dimethylcasein. This assay can also be inhibited by EGTA or cystamine.

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Year:  1986        PMID: 2872082     DOI: 10.1016/0014-5793(86)81152-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Transglutaminase in membranes rich in nicotinic acetylcholine receptors.

Authors:  G Bandini; F Hucho
Journal:  J Protein Chem       Date:  1989-06

2.  Stabilization of collagen-tailed acetylcholinesterase in muscle cells through extracellular anchorage by transglutaminase-catalyzed cross-linking.

Authors:  D Hand; D Dias; L W Haynes
Journal:  Mol Cell Biochem       Date:  2000-01       Impact factor: 3.396

  2 in total

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