Partially purified flounder muscle (Pseudopleuronectus americanus) glyceraldehyde 3-phosphate dehydrogenase was immobilized on cyanogen bromide-activated Sepharose. The catalytic properties of the immobilized preparation were studied to determine if immobilization alters the kinetic properties of th
Glyceraldehyde-3-phosphate dehydrogenase and apoptosis
β Scribed by M.D. Berry; A.A. Boulton
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 62 KB
- Volume
- 60
- Category
- Article
- ISSN
- 0360-4012
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β¦ Synopsis
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as playing an integral role in glycolysis. During the past 20 years, however, a number of novel, additional functions for GAPDH have been described. These include acting as an uracil DNA glycosylase, activator of transcription, binding to RNA, and an involvement in tubulin assembly. One of the most intriguing functions which has recently been recognized is an involvement in the initiation of apoptosis. Further, GAPDH associates with proteins implicated in human neurodegenerative disorders. This review summarizes the evidence implicating GAPDH in the initiation of one or more apoptotic cascades. The possible functions of GAPDH in the nucleus which could result in the initiation of apoptosis are also discussed.
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