Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-27T02:59:56.537Z Has data issue: false hasContentIssue false

Alterations in the Molecular Interaction of Bcl-2 and Bax During Apoptosis Assessed Using Fluroescence Resonance Energy Transfer (FRET) Microscopy and Green Fluorescent Protein (GFP)-Bax and Blue Fluorescent Protein (BFP)-Bcl-2 Expressing Proteins

Published online by Cambridge University Press:  02 July 2020

N. Mahajan
Affiliation:
Department of Cell Biology and Anatomy, University of North Carolina at Chapel Hill, Chapel Hill, NC27599
B. Herman
Affiliation:
Department of Cell Biology and Anatomy, University of North Carolina at Chapel Hill, Chapel Hill, NC27599
Get access

Extract

Apoptosis or programmed cell death, is a mechanism of cellular demise which is believed to play a role in many physiological processes, and which when defective, can contribute to the pathogenesis of cancer. Apoptosis is stimulated in cells by the p53 tumor suppresser, Bax and El A proteins and inhibited by overexpression of Bcl-2 and adenovirus E1B 19 kDa oncoproteins. A role for altered apoptosis in cancer comes from recent reports which have documented that inactivation of p53 (which promotes apoptosis) and/or overexpression of bcl-2 (which inhibits apoptosis) occurs in numerous cancers. Recent work from our laboratory has shown that inactivation of p53 (either by physical complex formation between p53 and Human Papillomavirus (HPV) type 16- or 18- E6 protein or by mutation of p53), is associated with increased expression of bcl-2 in cervical carcinoma cells. The combination of inactive p53 and increased expression of bcl-2 may lead to inhibition of apoptosis and thereby contribute to the development or progression of cervical cancer.

Type
Cell Biology Applications of Green Fluorescent Protein and other Vital Labeling Probes
Copyright
Copyright © Microscopy Society of America 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)