Heat shock protein 27 inhibition of the caspase cascade in human breast cancer cells

Cells may die via a programmed cell death called apoptosis. Apoptosis can be triggered by many death signals, some of which cause cytochrome c to be released from the mitochondria initiating the caspase cascade. When there is an over-expression of Heat Shock Protein 27 (HSP27), the cell does not obey the death signals that it receives. In this study, the molecular mechanism for the HSP 27 inhibition of the caspase cascade is described in human breast cancer cells that were engineered to constitutively express HSP 27. HSP 27 directly bound to cytochrome c and inhibited the activation of caspase 9 and caspase 3. In the presence of an excess amount of cytochrome c, the caspase cascade was reactivated. Granzyme B activated caspase 3 even in the presence of HSP 27. This suggests the conclusion that HSP 27 is a novel inhibitor of apoptosis by binding to cytochrome c.

Name thesis:degree_name

Master of Science (MS)

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Chemistry

Grantor dc:publisher

University of Nevada, Las Vegas

Year

2000

Author dc:creator

• Stafford, Lewis Joe

Contributors dc:contributor

• Stephen W. Carper

Statement dc:rights

• IN COPYRIGHT. For more information about this rights statement, please visit http://rightsstatements.org/vocab/InC/1.0/

Language dc:language

English

Identifier

https://oasis.library.unlv.edu/rtds/1174

OAI identifier oai:identifier

oai:oasis.library.unlv.edu:rtds-2173