Source:http://linkedlifedata.com/resource/pubmed/id/10224500
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1999-6-29
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pubmed:abstractText |
During the process of terminal differentiation, the fibre cells in the eye lens undergo many changes that are reminiscent of apoptotic/necrotic changes. Mitochondria, for instance, undergo permeability transition and nuclear degradation is accompanied by chromatin condensation, disintegration of the nucleolus, dissolution of the nuclear lamina, nuclear pore clustering and fragmentation of the DNA into oligonucleosomal fragments. As during apoptosis, members of the caspase family of proteases were shown to be active during fibre cell differentiation and Bcl-2 overexpression was demonstrated to block normal differentiation of lens cells. In this review, the current knowledge of the sequence of events during cell death is summarised and contrasted with events during lens fibre cell differentiation. Due to the numerous similarities between these processes, lens fibre cell differentiation is suggested to represent an attenuated form of cell death.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0030-3747
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
163-83
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10224500-Animals,
pubmed-meshheading:10224500-Apoptosis,
pubmed-meshheading:10224500-Calcium,
pubmed-meshheading:10224500-Caspases,
pubmed-meshheading:10224500-Cell Cycle,
pubmed-meshheading:10224500-Cell Differentiation,
pubmed-meshheading:10224500-Cell Nucleus,
pubmed-meshheading:10224500-Cytoskeleton,
pubmed-meshheading:10224500-Humans,
pubmed-meshheading:10224500-Lens, Crystalline,
pubmed-meshheading:10224500-Mitochondria,
pubmed-meshheading:10224500-Necrosis
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pubmed:year |
1999
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pubmed:articleTitle |
Lens fibre cell differentiation - A link with apoptosis?
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pubmed:affiliation |
Department of Biochemistry, Medical Sciences Institute, University of Dundee, UK. ralf.dahm@tuebingen.mpg.de
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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