| pubmed-article:8549682 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8549682 | lifeskim:mentions | umls-concept:C0002257 | lld:lifeskim |
| pubmed-article:8549682 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:8549682 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8549682 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8549682 | pubmed:dateCreated | 1996-2-20 | lld:pubmed |
| pubmed-article:8549682 | pubmed:abstractText | Alpha crystallin can function as a molecular chaperone in suppressing the heat-induced aggregation of other crystallins and proteins. During cataractogenesis, alpha-crystallin becomes a water-insoluble, high-molecular-weight, cross-linked aggregate. To determine whether the chaperone activity of alpha crystallin is lost during this age-related modification, extracts were prepared by sonication of water-insoluble proteins isolated from aged bovine lenses and human cataract lenses. All the preparations were tested for chaperone-like activity using beta L-crystallin as the target protein and the percentage of alpha-crystallin in water-insoluble sonicated supernatant (WISS) was determined by slot blot immunoassay. The WISS from bovine as well as human lenses were still effective in protecting beta L-crystallin aggregation at 56 degrees C. The bovine cortical WISS with 50% immunoreactive alpha-crystallin showed 62% of the chaperone-like activity displayed by native alpha-crystallin. The WISS from bovine lens nucleus and human lenses with 17% and 5% immunoreactive alpha-crystallin showed 19% and 4% chaperone-like activity compared to native alpha-crystallin. Prior treatment of the WISS of both bovine and human lenses with dithiothreitol resulted in nearly 50% increase in chaperone-like activity suggesting possible loss of chaperone-like activity due to disulfide cross-links. To see if the chaperone-like activity of alpha-crystallin can be altered by non-disulfide cross-linking, native alpha-crystallin isolated from bovine lenses was cross-linked with dimethylsuberimidate (DMS) and dimethyl 3,3'-dithiobispropionimidate (DTBP) and tested for chaperone-like activity. The DMS cross-linked alpha-crystallin was effective in inhibiting the aggregation of beta L-crystallins at 56 degrees C, but required a two- to five-fold higher concentration than the native alpha-crystallin. alpha-Crystallin with higher degree of cross-linking showed lower chaperone-like activity. alpha-Crystallin cross-linked with DTBP, a cleavable cross-linking agent, also showed a 80% loss in chaperone-like activity. However, when the DTBP cross-linked alpha-crystallin was treated with dithiothreitol to cleave the cross-links there was a 50% recovery in the chaperone-like activity. These data suggest that the age-related cross-linking, which restricts the molecular flexibility of alpha-crystallin decreases its chaperone-like function. | lld:pubmed |
| pubmed-article:8549682 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8549682 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8549682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8549682 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8549682 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8549682 | pubmed:issn | 0014-4835 | lld:pubmed |
| pubmed-article:8549682 | pubmed:author | pubmed-author:SharmaK KKK | lld:pubmed |
| pubmed-article:8549682 | pubmed:author | pubmed-author:OrtwerthB JBJ | lld:pubmed |
| pubmed-article:8549682 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8549682 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:8549682 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8549682 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8549682 | pubmed:pagination | 413-21 | lld:pubmed |
| pubmed-article:8549682 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:8549682 | pubmed:meshHeading | pubmed-meshheading:8549682-... | lld:pubmed |
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| pubmed-article:8549682 | pubmed:meshHeading | pubmed-meshheading:8549682-... | lld:pubmed |
| pubmed-article:8549682 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8549682 | pubmed:articleTitle | Effect of cross-linking on the chaperone-like function of alpha crystallin. | lld:pubmed |
| pubmed-article:8549682 | pubmed:affiliation | Mason Institute of Ophthalmology, University of Missouri, Columbia 65212, USA. | lld:pubmed |
| pubmed-article:8549682 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8549682 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8549682 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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