Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-4-4
pubmed:abstractText
In the absence of immunoglobulin heavy-chain expression, some immunoglobulin light (L) chains are retained and degraded within the cell. We investigated the fate of two different nonsecreted murine L chains which exhibit different half-lives (50 min and 3-4 hr). Our results demonstrate that both nonsecreted L chains are quantitatively bound to BiP as partially oxidized molecules. The kinetics of L-chain degradation coincided with those of L-chain dissociation from BiP, which suggests that these two processes are functionally related. L-chain degradation does not depend on vesicular transport, indicating that these soluble proteins are degraded in the endoplasmic reticulum (ER). In contrast, secreted L chains, which interact only transiently with BiP, are completely oxidized and are not degraded even when they are artificially retained in the ER. Our data support the model that, by means of BiP interaction, the ER degradation mechanism has the potential to discriminate between partially and completely folded molecules.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-1172191, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-1400441, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-1563355, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-1730749, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-1904064, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2122454, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2139038, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2201450, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2275818, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2501663, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2513329, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2531748, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2565905, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2663883, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2829122, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-2974039, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-3087629, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-3127200, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-3138111, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-3292055, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-3304334, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-3462704, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-6340834, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-6402777, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-8245027, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-825374, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-8305733, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-8314799, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-8388424, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-8449979, http://linkedlifedata.com/resource/pubmed/commentcorrection/7878056-8456316
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1764-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum.
pubmed:affiliation
Institute for Biochemistry I, University of Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't