Linked Life Data

9058786

Source:http://linkedlifedata.com/resource/pubmed/id/9058786

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-4-2
pubmed:abstractText
Pre-B cells can express secretory mu (mu(s))- as well as membrane mu (mu(m))-chains. We evaluated the ability of mu(s)-chains to associate with surrogate light chains and assemble into a pre-B cell receptor (BCR) complex in pre-B cells, and explored whether mu(s)-chains could be exploited to generate a secreted soluble pre-BCR. We demonstrate that mu(s)-chains can associate with SLC internally. The mu(s)-containing complexes form higher order polymeric structures, but these are never assembled into completed covalent structures. Instead, the complexes are efficiently retained and rapidly degraded. Alteration of the intracellular redox state by incubation with 2-ME resulted in the secretion of mu(s)-chains, suggesting that they are retained by a thiol-mediated retention mechanism. To identify the sequences on mu(s)-chains responsible for their retention, we generated stable transfectants of a mu-negative pre-B cell line expressing either wild-type or mutant mu(s) constructs. Mutation of a single cysteine (Cys575) in the mu(s) tailpiece resulted in the release and secretion of the mu(s) H chains. These were associated with the surrogate light chain proteins lambda5 and VpreB, and thus appear to constitute an authentic secreted soluble pre-BCR. The soluble pre-BCR has a specificity distinct from Ab consisting of the same heavy chain V region paired with conventional light chains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
158
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2551-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Secretion of soluble pre-B cell receptors by pre-B cells.
pubmed:affiliation
Department of Microbiology, Boston University School of Medicine, MA 02118, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't