Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-6-6
pubmed:abstractText
Zero-length chemical crosslinking with 1-ethyl-3-[3-(dimethyl amino)propyl]carbodiimide (EDC) indicated an association of the Ca2+-binding protein S100A2 with tropomyosin (TM) in vitro. The mobility of the crosslinked product on SDS-PAGE gels indicated the formation of a 1:1 complex between S100A2 and TM and the interaction was Ca2+ dependent. Monoclonal antibodies were raised against S100A2 and used to determine its cellular localization in the porcine epithelial cell line LLC PK1. It was found that the localization of S100A2 depended on the differentiation state of the cells, being absent from actin stress fibers in sparsely seeded cultures, but present in the actin-containing microvilli characteristic of differentiated cells. Immunoprecipitations of [35S]methionine-labeled extracts using S100A2 as well as TM-specific antibodies failed to co-precipitate TM and S100A2, indicating a transient association between these two molecules in solution. Affinity chromatography of cell extracts on immobilized recombinant TMs, however, confirmed the Ca2+-dependent interaction between S100A2 and both muscle TMs as well as with high and low molecular mass nonmuscle TMs, suggesting that the binding site resides in one of the conserved regions of TM. Our data demonstrate the possible interaction of S100A2 with TM that is not bound to the microfilaments and indicate a differentiation-related function for S100A2 in LLC PK1 cells. The possible functional implications of this interaction are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
110 ( Pt 5)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
611-21
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9092943-Amino Acid Sequence, pubmed-meshheading:9092943-Animals, pubmed-meshheading:9092943-Antibodies, Monoclonal, pubmed-meshheading:9092943-Biological Markers, pubmed-meshheading:9092943-Birds, pubmed-meshheading:9092943-Calcium, pubmed-meshheading:9092943-Cell Line, pubmed-meshheading:9092943-Chromatography, High Pressure Liquid, pubmed-meshheading:9092943-Cross-Linking Reagents, pubmed-meshheading:9092943-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:9092943-Humans, pubmed-meshheading:9092943-Molecular Sequence Data, pubmed-meshheading:9092943-Muscles, pubmed-meshheading:9092943-Precipitin Tests, pubmed-meshheading:9092943-Protein Binding, pubmed-meshheading:9092943-S100 Proteins, pubmed-meshheading:9092943-Sequence Homology, Amino Acid, pubmed-meshheading:9092943-Swine, pubmed-meshheading:9092943-Tropomyosin
pubmed:year
1997
pubmed:articleTitle
Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins.
pubmed:affiliation
Cold Spring Harbor Laboratory, NY 11724, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't