Linked Life Data

12809519

Source:http://linkedlifedata.com/resource/pubmed/id/12809519

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2003-6-17
pubmed:abstractText
Polycystin-L (PCL) is an isoform of polycystin-2, the product of the second gene associated with autosomal dominant polycystic kidney disease, and functions as a Ca(2+)-regulated nonselective cation channel. We recently demonstrated that polycystin-2 interacts with troponin I, an important regulatory component of the actin microfilament complex in striated muscle cells and an angiogenesis inhibitor. In this study, using the two-microelectrode voltage-clamp technique and Xenopus oocyte expression system, we showed that the calcium-induced PCL channel activation is substantially inhibited by the skeletal and cardiac troponin I (60% and 31% reduction, respectively). Reciprocal co-immunoprecipitation experiments demonstrated that PCL physically associates with the skeletal and cardiac troponin I isoforms in overexpressed Xenopus oocytes and mouse fibroblast NIH 3T3 cells. Furthermore, both native PCL and cardiac troponin I were present in human heart tissues where they indeed associate with each other. GST pull-down and microtiter binding assays showed that the C-terminus of PCL interacts with the troponin I proteins. The yeast two-hybrid assay further verified this interaction and defined the corresponding interacting domains of the PCL C-terminus and troponin I. Taken together, this study suggests that troponin I acts as a regulatory subunit of the PCL channel complex and provides the first direct evidence that PCL is associated with the actin cytoskeleton through troponin I.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7618-25
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12809519-3T3 Cells, pubmed-meshheading:12809519-Amino Acid Sequence, pubmed-meshheading:12809519-Animals, pubmed-meshheading:12809519-Calcium, pubmed-meshheading:12809519-Calcium Channels, pubmed-meshheading:12809519-Drug Interactions, pubmed-meshheading:12809519-Glutathione Transferase, pubmed-meshheading:12809519-Humans, pubmed-meshheading:12809519-Ion Channels, pubmed-meshheading:12809519-Membrane Glycoproteins, pubmed-meshheading:12809519-Mice, pubmed-meshheading:12809519-Molecular Sequence Data, pubmed-meshheading:12809519-Muscle, Skeletal, pubmed-meshheading:12809519-Myocardium, pubmed-meshheading:12809519-Oocytes, pubmed-meshheading:12809519-Patch-Clamp Techniques, pubmed-meshheading:12809519-Phosphoproteins, pubmed-meshheading:12809519-Protein Isoforms, pubmed-meshheading:12809519-Receptors, Cell Surface, pubmed-meshheading:12809519-Sequence Homology, Amino Acid, pubmed-meshheading:12809519-Sequence Tagged Sites, pubmed-meshheading:12809519-Troponin I, pubmed-meshheading:12809519-Two-Hybrid System Techniques, pubmed-meshheading:12809519-Xenopus
pubmed:year
2003
pubmed:articleTitle
Troponin I binds polycystin-L and inhibits its calcium-induced channel activation.
pubmed:affiliation
Membrane Protein Research Group, Department of Physiology, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't