Linked Life Data

18022329

Source:http://linkedlifedata.com/resource/pubmed/id/18022329

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2007-12-18
pubmed:databankReference
pubmed:abstractText
Human RCAN3 (Regulator of calcineurin 3; previously known as DSCR1L2, Down syndrome critical region gene 1-like 2) is a five-exon gene mapped on chromosome 1 and belongs to the human RCAN gene family which also includes RCAN1 and RCAN2. The novel denomination RCAN for genes and proteins, instead of DSCR1L (Down syndrome critical region gene 1-like) has recently been widely discussed. The aim of the present work was to perform a multiple approach analysis of five RCAN3 mRNA and encoded protein isoforms, two of which have been identified for the first time in this research. The two new RCAN3 mRNA isoforms, RCAN3-2,4,5, which lacks exon 3, and RCAN3-2,3,5, which lacks exon 4, were identified during RCAN3 RT-PCR (reverse transcription-polymerase chain reaction) cloning, the product of which unexpectedly revealed the presence of five isoforms as opposed to the three previously known. In order to analyze the expression pattern of the five RCAN3 mRNA isoforms in seven different human tissues, a quantitative relative RT-PCR was performed: interestingly, all isoforms are present in all tissues investigated, with a statistically significant constant prevalence of RCAN3 isoform (the most complete, "reference" isoform). The RCAN3 locus expression level was comparable in all seven tissues analyzed, considering all isoforms, which indicates a ubiquitous expression of this human RCAN family member. To date two possible interactors have been described for this protein: human cardiac troponin I (TNNI3) and calcineurin. Here we report the interaction between the new RCAN3 variants and TNNI3, demonstrated by both yeast cotransformation and by the GST (glutathione-sepharose transferase) fusion protein assay, as was to be expected from the presence of exon 2 whose product has been seen to be sufficient for binding to TNNI3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
407
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
159-68
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:18022329-Adaptor Proteins, Signal Transducing, pubmed-meshheading:18022329-Amino Acid Sequence, pubmed-meshheading:18022329-Cloning, Molecular, pubmed-meshheading:18022329-DNA, Complementary, pubmed-meshheading:18022329-Exons, pubmed-meshheading:18022329-Glutathione Transferase, pubmed-meshheading:18022329-Humans, pubmed-meshheading:18022329-Molecular Sequence Data, pubmed-meshheading:18022329-Protein Interaction Domains and Motifs, pubmed-meshheading:18022329-Protein Isoforms, pubmed-meshheading:18022329-Proteins, pubmed-meshheading:18022329-RNA, Messenger, pubmed-meshheading:18022329-Recombinant Fusion Proteins, pubmed-meshheading:18022329-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:18022329-Tissue Distribution, pubmed-meshheading:18022329-Troponin T, pubmed-meshheading:18022329-Two-Hybrid System Techniques, pubmed-meshheading:18022329-Yeasts
pubmed:year
2008
pubmed:articleTitle
Identification and analysis of human RCAN3 (DSCR1L2) mRNA and protein isoforms.
pubmed:affiliation
Department of Histology, Embryology and Applied Biology, University of Bologna, Via Belmeloro, Bologna (BO), Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't