Cloning and characterization of SCART1, a novel scavenger receptor cysteine-rich type I transmembrane molecule

Publication: Research - peer-reviewJournal article – Annual report year: 2009

Without internal affiliation

  • Author: Holm, Dorte

    University of Southern Denmark

  • Author: Fink, Dorte Rosenbek

    Unknown

  • Author: Grønlund, Jørn

    University of Southern Denmark

  • Author: Hansen, Søren

    University of Southern Denmark

  • Author: Holmskov, Uffe

    University of Southern Denmark

View graph of relations

We have cloned and characterized a novel murine transmembrane molecule, mSCART1 belonging to the scavenger receptor cysteine-rich superfamily. The cDNA encodes a polypeptide chain of 989 amino acids, organized as a type I transmembrane protein that contains eight extracellular SRCR domains followed by a transmembrane region and a cytoplasmic domain. The cytoplasmic domain contains two putative src kinase consensus substrate sequences, three additional potential phosphorylation sites, and two potential internalization motifs. Two possible secreted forms that lack the transmembrane region arise by alternative splicing. The murine SCART1 gene maps to chromosome 7 band F5 and the analysis of the genomic organization showed that the gene spans 12.86 kb and contains 14 exons. Quantitative real-time PCR analyses on murine tissues showed high mSCART1 mRNA expression in the lymph node, the trachea, and the lung, and low expression was found in the thymus, the spleen, the skin, and in tissues throughout the gastrointestinal tract. Comparative studies of the domain organization as well as the cytoplasmic domain of mSCART1 with the other members of the SRCR superfamily show that mSCART1 is highly related to the WC1 family of the SRCR superfamily. Finally, a novel human scavenger receptor cysteine-rich molecule with high homology to mSCART1 was identified by searching in the human genomic databases using the mSCART1 cDNA sequence.
Original languageEnglish
JournalMolecular Immunology
Publication date2009
Volume46
Issue9-9
Pages1663–1672
ISSN0161-5890
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 9
Download as:
Download as PDF
Select render style:
APAAuthorCBEHarvardMLAStandardVancouverShortLong
PDF
Download as HTML
Select render style:
APAAuthorCBEHarvardMLAStandardVancouverShortLong
HTML
Download as Word
Select render style:
APAAuthorCBEHarvardMLAStandardVancouverShortLong
Word

ID: 9679106