Show simple item record

dc.contributor.authorEast, L
dc.contributor.authorRushton, S
dc.contributor.authorTaylor, ME
dc.contributor.authorIsacke, CM
dc.date.accessioned2018-07-31T14:35:01Z
dc.date.issued2002-12
dc.identifier.citationThe Journal of biological chemistry, 2002, 277 (52), pp. 50469 - 50475
dc.identifier.issn0021-9258
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2237
dc.identifier.eissn1083-351X
dc.identifier.doi10.1074/jbc.m208985200
dc.description.abstractMembers of the mannose receptor family, the mannose receptor, the phospholipase A(2) receptor, DEC-205, and Endo180, contain multiple C-type lectin-like domains (CTLDs) within a single polypeptide. In addition, at their N termini, all four family members contain a cysteine-rich domain similar to the R-type carbohydrate recognition domains of ricin. However, despite the common presence of multiple lectin-like domains, these four endocytic receptors have divergent ligand binding activities, and it is clear that the majority of these domains do not bind sugars. Here the functions of the lectin-like domains of the most recently discovered family member, Endo180, have been investigated. Endo180 is shown to bind in a Ca(2+)-dependent manner to mannose, fucose, and N-acetylglucosamine but not to galactose. This activity is mediated by one of the eight CTLDs, CTLD2. Competition assays indicate that the monosaccharide binding specificity of Endo180 CTLD2 is similar to that of mannose receptor CTLD4. However, additional experiments indicate that, unlike the cysteine-rich domain of the mannose receptor, the cysteine-rich domain of Endo180 does not bind sulfated sugars. Thus, although Endo180 and the mannose receptor are now both known to be mannose binding lectins, each receptor is likely to have a distinct set of glycoprotein ligands in vivo.
dc.formatPrint-Electronic
dc.format.extent50469 - 50475
dc.languageeng
dc.language.isoeng
dc.subjectHumans
dc.subjectCalcium
dc.subjectMonosaccharides
dc.subjectPeptide Fragments
dc.subjectMembrane Glycoproteins
dc.subjectLectins
dc.subjectLectins, C-Type
dc.subjectMannose-Binding Lectins
dc.subjectReceptors, Cell Surface
dc.subjectReceptors, Mitogen
dc.subjectRecombinant Proteins
dc.subjectDNA Primers
dc.subjectRestriction Mapping
dc.subjectCloning, Molecular
dc.subjectBinding Sites
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectSubstrate Specificity
dc.subjectKinetics
dc.subjectMolecular Sequence Data
dc.titleCharacterization of sugar binding by the mannose receptor family member, Endo180.
dc.typeJournal Article
rioxxterms.versionofrecord10.1074/jbc.m208985200
rioxxterms.licenseref.startdate2002-12
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfThe Journal of biological chemistry
pubs.issue52
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research/Molecular Cell Biology
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research/Molecular Cell Biology
pubs.publication-statusPublished
pubs.volume277
pubs.embargo.termsNot known
icr.researchteamMolecular Cell Biologyen_US
dc.contributor.icrauthorIsacke, Clareen


Files in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record