Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/13493
Full metadata record
DC FieldValueLanguage
dc.contributor.authorOsman, N-
dc.contributor.authorMcKenzie, Ian F C-
dc.contributor.authorMouhtouris, E-
dc.contributor.authorSandrin, Mauro S-
dc.date.accessioned2015-05-16T03:21:39Z
dc.date.available2015-05-16T03:21:39Z
dc.date.issued1996-12-20-
dc.identifier.citationThe Journal of Biological Chemistry; 271(51): 33105-9en_US
dc.identifier.otherPUBMEDen
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/13493en
dc.description.abstractWhen alpha(1,2)fucosyltransferase cDNA is expressed in cells that normally express large amounts of the terminal carbohydrate Galalpha(1,3)Gal, and therefore the alpha(1,3)galactosyltransferase (GT), the Galalpha(1,3)Gal almost disappears, indicating that the presence of the alpha(1,2)fucosyltransferase (HT) gene/enzyme alters the synthesis of Galalpha(1,3)Gal. A possible mechanism to account for these findings is enzyme location within the Golgi apparatus. We examined the effect of Golgi localization by exchanging the cytoplasmic tails of HT and GT; if Golgi targeting signals are contained within the cytoplasmic tail sequences of these enzymes then a "tail switch" would permit GT first access to the substrate and thereby reverse the observed dominance of HT. Two chimeric glycosyltransferase proteins were constructed and compared with the normal glycosyltransferases after transfection into COS cells. The chimeric enzymes showed Km values and cell surface carbohydrate expression comparable with normal glycosyltransferases. Co-expression of the two chimeric glycosyltransferases resulted in cell surface expression of Galalpha(1,3)Gal, and virtually no HT product was expressed. Thus the cytoplasmic tail of HT determines the temporal order of action, and therefore dominance, of these two enzymes.en_US
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherCOS Cellsen
dc.subject.otherCytoplasm.metabolismen
dc.subject.otherFucosyltransferases.chemistryen
dc.subject.otherGalactosides.metabolismen
dc.subject.otherGalactosyltransferases.metabolismen
dc.subject.otherKineticsen
dc.subject.otherRecombinant Fusion Proteinsen
dc.subject.otherStructure-Activity Relationshipen
dc.subject.otherSwineen
dc.titleSwitching amino-terminal cytoplasmic domains of alpha(1,2)fucosyltransferase and alpha(1,3)galactosyltransferase alters the expression of H substance and Galalpha(1,3)Gal.en_US
dc.typeJournal Articleen_US
dc.identifier.journaltitleThe Journal of Biological Chemistryen_US
dc.identifier.affiliationInfectious Diseasesen_US
dc.description.pages33105-9en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/8955158en
dc.type.contentTexten_US
dc.type.austinJournal Articleen
local.name.researcherMouhtouris, Effie
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
crisitem.author.deptInfectious Diseases-
crisitem.author.deptSurgery (University of Melbourne)-
Appears in Collections:Journal articles
Show simple item record

Page view(s)

14
checked on Mar 28, 2024

Google ScholarTM

Check


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.