Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-12-22
pubmed:abstractText
Biosynthetic studies on the human MUC5AC mucin were performed by immunoprecipitations with antisera recognizing only the non-O-glycosylated apomucin in the colon adenocarcinoma cell line LS 174T. Pulse-chase studies and subcellular fractionations showed that MUC5AC formed dimers in the rough endoplasmic reticulum within 15 min of the initiation of biosynthesis. No non-O-glycosylated species larger than dimers were identified. The dimerization was N-glycosylation-dependent, because tunicamycin treatment significantly lowered the rate of dimerization. When the biosynthesis of MUC5AC apomucin was compared with that of MUC2 apomucin, also produced in the LS 174T cell line, both apomucins were assembled in similar ways with respect to their rates of dimerization with and without inhibition of N-glycosylation. No heterodimerization was observed between the human MUC5AC and the MUC2 apomucins despite the extensive sequence similarities in the positions of the cysteine residues in the C-termini proposed to be involved in mucin dimerization.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-1400449, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-1727693, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-2033060, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-2162354, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-2211687, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-2275814, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-2864688, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-3020051, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7513696, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7529492, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7663117, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7775418, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7778880, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7826332, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-7946402, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8292021, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8300571, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8308060, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8360170, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8621668, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8910003, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8910009, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8948445, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-8975711, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9164870, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9195947, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9201995, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9451015, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9588204, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9668061, http://linkedlifedata.com/resource/pubmed/commentcorrection/9761738-9668062
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
335 ( Pt 2)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
381-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9761738-Amino Acid Sequence, pubmed-meshheading:9761738-Animals, pubmed-meshheading:9761738-Biochemistry, pubmed-meshheading:9761738-Carcinoma, pubmed-meshheading:9761738-Colonic Neoplasms, pubmed-meshheading:9761738-Cross Reactions, pubmed-meshheading:9761738-Dimerization, pubmed-meshheading:9761738-Endoplasmic Reticulum, Rough, pubmed-meshheading:9761738-Gastric Mucins, pubmed-meshheading:9761738-Glycosylation, pubmed-meshheading:9761738-Humans, pubmed-meshheading:9761738-Immune Sera, pubmed-meshheading:9761738-Molecular Sequence Data, pubmed-meshheading:9761738-Mucin 5AC, pubmed-meshheading:9761738-Mucin-2, pubmed-meshheading:9761738-Mucins, pubmed-meshheading:9761738-Rabbits, pubmed-meshheading:9761738-Subcellular Fractions, pubmed-meshheading:9761738-Tumor Cells, Cultured, pubmed-meshheading:9761738-Tunicamycin, pubmed-meshheading:9761738-Ultracentrifugation
pubmed:year
1998
pubmed:articleTitle
Human MUC5AC mucin dimerizes in the rough endoplasmic reticulum, similarly to the MUC2 mucin.
pubmed:affiliation
Department of Medical Biochemistry, Göteborg University, Medicinaregatan 9A, S-413 90 Gothenburg, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't