| pubmed-article:17711303 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C0064239 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C0439834 | lld:lifeskim |
| pubmed-article:17711303 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:17711303 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:17711303 | pubmed:dateCreated | 2007-9-18 | lld:pubmed |
| pubmed-article:17711303 | pubmed:abstractText | We examined glycosylation of FLAG-hKOR expressed in CHO cells and determined its functional significance. FLAG-hKOR was resolved as a broad and diffuse 55-kDa band and a less diffuse 45-kDa band by immunoblotting, indicating that the receptor is glycosylated. Endoglycosidase H cleaved the 45-kDa band to approximately 38 kDa but did not change the 55-kDa band, demonstrating that the 45-kDa band is N-glycosylated with high-mannose or hybrid-type glycan. Peptide-N-glycosidase F digestion of solubilized hKOR or incubation of cells with tunicamycin resulted in two species of 43 and 38 kDa, suggesting that the 43-kDa band is O-glycosylated. FLAG-hKOR was reduced to lower Mr bands by neuraminidase and O-glycosidase, indicating that the hKOR contains O-linked glycan. Mutation of Asn25 or Asn39 to Gln in the N-terminal domain reduced the Mr by approximately 5 kDa, indicating that both residues were glycosylated. The double mutant hKOR-N25/39Q was resolved as a 43-kDa (mature form) and a 38-kDa (intermediate form) band. When transiently expressed, hKOR-N25/39Q had a lower expression level than the wild type. In CHO cells stably expressing the hKOR-N25/39Q, pulse-chase experiments revealed that the turnover rate constants (ke) of the intermediate and mature forms were approximately 3 times those of the wild type. In addition, the maturation rate constant (ka) of the 43-kDa form of hKOR-N25/39Q was 6 times that of the mature form of the wild type. The hKOR-N25/39Q mutant showed increased agonist-induced receptor phosphorylation, desensitization, internalization, and downregulation, without changing ligand binding affinity or receptor-G protein coupling. Thus, N-glycosylation of the hKOR plays important roles in stability and trafficking along the biosynthesis pathway of the receptor protein as well as agonist-induced receptor regulation. | lld:pubmed |
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| pubmed-article:17711303 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17711303 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17711303 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17711303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17711303 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17711303 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:17711303 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:17711303 | pubmed:author | pubmed-author:LiJian-GuoJG | lld:pubmed |
| pubmed-article:17711303 | pubmed:author | pubmed-author:ChenChongguan... | lld:pubmed |
| pubmed-article:17711303 | pubmed:author | pubmed-author:Liu-ChenLee-Y... | lld:pubmed |
| pubmed-article:17711303 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17711303 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:17711303 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:17711303 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17711303 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17711303 | pubmed:pagination | 10960-70 | lld:pubmed |
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| pubmed-article:17711303 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17711303 | pubmed:articleTitle | N-Glycosylation of the human kappa opioid receptor enhances its stability but slows its trafficking along the biosynthesis pathway. | lld:pubmed |
| pubmed-article:17711303 | pubmed:affiliation | Department of Pharmacology and Center for Substance Abuse Research, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA. | lld:pubmed |
| pubmed-article:17711303 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17711303 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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