Matches in SemOpenAlex for { <https://semopenalex.org/work/W1994775352> ?p ?o ?g. }
- W1994775352 abstract "T4-binding globulin (TBG), the principal carrier of thyroid hormone in serum, is a glycoprotein containing 20% carbohydrate. The importance of the carbohydrate moiety has been previously studied by enzymatic deglycosylation, which showed that deglycosylated TBG retains its original immunological an T4-binding properties. However, the structure and properties of TBG before glycosylation and the steps involved in carbohydrate addition have not been explored. In the present report, we used a human hepatoma cell line (Hep G2) which synthesizes and secretes TBG into the medium. This TBG binds T4 and possesses immunoreactivity and microheterogeneity identical to those of native TBG (nTBG) from serum. Cells were pulsed with [35S]methionine, [3H]mannose, and [3H]glucosamine in the absence or presence of 5 micrograms tunicamycin/ml medium. Materials from cells and media were immunoprecipitated with antibodies specific for nTBG and denatured TBG molecule. They were then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cells incubated with [35S]methionine contained two forms of labeled TBG, with apparent mol wt of 60K (TBG1) and 54K (TBG2). Medium contained only the TBG1 form, which is identical to nTBG in serum. In contrast, in the presence of tunicamycin, the predominant intracellular form of TBG had an apparent mol wt of 44K (TBG3). At no time was this material detected in the medium. [3H]Mannose and [3H]glucosamine labeled both TBG1 and TBG2, but not TBG3. TBG1 and TBG2 reacted with anti-nTBG serum, whereas TBG3 reacted only with anti-dentured TBG serum, specific for the unfolded TBG molecule. Intracellular TBG was rich (80-90%) in high mannose (seven to nine mannose residues) oligosaccharides and was relatively poor (10-20%) in complex-type species, resistant to endoglycosidase H. These results indicate that 1) the precursor nonglycosylated 44K TBG3 is glycosylated to produce TBG2 (54K) and TBG1 (60K); 2) TBG2 contains oligosaccharides rich in mannose and appears to be a major intracellular intermediate in the synthesis of TBG1; 3) only the endoglycosidase H-resistant TBG1 is secreted; and 4) prior glycosylation of TBG appears to be required for the molecule to assume its tertiary structure and, ultimately, for its secretion. However, once the peptide chain is folded, removal of the carbohydrate moieties does not alter the tertiary structure." @default.
- W1994775352 created "2016-06-24" @default.
- W1994775352 creator A5007121924 @default.
- W1994775352 creator A5038183050 @default.
- W1994775352 creator A5073334494 @default.
- W1994775352 date "1986-04-01" @default.
- W1994775352 modified "2023-09-27" @default.
- W1994775352 title "The Role of Glycosylation in the Molecular Conformation and Secretion of Thyroxine-Binding Globulin*" @default.
- W1994775352 cites W1495234535 @default.
- W1994775352 cites W1509508362 @default.
- W1994775352 cites W1521280325 @default.
- W1994775352 cites W1531251848 @default.
- W1994775352 cites W1534242591 @default.
- W1994775352 cites W1559717664 @default.
- W1994775352 cites W1563159976 @default.
- W1994775352 cites W1564666930 @default.
- W1994775352 cites W1569268787 @default.
- W1994775352 cites W1913451380 @default.
- W1994775352 cites W1991933562 @default.
- W1994775352 cites W2017727751 @default.
- W1994775352 cites W2020570553 @default.
- W1994775352 cites W2037092882 @default.
- W1994775352 cites W2037181144 @default.
- W1994775352 cites W2043726924 @default.
- W1994775352 cites W2045682314 @default.
- W1994775352 cites W2059926505 @default.
- W1994775352 cites W2076845293 @default.
- W1994775352 cites W2115912999 @default.
- W1994775352 cites W569295418 @default.
- W1994775352 doi "https://doi.org/10.1210/endo-118-4-1614" @default.
- W1994775352 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3081330" @default.
- W1994775352 hasPublicationYear "1986" @default.
- W1994775352 type Work @default.
- W1994775352 sameAs 1994775352 @default.
- W1994775352 citedByCount "29" @default.
- W1994775352 countsByYear W19947753522015 @default.
- W1994775352 countsByYear W19947753522017 @default.
- W1994775352 countsByYear W19947753522019 @default.
- W1994775352 countsByYear W19947753522021 @default.
- W1994775352 crossrefType "journal-article" @default.
- W1994775352 hasAuthorship W1994775352A5007121924 @default.
- W1994775352 hasAuthorship W1994775352A5038183050 @default.
- W1994775352 hasAuthorship W1994775352A5073334494 @default.
- W1994775352 hasConcept C101660505 @default.
- W1994775352 hasConcept C108625454 @default.
- W1994775352 hasConcept C116084860 @default.
- W1994775352 hasConcept C134018914 @default.
- W1994775352 hasConcept C139447449 @default.
- W1994775352 hasConcept C153911025 @default.
- W1994775352 hasConcept C158617107 @default.
- W1994775352 hasConcept C181199279 @default.
- W1994775352 hasConcept C185592680 @default.
- W1994775352 hasConcept C2775887612 @default.
- W1994775352 hasConcept C2777239931 @default.
- W1994775352 hasConcept C2777313579 @default.
- W1994775352 hasConcept C2777575526 @default.
- W1994775352 hasConcept C2778125326 @default.
- W1994775352 hasConcept C2778288131 @default.
- W1994775352 hasConcept C55493867 @default.
- W1994775352 hasConcept C71315377 @default.
- W1994775352 hasConcept C79879829 @default.
- W1994775352 hasConcept C81358767 @default.
- W1994775352 hasConcept C86803240 @default.
- W1994775352 hasConceptScore W1994775352C101660505 @default.
- W1994775352 hasConceptScore W1994775352C108625454 @default.
- W1994775352 hasConceptScore W1994775352C116084860 @default.
- W1994775352 hasConceptScore W1994775352C134018914 @default.
- W1994775352 hasConceptScore W1994775352C139447449 @default.
- W1994775352 hasConceptScore W1994775352C153911025 @default.
- W1994775352 hasConceptScore W1994775352C158617107 @default.
- W1994775352 hasConceptScore W1994775352C181199279 @default.
- W1994775352 hasConceptScore W1994775352C185592680 @default.
- W1994775352 hasConceptScore W1994775352C2775887612 @default.
- W1994775352 hasConceptScore W1994775352C2777239931 @default.
- W1994775352 hasConceptScore W1994775352C2777313579 @default.
- W1994775352 hasConceptScore W1994775352C2777575526 @default.
- W1994775352 hasConceptScore W1994775352C2778125326 @default.
- W1994775352 hasConceptScore W1994775352C2778288131 @default.
- W1994775352 hasConceptScore W1994775352C55493867 @default.
- W1994775352 hasConceptScore W1994775352C71315377 @default.
- W1994775352 hasConceptScore W1994775352C79879829 @default.
- W1994775352 hasConceptScore W1994775352C81358767 @default.
- W1994775352 hasConceptScore W1994775352C86803240 @default.
- W1994775352 hasLocation W19947753521 @default.
- W1994775352 hasLocation W19947753522 @default.
- W1994775352 hasOpenAccess W1994775352 @default.
- W1994775352 hasPrimaryLocation W19947753521 @default.
- W1994775352 hasRelatedWork W1592459539 @default.
- W1994775352 hasRelatedWork W1965252847 @default.
- W1994775352 hasRelatedWork W1972585736 @default.
- W1994775352 hasRelatedWork W1982693670 @default.
- W1994775352 hasRelatedWork W1986167530 @default.
- W1994775352 hasRelatedWork W1986997442 @default.
- W1994775352 hasRelatedWork W1994775352 @default.
- W1994775352 hasRelatedWork W2019783927 @default.
- W1994775352 hasRelatedWork W2054144997 @default.
- W1994775352 hasRelatedWork W2132171871 @default.
- W1994775352 isParatext "false" @default.
- W1994775352 isRetracted "false" @default.
- W1994775352 magId "1994775352" @default.