| Reassessment of the location of the thyrotropin receptor 50 amino acid "insertion" provides evidence in favor of a second downstream cleavage site. | |
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MedLine Citation:
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PMID: 11288979 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cleavage of thyrotropin receptors (TSHR) on the cell surface into disulfide-linked A and B subunits involves deletion of an intervening region that corresponds approximately to a 50 amino acid "insertion" in the TSHR relative to the noncleaving luteinizing hormone/choriogonadotropin receptor (LH/CGR). The location of this insertion is imprecise because of the relatively low homology between the two receptors in this region. We tested the hypothesis that the TSHR 50 amino acid insertion was further downstream than we previously concluded, a possibility that would relocate the crucial LH/CGR glycan at N291 relative to the position of the TSHR insertion, and that would mitigate against the 50 amino acid insertion playing a role in TSHR intramolecular cleavage. Thus, we transferred the LH/CGR glycan at amino acid 291 from downstream (N367) to upstream of the 50 amino acid insertion (N317) in the TSHR, leaving this insertion intact. TSHR cleavage persisted. Moreover, deletion of amino acid residues 320-366 in addition to the upstream N291 substitution (ALN317-319NET) also did not prevent cleavage. On the other hand, deletion of three contiguous downstream residues (GQE367-369) in the TSHR 50 amino acid insertion abolished receptor cleavage into subunits. In summary, the present data are consistent with our previous location of the TSHR 50 amino acid insertion and, therefore, do not undermine evidence for the involvement of this insertion in TSHR cleavage. In addition, the data regarding TSHR residues GQE367-369 (far downstream of cleavage site 1) support the controversial possibility of a secondary cleavage site downstream of the insertion. |
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Authors:
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K Tanaka; G D Chazenbalk; B Rapoport; S M McLachlan |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Thyroid : official journal of the American Thyroid Association Volume: 11 ISSN: 1050-7256 ISO Abbreviation: Thyroid Publication Date: 2001 Feb |
Date Detail:
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Created Date: 2001-04-05 Completed Date: 2001-07-19 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 9104317 Medline TA: Thyroid Country: United States |
Other Details:
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Languages: eng Pagination: 111-4 Citation Subset: IM |
Affiliation:
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Autoimmune Disease Unit, Cedars-Sinai Research Institute and School of Medicine, University of California, Los Angeles, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence
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genetics Animals CHO Cells Cricetinae Cross-Linking Reagents / pharmacology DNA Transposable Elements* Gene Deletion Molecular Sequence Data Mutation / genetics Receptors, Thyrotropin / genetics* |
| Grant Support | |
ID/Acronym/Agency:
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DK19289/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cross-Linking Reagents; 0/DNA Transposable Elements; 0/Receptors, Thyrotropin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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