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Article

Cleavage of the thyrotropin receptor does not occur at a classical subtilisin-related proprotein convertase endoproteolytic site.

The Journal of biological chemistry - 23 Dec 1994

Chazenbalk G D, Rapoport B

Abstract excerpt

The human thyrotropin receptor (TSHR) undergoes proteolytic cleavage closely upstream to amino acid 317. Between residues 261 and 313 are three clusters of positively charged amino acids, arginines (Arg) and lysines (Lys), which are potential subtilisin-related proprotein convertase sites. We used oligonucleotide-directed mutagenesis to perform conservative amino acid substitutions within these regions (Arg or...

Topics

Amino Acid Sequence
Animals
Binding Sites
CHO Cells
Cricetinae
Humans
Hydrolysis
Molecular Sequence Data
Mutation
Receptors, Thyrotropin
Serine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Subtilisins

Source

Identifiers

PMID: 7798220

Genes

TSHR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7798220-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Cleavage of the thyrotropin receptor does not occur at a classical subtilisin-related proprotein convertase endoproteolytic site.PMID 7798220Read ↗

Evidence that cleavage of the thyrotropin receptor involves a "molecular ruler" mechanism: deletion of amino acid residues 305-320 causes a spatial shift in cleavage site 1 independent of amino acid motif.Semantic proximity Read ↗

Insight into thyrotropin receptor cleavage by engineering the single polypeptide chain luteinizing hormone receptor into a cleaving, two subunit receptor.Semantic proximity Read ↗

Reassessment of the location of the thyrotropin receptor 50 amino acid "insertion" provides evidence in favor of a second downstream cleavage site.Semantic proximity Read ↗

Thyrotropin receptor cleavage at site 1 involves two discontinuous segments at each end of the unique 50-amino acid insertion.Semantic proximity Read ↗

Site-Directed Mutagenesis of the Human Thyrotropin Receptor: Role of Asparagine-Linked Oligosaccharides in the Expression of a Functional ReceptorSemantic proximity Read ↗

On the functional importance of thyrotropin receptor intramolecular cleavage.Semantic proximity Read ↗

Structure-function relationships of two loss-of-function mutations of the thyrotropin receptor gene.Semantic proximity Read ↗

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An insertion in the human thyrotropin receptor critical for high affinity hormone binding.Semantic proximity Read ↗

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Site-directed mutagenesis of a portion of the extracellular domain of the rat thyrotropin receptor important in autoimmune thyroid disease and nonhomologous with gonadotropin receptors. Relationship of functional and immunogenic domains.Semantic proximity Read ↗

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