Differential Reactivities of Recombinant Glycosylated Ectodomains of Mouse and Human Thyrotropin Receptors with Patient Autoantibodies1

Autor:	Gattadahalli S. Seetharamaiah, Robert L. Peake, John S. Dallas, N. Rao Thotakura, Bellur S. Prabhakar, Sai A. Patibandla
Rok vydání:	1997
Předmět:	medicine.medical_specialty medicine.drug_class Autoantibody Biology Monoclonal antibody Molecular biology Immunoglobulin G Thyrotropin receptor law.invention Endocrinology law Internal medicine medicine biology.protein Extracellular Recombinant DNA Antibody Receptor
Zdroj:	Endocrinology. 138:1559-1566
ISSN:	1945-7170 0013-7227
DOI:	10.1210/endo.138.4.5093
Popis:	We expressed the extracellular domain of the mouse TSH receptor (mET-gp) using the baculovirus expression system. The recombinant protein was identified as mET-gp by immunoblotting and N-terminal amino acid sequencing. Carbohydrate analysis of the recombinant protein showed that the protein is glycosylated. Experimental antibodies raised against the extracellular domain of the human TSHr (ETSHr) were assayed for reactivity against mET-gp and glycosylated human ETSHr (ETSHr-gp) in an ELISA and found to be comparable. Similarly, both mET-gp and ETSHr-gp proteins neutralized the TSH binding inhibitory immunoglobulin (TBII) activity of rabbit anti-ETSHr antibodies in a RRA. However, when these proteins were compared for their ability to neutralize TBII and blocking activities (TSBAb) of IgG from patients with thyroid autoimmune disorders, only ETSHr-gp was able to neutralize these activities. In contrast, mET-gp partially neutralized, whereas ETSHr-gp completely neutralized the stimulatory (TSAb) activities o...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8efa417c90bf7ca4c35aad3e4c203719 https://doi.org/10.1210/endo.138.4.5093 Zobrazit plný text záznamu