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001-es BibID:	BIBFORM041176
Első szerző:	Burch, Henry B.
Cím:	Expression polymerase chain reaction for the in vitro synthesis and epitope mapping of autoantigen application to the human thyrotropin receptor / Burch Henry B., Nagy Endre V., Kain Kevin C., Lanar David E., Carr Frances E., Wartofsky Leonard, Burman Kenneth D.
Dátum:	1993
ISSN:	0022-1759
Megjegyzések:	The clinical applicability of a newly described polymerase chain reaction directed protein expression system was assessed for the in vitro synthesis and partial epitope mapping of large radiolabeled human thyrotropin receptor (hTSH-R) protein segments. PCR amplification of targeted regions within the hTSH-R cDNA followed by in vitro transcription and translation permitted rapid synthesis of protein segments ranging in size from 18 to 62 kDa. Initial epitope mapping was directed at a 52 amino acid segment unique to the hTSH-R compared to otherwise homologous glycoprotein hormone receptors. Sera from Graves' disease patients known to have autoantibodies against the hTSH-R were used to immunoprecipitate two protein fragments differing only by the presence of the unique region in the larger fragment (E5) but not in the smaller fragment (E4). Dense precipitation bands were obtained using Graves' sera to immunoprecipitate E5 whereas little or no specific immunoprecipitation of E4 occurred. Normal sera gave only weak immunoprecipitation bands of E5. The technique provides significant advantages over conventional cloning methods and should have general applicability in the study of other protein targets of autoimmune disease.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal Of Immunological Methods. - 158 : 1 (1993), p. 123-130. -
További szerzők:	Nagy Endre V. (1957-) (belgyógyász, endokrinológus) Kain, Kevin C. Lanar, David E. Carr, Frances E. Wartofsky, Leonard Burman, Kenneth D.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM041178
Első szerző:	Mengistu, M.
Cím:	TSH receptor gene expression in retroocular fibroblasts / Mengistu, M., Lukes, Y. G., Nagy, V. E., Burch, H. B., Carr, F. E., Lahiri, S., Burman, K. D.
Dátum:	1994
ISSN:	0391-4097
Megjegyzések:	RNA was isolated from fibroblasts from the retroocular area, from endomysial fibroblasts obtained from orbital lateral rectus muscle, and from abdominal skin fibroblasts. The RNA was reverse transcribed into cDNA which was then used as a template for PCR with primers encompassing a portion (nucleotides 989-1235) of the extra-cellular domain of the human TSH receptor (hTSH-R). A definite 247 BP product was detected from fibroblast RNA by ethidium bromide staining, and was confirmed by hybridization with labelled hTSH-R cDNA. The product had homology with the known TSH-R cDNA. These studies indicate that human fibroblasts can express hTSH-R, and they suggest that a cross reactive immunologic response between anti-hTSH-R and these fibroblast TSH receptors may play a role in the genesis of Graves' ophthalmopathy.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal Of Endocrinological Investigation. - 17 : 6 (1994), p. 437-441. -
További szerzők:	Lukes, Yvonne G. Nagy Endre V. (1957-) (belgyógyász, endokrinológus) Burch, Henry B. Carr, Frances E. Lahiri, Susanta Burman, Kenneth D.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM041290
035-os BibID:	PMID:7901266
Első szerző:	Nagy Endre V. (belgyógyász, endokrinológus)
Cím:	Immunogenicity of a unique region of the human thyrotropin receptor / E. V. Nagy, H. B. Burch, Y. G. Lukes, F. E. Carr, S. Kosugi, L. D. Kohn, K. D. Burman
Dátum:	1993
ISSN:	0391-4097
Megjegyzések:	Clarifying the role of the TSH receptor protein in the autoimmune process may be the key to understanding the development of Graves' disease. In the present study we used a 16 amino acid peptide of the human TSH receptor (hTSHR) to immunize rabbits. A comparable, but theoretically less immunogenic, peptide was injected into other rabbits. The antibody response against these and other peptides, as well as against solubilized human thyroid membrane (TM) and guinea pig fat cell membrane (GPF) proteins, was tested using ELISA and Western blots. The GPF and TM binding pattern of rabbits' sera was compared to that of Graves' patients' sera. We have identified an area of antigenic cross-reactivity between GPF and TM; a 63 kD protein was present in both GPF and TM, and this protein uniformly bound IgG-s of the rabbits' postimmunization sera and one of eight Graves' patient's serum. We have shown that i) a theoretically immunogenic 16 amino acid peptide was indeed highly immunogenic in rabbits, ii) antibodies binding to GPF and TM were detected after immunization, and iii) the peak of thyroid stimulating immunoglobulin activity of sera was followed by a transient elevation of serum triiodothyronine levels. Further studies investigating the immunogenic epitopes of the hTSHR as well as characterizing the 63 kD protein are indicated.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Journal of Endocrinological Investigation. - 16 : 7 (1993), p. 485-493. -
További szerzők:	Burch, Henry B. Lukes, Yvonne G. Carr, Frances E. Kosugi, S. Kohn, L. D. Burman, Kenneth D.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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