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001-es BibID:	BIBFORM041173
Első szerző:	Burch, Henry B.
Cím:	Nucleotide and amino acid homology between the human thyrotropin receptor and the HIV-1 nef protein: Identification and functional analysis / Burch Henry B., Nagy Endre V., Lukes Yvonne G., Wartofsky Leonard, Burman Kenneth D.
Dátum:	1991
ISSN:	0006-291X
Megjegyzések:	A comparison of the nucleotide sequence of the human thyrotropin receptor (hTSH-R) with that of HIV-1 revealed 61% homology between a 161 base pair region encoding a unique portion of the hTSH-R and an immunogenic HIV-1 regulatory protein, nef. Amino acid analysis of this region shows 27% homology, including a segment in which 7/10 consecutive amino acids are identical. Sera from rabbits successfully immunized with a 16 amino acid portion of the hTSH-R (352-367, p1) was assessed for reactivity against a partially homologous nef peptide (nef-1) by ELISA, with a finding five-fold higher post-immunization values compared to pre-immune sera. The specificity of this response was verified with Western blot, using recombinant nef protein. An ELISA using nef-1 gave 64% higher values with sera from Graves' disease patients than with normal controls. This homology and immunologic cross-reactivity suggests an avenue through which a shared immune response against an HIV-1 related retrovirus could play a role in the pathogenesis of Graves' disease.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochemical And Biophysical Research Communications. - 181 : 1 (1991), p. 498-505. -
További szerzők:	Nagy Endre V. (1957-) (belgyógyász, endokrinológus) Lukes, Yvonne G. 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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001-es BibID:	BIBFORM041174
Első szerző:	Nagy Endre V. (belgyógyász, endokrinológus)
Cím:	Graves' IgG recognizes linear epitopes in the human thyrotropin receptor / Nagy Endre V., Burch Henry B., Mahoney Karen, Lukes Yvonne G., Morris John C., Burman Kenneth D.
Dátum:	1992
ISSN:	0006-291X
Megjegyzések:	Twenty-nine peptides covering the full extracellular domain of the human thyrotropin receptor have been synthesized and tested for reactivity with Graves' patients' and normal sera in ELISA. Two peptides, amino acids 331-350 and the second extracellular loop of the transmembrane segment, bound IgG-s from 5 and 4 of 10 Graves' disease patients' sera, respectively. Neither of these two peptides showed enhanced binding to normal IgG. There were no apparent differences between the Graves' disease and normal group with respect to the other 27 peptides. We conclude that peptide 331-350 and the second extracellular loop carry important linear epitopes which may contribute to the disease process in selected Graves' patients.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochemical And Biophysical Research Communications. - 188 : 1 (1992), p. 28-33. -
További szerzők:	Burch, Henry B. Mahoney, Karen Lukes, Yvonne G. Morris, John C. Burman, Kenneth D.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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