Characterization of the human thyroid microsomal antigen involved in thyroid autoimmunity

1984 ◽  
Vol 12 (6) ◽  
pp. 1118-1119 ◽  
Author(s):  
J. PAUL BANGA ◽  
GARETH PRYCE ◽  
LINDA HAMMOND ◽  
IVAN M. ROITT
Keyword(s):  
Thyroid Autoimmunity ◽  
Human Thyroid ◽  
Thyroid Microsomal Antigen ◽  
Microsomal Antigen

Cellular localization of the microsomal antigen and the thyroid peroxidase antigen

1987 ◽  
Vol 116 (1_Suppl) ◽  
pp. S57-S62 ◽  
Author(s):  
A. Pinchera ◽  
S. Mariotti ◽  
L. Chiovato ◽  
P. Vitti ◽  
G. Lopez ◽  
...  
Keyword(s):  
Cellular Localization ◽  
Biochemical Characterization ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Immunofluorescence Analysis ◽  
Thyroid Cells ◽  
Hla Dr ◽  
Microsomal Antigen ◽  
Dependent Mechanism

Abstract. Evidence has been accumulated that human thyroid microsomal/microvillar autoantigen (M) is expressed both in the cytoplasm and on the surface of thyroid follicular cells. The availability of this autoantigen to the immune system, possibly associated with abnormally expressed HLA-DR antigens may be relevant both to the triggering and to maintenance of thyroid autoimmune reactions. Preliminary biochemical characterization of M suggested that it was a glycoprotein with a mol. wt. of about 100–110 kD. recent studies carried out in our laboratories taking advantage of monoclonal antibodies provided evidence that the structure presently referred as M-Ag is represented by thyroid peroxidase (TPO). The identity between TPO and M is further supported by four-layer immunofluorescence analysis showing a complete overlap of the two antigens both in the surface and in the cytoplasm of thyroid cells and by the observation that the expression of M and TPO is similarly modulated by TSH, possibly through a cAMP-dependent mechanism.

Solubilization of Human Thyroid Microsomal Antigen*

1979 ◽  
Vol 48 (2) ◽  
pp. 207-212 ◽  
Author(s):  
S. MARIOTTI ◽  
A. PINCHERA ◽  
C. MARCOCCI ◽  
P. VITTI ◽  
C. URBANO ◽  
...  
Keyword(s):  
Human Thyroid ◽  
Thyroid Microsomal Antigen ◽  
Microsomal Antigen

The SCID-hu mouse and thyroid autoimmunity: Characterization of human thyroid autoantibody secretion

1991 ◽  
Vol 60 (2) ◽  
pp. 319-330 ◽  
Author(s):  
T.F. Davies ◽  
H. Kimura ◽  
P. Fong ◽  
D. Kendler ◽  
L.D. Shultz ◽  
...  
Keyword(s):  
Thyroid Autoimmunity ◽  
Human Thyroid ◽  
Thyroid Autoantibody

Further Characterization of the Thyroid Microsomal Antigen by Monoclonal Antibodies

1987 ◽  
pp. 279-281 ◽  
Author(s):  
Luc Portmann ◽  
Noboru Hamada ◽  
Wilfred A. Franklin ◽  
Leslie J. DeGroot
Keyword(s):  
Monoclonal Antibodies ◽  
Thyroid Microsomal Antigen ◽  
Microsomal Antigen

scholarly journals Characterization of the thyroid microsomal antigen, and its relationship to thyroid peroxidase, using monoclonal antibodies.

1988 ◽  
Vol 81 (4) ◽  
pp. 1217-1224 ◽  
Author(s):  
L Portmann ◽  
F W Fitch ◽  
W Havran ◽  
N Hamada ◽  
W A Franklin ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Thyroid Peroxidase ◽  
Thyroid Microsomal Antigen ◽  
Microsomal Antigen

Development of thyroid autoimmunity

1985 ◽  
Vol 108 (1) ◽  
pp. 61-64 ◽  
Author(s):  
K. Aho ◽  
A. Gordin ◽  
T. Palosuo ◽  
J. Takala
Keyword(s):  
Epidemiological Study ◽  
Rural Population ◽  
Thyroid Autoimmunity ◽  
Blood Samples ◽  
Thyroid Microsomal Antigen ◽  
Age Range ◽  
Microsomal Antigen

Abstract. Two blood samples were taken at an interval of 5 years in a continuing epidemiological study of a rural population in south-western Finland with an age range of 40–64 years at commencement. Paired sera of 680 subjects were tested for antibodies against thyroglobulin and thyroid microsomal antigen. In the seroconversion cases the titres in the second specimens were either low or medium but never high. In the cases selected on the basis of the highest titres in the follow-up specimens, the titres in the baseline specimens were either high or medium but never low. These findings suggest that the emergence and the development of thyroid autoimmune seroreactions are slow processes.

Thyroid peroxidase is the organ-specific 'microsomal' autoantigen involved in thyroid autoimmunity

1987 ◽  
Vol 116 (1_Suppl) ◽  
pp. S49-S56 ◽  
Author(s):  
Jean Ruf ◽  
Barbara Czarnocka ◽  
Catherine De Micco ◽  
Catherine Dutoit ◽  
Mireille Ferrand ◽  
...  
Keyword(s):  
Plasma Membranes ◽  
Specific Activity ◽  
Thyroid Autoimmunity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Thyroid Tissue ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Dependent Manner ◽  
Autoimmune Thyroid Diseases ◽  
Microsomal Antigen

Abstract. Autoantibodies (aAb) in serum of patients with autoimmune thyroid diseases (AITD) are directed to an antigen associated with thyroid microsomes. Although it has been investigated over almost three decades, the nature of this autoantigen remained unknown. Taking advantage of monoclonal antibodies (mAb) produced in our laboratory, we have demonstrated that thyroid peroxidase (TPO) is the 'microsomal' antigen. Sera of patients with AITD strongly inhibited the binding of only one of 19 mAb raised against human thyroid plasma membranes. This mAb did not react with thyroglobulin but achieved significant binding to preparations of human, bovine and porcine TPO, bovine lactoperoxidase and human myeloperoxidase without altering the enzyme activity. The mAb has been used to immunopurify the human TPO from solubilized thyroid microsomes. The procedure allowed high purification (∼ 3500-fold) of the native enzyme with a reasonable yield (∼ 10 mg TPO/kg thyroid tissue). Human TPO exhibited a specific activity of 350–400 guaiacol U/mg, a peak in the Soret region and a ratio of A411 nm to A280 nm of 0.20–0.25. Upon SDS-polyacrylamide gel electrophoresis, the purified enzyme gave two contiguous bands in the 100 kDa region. Performed in non-reducing conditions, electrophoresis of TPO showed one band in the same 100 kDa region. Sera with aAb to the microsomal antigen immunoprecipitated purified TPO to an extent ranging from 80 to 100% of the initial enzyme amount while sera from normal subjects or from patients with undectable level of anti-microsomal aAb elicit a decrease of less than 30% of the total TPO activity. IgG from sera of patients with AITD were also shown to bind to purified TPO and to inhibit, in a dose-dependent manner the mAb binding to TPO. Furthermore anti-microsomal aAb were specifically adsorbed onto TPO-sepharose column and eluted only with high ionic strength buffers. Taking into account that TPO shares almost all the characteristics attributed to the microsomal antigen and that anti-TPO and anti-microsomal aAb are undistinguishable, it can be concluded that TPO is the thyroid autoantigen termed to date the 'microsomal' antigen.

scholarly journals Cloning and Characterization of a cDNA That Encodes a 70-kDa Novel Human Thyroid Autoantigen

1989 ◽  
Vol 264 (7) ◽  
pp. 3651-3654
Author(s):  
J Y Chan ◽  
M I Lerman ◽  
B S Prabhakar ◽  
O Isozaki ◽  
P Santisteban ◽  
...  
Keyword(s):  
Human Thyroid
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