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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
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Image Search Results


Figure 1 TSHR structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.

Journal: Journal of Endocrinology

Article Title: Antibody-induced modulation of TSH receptor post-translational processing

doi: 10.1677/joe-07-0058

Figure Lengend Snippet: Figure 1 TSHR structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.

Article Snippet: 2C11 was a mouse IgG1 TSHR-mAb (Shepherd et al. 1999) purchased from Serotec (Raleigh, NC, USA).

Techniques: Membrane

Figure 2 Recognition of the TSHR cleaved region by sera from a hamster model of Graves’ disease. TSHR-Abs to the cleaved region in sera from a hamster model of GD as determined by TSHR peptide ELISAs. The numbers shown below each column indicate the initial AA of each synthetic peptide as described in the Materials and Methods section. Immunoreactivity (OD) was compared with peptide 382 and an irrelevant control mAb (data are mean of duplicate measurements). *P!0.05 and **P!0.01.

Journal: Journal of Endocrinology

Article Title: Antibody-induced modulation of TSH receptor post-translational processing

doi: 10.1677/joe-07-0058

Figure Lengend Snippet: Figure 2 Recognition of the TSHR cleaved region by sera from a hamster model of Graves’ disease. TSHR-Abs to the cleaved region in sera from a hamster model of GD as determined by TSHR peptide ELISAs. The numbers shown below each column indicate the initial AA of each synthetic peptide as described in the Materials and Methods section. Immunoreactivity (OD) was compared with peptide 382 and an irrelevant control mAb (data are mean of duplicate measurements). *P!0.05 and **P!0.01.

Article Snippet: 2C11 was a mouse IgG1 TSHR-mAb (Shepherd et al. 1999) purchased from Serotec (Raleigh, NC, USA).

Techniques: Control

Figure 7 TSHR expression by immunoblot. Membranes prepared from TSH- and antibody-treated cells were resolved on 10% SDS-PAGE and blotted on to PVDF. The membrane was probed with an amino terminal TSHR-mAb (A10; Morgenthaler et al. 1997) at 1:5000 dilution. (A) Lane 1, untreated cells; lane 2, treated with TAb-8 antibody (2 mg/ml) for 24 h; and lane 3, treated with TSH (1000 mU/ml) for 24 h. *P!0.01. (B) Densitometric representation of the TSH holoreceptor bands indicated in (A).

Journal: Journal of Endocrinology

Article Title: Antibody-induced modulation of TSH receptor post-translational processing

doi: 10.1677/joe-07-0058

Figure Lengend Snippet: Figure 7 TSHR expression by immunoblot. Membranes prepared from TSH- and antibody-treated cells were resolved on 10% SDS-PAGE and blotted on to PVDF. The membrane was probed with an amino terminal TSHR-mAb (A10; Morgenthaler et al. 1997) at 1:5000 dilution. (A) Lane 1, untreated cells; lane 2, treated with TAb-8 antibody (2 mg/ml) for 24 h; and lane 3, treated with TSH (1000 mU/ml) for 24 h. *P!0.01. (B) Densitometric representation of the TSH holoreceptor bands indicated in (A).

Article Snippet: 2C11 was a mouse IgG1 TSHR-mAb (Shepherd et al. 1999) purchased from Serotec (Raleigh, NC, USA).

Techniques: Expressing, Western Blot, SDS Page, Membrane