Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins
Bullous pemphigoid is a subepidermal blistering disease in which patients have autoantibodies against the plaque of the hemidesmosome. Starting with a previously isolated 2-kilobase (kb) cDNA for bullous pemphigoid antigen (BPA), we used primer extension of keratinocyte mRNA to isolate overlapping c...
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Published in | The Journal of biological chemistry Vol. 266; no. 19; pp. 12555 - 12559 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
05.07.1991
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Abstract | Bullous pemphigoid is a subepidermal blistering disease in which patients have autoantibodies against the plaque of the hemidesmosome.
Starting with a previously isolated 2-kilobase (kb) cDNA for bullous pemphigoid antigen (BPA), we used primer extension of
keratinocyte mRNA to isolate overlapping cDNAs with a combined open reading frame of 6.3 kb, encoding most (243 kDa) of the
BPA, but lacking the far amino terminus. Analysis of this amino acid sequence revealed a carboxyl-terminal domain containing
two regions of 174 and 176 residues with high sequence identity. Most of the amino-terminal two-thirds of BPA is predicted
to be in an alpha-helical conformation in which two chains would aggregate into a coiled-coil rod structure. BPA and desmoplakin
I, a desmosome plaque protein, show remarkable sequence and structural homology. In its carboxyl-terminal domain, desmoplakin
I also has 176 residue repeats with 40% sequence identity to those in BPA. The repeats in both molecules have a regular linear
distribution of acidic and basic residues with a period of 9.5, the same as that found in the 1B segment of keratin filaments,
suggesting a means of ionic interaction between keratin and these plaque proteins. Also, desmoplakin I, like BPA, is predicted
to have a rod domain, which in both proteins has similar regular charge periodicities, suggesting a means of ionic self-aggregation.
These findings extend those of Green et al. (Green, K. J., Parry, D. A. D., Steinert, P. S., Virata, L. A., Wagner, R. M.,
Angst, B. D., and Nilles, L. A. (1990) J. Biol. Chem. 265, 2603-2612) which show that BPA and desmoplakin I represent the
first members of a new family of adhesion junction plaque proteins. |
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AbstractList | Bullous pemphigoid is a subepidermal blistering disease in which patients have autoantibodies against the plaque of the hemidesmosome.
Starting with a previously isolated 2-kilobase (kb) cDNA for bullous pemphigoid antigen (BPA), we used primer extension of
keratinocyte mRNA to isolate overlapping cDNAs with a combined open reading frame of 6.3 kb, encoding most (243 kDa) of the
BPA, but lacking the far amino terminus. Analysis of this amino acid sequence revealed a carboxyl-terminal domain containing
two regions of 174 and 176 residues with high sequence identity. Most of the amino-terminal two-thirds of BPA is predicted
to be in an alpha-helical conformation in which two chains would aggregate into a coiled-coil rod structure. BPA and desmoplakin
I, a desmosome plaque protein, show remarkable sequence and structural homology. In its carboxyl-terminal domain, desmoplakin
I also has 176 residue repeats with 40% sequence identity to those in BPA. The repeats in both molecules have a regular linear
distribution of acidic and basic residues with a period of 9.5, the same as that found in the 1B segment of keratin filaments,
suggesting a means of ionic interaction between keratin and these plaque proteins. Also, desmoplakin I, like BPA, is predicted
to have a rod domain, which in both proteins has similar regular charge periodicities, suggesting a means of ionic self-aggregation.
These findings extend those of Green et al. (Green, K. J., Parry, D. A. D., Steinert, P. S., Virata, L. A., Wagner, R. M.,
Angst, B. D., and Nilles, L. A. (1990) J. Biol. Chem. 265, 2603-2612) which show that BPA and desmoplakin I represent the
first members of a new family of adhesion junction plaque proteins. Starting with a previously isolated 2-kilobase (kb) cDNA for bullous pemphigoid antigen (BPA), we used primer extension of keratinocyte mRNA to isolate overlapping cDNAs with a combined open reading frame of 6.3 kb, encoding most (243 kDa) of the BPA, but lacking the far amino terminus. Analysis of this amino acid sequence revealed a carboxyl-terminal domain containing two regions of 174 and 176 residues with high sequence identity. Most of the amino-terminal two-thirds of BPA is predicted to be in an alpha -helical conformation in which two chains would aggregate into a coiled-coil rod structure. BPA and desmoplakin I, a desmosome plaque protein, show remarkable sequence and structural homology. In its carboxyl-terminal domain, desmoplakin I also has 176 residue repeats with 40% sequence identity to those in BPA. Bullous pemphigoid is a subepidermal blistering disease in which patients have autoantibodies against the plaque of the hemidesmosome. Starting with a previously isolated 2-kilobase (kb) cDNA for bullous pemphigoid antigen (BPA), we used primer extension of keratinocyte mRNA to isolate overlapping cDNAs with a combined open reading frame of 6.3 kb, encoding most (243 kDa) of the BPA, but lacking the far amino terminus. Analysis of this amino acid sequence revealed a carboxyl-terminal domain containing two regions of 174 and 176 residues with high sequence identity. Most of the amino-terminal two-thirds of BPA is predicted to be in an alpha-helical conformation in which two chains would aggregate into a coiled-coil rod structure. BPA and desmoplakin I, a desmosome plaque protein, show remarkable sequence and structural homology. In its carboxyl-terminal domain, desmoplakin I also has 176 residue repeats with 40% sequence identity to those in BPA. The repeats in both molecules have a regular linear distribution of acidic and basic residues with a period of 9.5, the same as that found in the 1B segment of keratin filaments, suggesting a means of ionic interaction between keratin and these plaque proteins. Also, desmoplakin I, like BPA, is predicted to have a rod domain, which in both proteins has similar regular charge periodicities, suggesting a means of ionic self-aggregation. These findings extend those of Green et al. (Green, K. J., Parry, D. A. D., Steinert, P. S., Virata, L. A., Wagner, R. M., Angst, B. D., and Nilles, L. A. (1990) J. Biol. Chem. 265, 2603-2612) which show that BPA and desmoplakin I represent the first members of a new family of adhesion junction plaque proteins. |
Author | T Tanaka J R Stanley D A Parry V Klaus-Kovtun P M Steinert |
Author_xml | – sequence: 1 givenname: T surname: TANAKA fullname: TANAKA, T organization: NIH, national inst. arthritis musculoskeletal skin diseases, dermatology branch, Bethesda MD 20892, United States – sequence: 2 givenname: D. A. D surname: PARRY fullname: PARRY, D. A. D organization: NIH, national inst. arthritis musculoskeletal skin diseases, dermatology branch, Bethesda MD 20892, United States – sequence: 3 givenname: V surname: KLAUS-KOVTUN fullname: KLAUS-KOVTUN, V organization: NIH, national inst. arthritis musculoskeletal skin diseases, dermatology branch, Bethesda MD 20892, United States – sequence: 4 givenname: P. M surname: STEINERT fullname: STEINERT, P. M organization: NIH, national inst. arthritis musculoskeletal skin diseases, dermatology branch, Bethesda MD 20892, United States – sequence: 5 givenname: J. R surname: STANLEY fullname: STANLEY, J. R organization: NIH, national inst. arthritis musculoskeletal skin diseases, dermatology branch, Bethesda MD 20892, United States |
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Keywords | Bullous dermatosis Antigen Human Proteins Immunopathology Skin disease Bullous pemphigoid Autoimmune disease Homology Primary structure Desmosome Molecular cloning |
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Snippet | Bullous pemphigoid is a subepidermal blistering disease in which patients have autoantibodies against the plaque of the hemidesmosome.
Starting with a... Bullous pemphigoid is a subepidermal blistering disease in which patients have autoantibodies against the plaque of the hemidesmosome. Starting with a... Starting with a previously isolated 2-kilobase (kb) cDNA for bullous pemphigoid antigen (BPA), we used primer extension of keratinocyte mRNA to isolate... |
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SubjectTerms | Amino Acid Sequence Autoantigens - genetics autoimmune diseases Biological and medical sciences Blotting, Northern Bullous diseases of the skin Carrier Proteins Cell Adhesion - genetics Cloning, Molecular Collagen Collagen Type XVII Cytoskeletal Proteins - immunology Dermatology desmoplakin I Desmoplakins Desmosomes - immunology DNA - genetics Dystonin Humans Medical sciences Molecular Sequence Data Nerve Tissue Proteins Non-Fibrillar Collagens Nucleic Acid Hybridization Open Reading Frames pemphigoid Pemphigoid, Bullous - immunology RNA - analysis Sequence Homology, Nucleic Acid skin diseases |
Title | Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins |
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