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Titolo:
Epiplakin, a novel member of the plakin family originally identified as a 450-kDa human epidermal autoantigen - Structure and tissue localization
Autore:
Fujiwara, S; Takeo, N; Otani, Y; Parry, DAD; Kunimatsu, M; Lu, R; Sasaki, M; Matsuo, N; Khaleduzzaman, M; Yoshioka, H;
Indirizzi:
Oita Med Univ, Dept Dermatol, Oita 8795593, Japan Oita Med Univ Oita Japan 8795593 niv, Dept Dermatol, Oita 8795593, Japan Nagoya City Univ, Sch Med, Dept Biochem, Mizuho Ku, Nagoya, Aichi 4678601,Japan Nagoya City Univ Nagoya Aichi Japan 4678601 , Nagoya, Aichi 4678601,Japan Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand Massey Univ Palmerston North New Zealand Palmerston North, New Zealand
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 16, volume: 276, anno: 2001,
pagine: 13340 - 13347
SICI:
0021-9258(20010420)276:16<13340:EANMOT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
BULLOUS PEMPHIGOID ANTIGEN; AMINO-ACID-SEQUENCES; PARANEOPLASTIC PEMPHIGUS; INTERMEDIATE FILAMENTS; EPIDERMOLYSIS-BULLOSA; HUMAN AUTOANTIBODIES; MUSCULAR-DYSTROPHY; DESMOPLAKIN-I; CDNA CLONING; COILED-COIL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Fujiwara, S Oita Med Univ, Dept Dermatol, Oita 8795593, Japan Oita Med Univ Oita Japan 8795593 rmatol, Oita 8795593, Japan
Citazione:
S. Fujiwara et al., "Epiplakin, a novel member of the plakin family originally identified as a 450-kDa human epidermal autoantigen - Structure and tissue localization", J BIOL CHEM, 276(16), 2001, pp. 13340-13347

Abstract

A 450-kDa human epidermal autoantigen was originally identified as a protein that reacted with the serum from an individual with a subepidermal blistering disease. Molecular cloning of this protein has now shown that it contains 5065 amino acids and has a molecular mass of 552 kDa. As reported previously this protein, which we call epiplakin, belongs to the plakin family,but it has some very unusual features. Epiplakin has 13 domains that are homologous to the B domain in the COOH-terminal region of desmoplakin. The last five of these B domains, together with their associated linker regions,are particularly strongly conserved. However, epiplakin lacks a coiled-coil rod domain and an amino-terminal domain, both of which are found in all other known members of the plakin family. Furthermore, no dimerization motifwas found in the sequence. Thus, it is likely that epiplakin exists in vivo as a single-chain structure. Epitope mapping experiments showed that the original patient's serum recognized a sequence unique to epiplakin, which was not found in plectin. Immunofluorescence staining revealed the presence of epiplakin in whole sheets: of epidermis and esophagus, in glandular cells of eccrine sweat and parotid glands and in mucous epithelial cells in thestomach and colon.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 22:28:05