ELECTRONIC LETTER

Selective disruption of muscle and brain-specific BPAG1 isoforms in a girl with a 6;15 translocation, cognitive and motor delay, and tracheo-oesophageal atresia

R Giorda¹, A Cerritello², M C Bonaglia¹, S Bova³, G Lanzi³, E Repetti⁴, S Giglio⁵, C Baschirotto¹, T Pramparo⁴, L Avolio², R Bragheri², P Maraschio⁴, O Zuffardi^2,4

¹ IRCCS Eugenio Medea, Bosisio Parini, Lecco, Italy
² IRCCS Policlinico San Matteo, Pavia, Italy
³ IRCCS Fondazione Casimiro Mondino, Pavia, Italy
⁴ Biologia Generale e Genetica Medica, Università di Pavia, Pavia, Italy
⁵ IRCCS Ospedale San Raffaele, Milan, Italy

Correspondence to:
Correspondence to:
R Giorda
IRCCS Eugenio Medea, Via Don Luigi Monza, 20-23842 Bosisio Parini, Lecco, Italy; rgiorda@bp.lnf.it Correspondence to:
O Zuffardi
Biologia Generale e Genetica Medica, Via Forlanini, 14-27100 Pavia, Italy; zuffardi@unipv.it

Received 25 August 2003

Accepted 6 September 2003

Keywords: BPAG1; dystonin; tracheo-oesophageal atresia; translocation breakpoint

Abbreviations: ABD, actin-binding domain; BP, bullous pemphigoid; CC, coiled-coil; DMEM, Dulbecco’s modified Eagle medium; EA, oesophageal atresia; EBV, Epstein-Barr virus; FBS, fetal bovine serum; FISH, fluorescent in situ hybridisation; FSHD, facioscapulohumeral muscular dystrophy; HAT, hypoxantine-aminopterin-thymidine; IF, intermediate filaments; IFBD, IF-binding domain; LCL, lymphoblastoid cell line; ODED, oculo-digito-oesophageal-duodenal; PA-JEB, junctional epidermolysis bullosa with pyloric atresia; PBL, peripheral blood lymphocytes; RPMI medium, Roswell Park Memorial Institute medium

The first 150 words of the full text of this article appear below.

The protein BPAG1 (MIM: 113810, 600088, http://www.ncbi.nlm.nih.gov/Omim/)/Dystonin is a 230 kDa hemidesmosomal protein belonging to the plakin family, originally identified as one of the major autoantigens of bullous pemphigoid (BP), an autoimmune subepidermal skin blistering disease.¹ Mutations in the Dystonin gene result in sensory neuron degeneration in the mutant mouse (dystonia muscolorum (dt/dt)).^2–4

The complex organisation of the gene has gradually emerged, initially with the discovery of neuronal isoforms with different NH2-terminal sequences,^3,5,6 and more recently with the demonstration of the existence of much longer brain- and muscle-specific isoforms with a complex COOH-terminal organisation.^7,8

Although a complete understanding of the variety of BPAG1 isoforms has not been reached yet, a general picture of the organisation of the gene is now available. The epithelial isoform (BPAG1e) is made of a coiled-coil (CC) rod domain flanked by an NH2-terminal head domain called the plakin domain,⁹ and by a COOH-terminal tail domain . . . [Full text of this article]

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