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Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo. (Articolo in rivista)

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Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo. (Articolo in rivista) (literal)

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Cipollini E, Riccio M, Di Giaimo R, Dal Piaz F, Pulice G, Catania S, Caldarelli I, Dembic M, Santi S, Melli M. (2008)
Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo.
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Cipollini E, Riccio M, Di Giaimo R, Dal Piaz F, Pulice G, Catania S, Caldarelli I, Dembic M, Santi S, Melli M. (literal)

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Department of Biology, University of Bologna, Via Selmi 3, 40126 Bologna, Italy; Department of Anatomy and Histology, University of Modena and Reggio Emilia, Largo Del Pozzo 71, 41100 Modena, Italy; Department of Biological Sciences, Federico II University, Via Mezzocannone 8, 80134, Naples, Italy; Department of Farmaceutical Sciences, University of Salerno, Via Ponte Don Melillo, 84084 Fisciano (SA), Italy; Institute of Organ Transplantation and Immunocitology-ITOI, C.N.R c/o I.O.R., 40136 Bologna, Italy. (literal)

Titolo

Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo. (literal)

Abstract

Progressive myoclonus epilepsy type 1 (EPM1) is a neurodegenerative disease correlating with mutations of the cystatin B gene. Cystatin B is described as a monomeric protein with antiprotease function. This work shows that, in vivo, cystatin B has a polymeric structure, highly resistant to SDS, urea, boiling and sensitive to reducing agents and alkaline pH. Hydrogen peroxide increases the polymeric structure of the protein. Mass spectrometry analysis shows that the only component of the polymers is cystatin B. EPM1 mutants of cystatin B transfected in cultured cells are also polymeric. The banding pattern generated by a cysteine-minus mutant is different from that of the wild-type protein as it contains only monomers, dimers and some very high MW bands while misses components of MW intermediate between 25 and 250 kDa. Overexpression of wild-type or EPM1 mutants of cystatin B in neuroblastoma cells generates cytoplasmic aggregates. The cysteine-minus mutant is less prone to the formation of inclusion bodies. We conclude that cystatin B in vivo has a polymeric structure sensitive to the redox environment and that overexpression of the protein generates aggregates. This work describes a protein with a physiological role characterized by highly stable polymers prone to aggregate formation in vivo. (literal)

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