Di Giaimo Rossella, Riccio Massimo, Santi Spartaco, Galeotti Cesira, Ambrosetti Davide C, Melli Marialuisa
Department of Biology, Bologna University, 40126 Bologna, Italy.
Hum Mol Genet. 2002 Nov 1;11(23):2941-50. doi: 10.1093/hmg/11.23.2941.
Cystatin B is an anti-proteolytic polypeptide implicated in progressive myoclonus epilepsy (EPM1), a degenerative disease of the central nervous system. The knock-out mouse model of the disease shows apoptosis of the cerebellar granule cells. We have identified five recombinant proteins interacting with cystatin B and none of them is a protease. We show that three of these proteins (RACK-1, beta-spectrin and NF-L) co-immunoprecipitate with cystatin B in rat cerebellum. Confocal immunofluorescence analysis shows that the same proteins are present in the granule cells of developing cerebellum, as well as in Purkinje cells of adult rat cerebellum. We propose that a cystatin B multiprotein complex has a specific cerebellar function and that the loss of this function might contribute to the disease in EPM1 patients.