Upregulation of Heat-Shock Protein (hsp)-27 in a Patient with Heterozygous SPG11 c.1951C>T and SYNJ1 c.2614G>T Mutations Causing Clinical Spastic Paraplegia

We report a 49-year-old patient suffering from spastic paraplegia with novel heterozygous mutation and analyzed the levels of heat shock proteins (hsp)-27, dopamine (DA), its metabolites in their cerebrospinal fluid (CSF). The hsp27 protein concentration patient’s CSF was assayed by an ELISA kit, while DA CSF, 3,4-dihydroxyphenylacetic acid (DOPAC), Cys-DA, Cys-DOPA were measured HPLC. Whole exome sequencing demonstrated SPG-11 c.1951C>T SYNJ1 c.2614G>T mutations, both recessive. DOPAC significantly decreased (53.0 ± 6.92 473.3 72.19, p < 0.05, respectively) no differences found Cys-DA. Nonetheless, Cys-DA/DOPAC ratio (0.213 0.024, 0.05) (1073.0 136.4, higher. To best our knowledge, has not been previously reported. Our does produce fully functional spatacsin synaptojanin-1 proteins. In this line, results showed indicating loss DAergic neurons. Many factors have described as being responsible for increased cys-DA/DOPAC ratio, such MAO inhibition antioxidant activity neurons which would increase catecholquinones consequently cysteinyl-catechols. conclusion, haploinsufficiency might be underlying cause neurodegeneration produced trafficking defects, vesicle trafficking/recycling processes, autophagy dysfunction, cell death leading to upregulation cellular mechanism protection and/or balance impaired trafficking.