Inscriere cercetatori

Premii Ad Astra

premii Ad Astra

Asociația Ad Astra anunță lansarea proiectului Premiilor Ad Astra 2022 (link aici), care își propune identificarea și popularizarea modelelor de succes, a rezultatelor excepționale ale cercetătorilor români din țară și din afara ei. Regulamentul de participare se poate gasi aici, iar  pagina de inscriere se poate accesa aici.

Asociatia Ad Astra a cercetatorilor romani lanseaza BAZA DE DATE A CERCETATORILOR ROMANI DIN DIASPORA. Scopul acestei baze de date este aceea de a stimula colaborarea dintre cercetatorii romani de peste hotare dar si cu cercetatorii din Romania. Cercetatorii care doresc sa fie nominalizati in aceasta baza de date sunt rugati sa trimita un email la

Tyrosinase exacerbates dopamine and -synuclein toxicity but is not genetically associated with Parkinson’s disease

Domenii publicaţii > Biologie + Tipuri publicaţii > Articol în revistã ştiinţificã

Autori: Greggio, E., Bergantino, E., Carter, D., Ahmad, R., Costin G.-E., Hearing, V. J., Clarimon, J., Singleton, A., Eerola, J., Hellström, O., Tienari, P. J., Miller, D. W., Beilina, A., Bubacco, L., Cookson, M. R.

Editorial: J. Neurochem., 93, p.246-256, 2005.


Tyrosinase is a key enzyme in the synthesis of melanin in skin and hair and has also been proposed to contribute to the formation of neuromelanin (NM). The presence of NM, which is biochemically similar to melanin in peripheral tissues, identifies groups of neurons susceptible in Parkinson’s disease (PD). Whether tyrosinase is beneficial or detrimental to neurons is unclear; whilst the enzyme activity of tyrosinase generates dopamine-quinones and other oxidizing compounds, NM may form a sink for such radical species. In the present study, we demonstrated that tyrosinase is expressed at low levels in the human brain. We found that mRNA, protein and enzyme activity are all present but at barely detectable levels. In cell culture systems, expression of tyrosinase increases neuronal susceptibility to oxidizing conditions, including dopamine itself. We related these in vitro observations to the human disease by assessing whether there was any genetic association between the gene encoding tyrosinase and idiopathic PD. We found neither genotypic or haplotypic association with three polymorphic markers of the gene. This argues against a strong genetic association between tyrosinase and PD, although the observed contribution to cellular toxicity suggests that a biochemical association is likely.

Cuvinte cheie: journal