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GRANADA UNIVERSITY RESEARCHERS INVESTIGATE THE PROTEIN MECHANISMS THAT CAUSE NEURODEGENERATIVE DISEASES
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2006-05-09 Gaona Ismael
Andalucia Investiga
Programa de Divulgacion Cientifica de Andalucia Parque de las Ciencias Avda del Mediterraneo s/n
18006 Granada
SPAIN
igaona@andaluciainvestiga.com
Tel: 34 68642717
www.andaluciainvestiga.com
The Granada scientists are collaborating with seven European laboratories, dedicated to researching the common characteristics that will make it possible to establish a general amyloid fibre formation mechanism.
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Scientists in Granada Universitys Physical Chemistry Department are investigating, using a model protein, the molecular bases that give rise to the formation of amyloid fibres, which cause certain degenerative diseases of the nervous system, such as Alzheimers Disease, Parkinsons Disease, or mad cows disease, both in animals and in humans, as well as other non-neurological conditions, such type II Diabetes, or certain disorders associated with haemodialysis. The main characteristic of these illnesses is the uncontrolled formation of protein deposits in the form of amyloid fibres, in tissue and organs, which alter their functions
Francisco Conejero Lara, researcher in charge of the project, explains that the more knowledge that can be obtained on the mechanism and characteristics of the formation process of these fibres, the earlier action can be taken against it, through drugs that prevent or delay fibre deposit. In this way it will be possible to prevent or reduce the damage that this process causes in the affected organs.
A number of different factors, many still unidentified, favour abnormal protein folding, which results in a configuration that determines and initiates the formation of amyloid fibres. In the intermediate stages of the process, extremely sticky structures are formed, which, according to the researcher, are the precursors of these protein aggregates.
In the aforementioned illnesses it has been observed that regardless of the protein responsible, all of them deposit themselves forming a common structure, which consists in an enormous ? lamina that extends without interruption along the fibre. Furthermore, according to the scientists, very different proteins, even some totally unrelated to amyloidosis type illnesses, can form the same fibres with the same appearance – under microscope – and structures, if subjected to the appropriate conditions.
The Granada researchers are working with an SH3 domain. This is a protein fragment that, despite not being associated with the formation of deposits in degenerative diseases, is susceptible to form these fibres. Based on in vitro experiments, the scientists are studying what molecular bases generate abnormal protein folding. For this purpose they are focussing on establishing the characteristics of stability, structure and factors (kinetic and thermodynamic) of the precursors of amyloid fibre formation in the SH3 domain.
The Granada scientists are collaborating with seven European laboratories, dedicated to researching the common characteristics that will make it possible to establish a general amyloid fibre formation mechanism.
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Subject: Life Science;
Country: SPAIN;
Institution: Public Research;
Category: Project;
