Neuromelanin was isolated from human substantia nigra using different procedures. in the pigment isolated by any of these procedures a peptide component covalently bound to the melanic structure was found, as shown by treatment with reagents known to eliminate noncovalently bound proteins. The amino acid content of such a peptide component was reproducible and corresponded to similar to 15% of the neuromelanin weight. Neuromelanin also showed the ability to absorb specifically lipid molecules, similar to 20% of its weight, and among these lipids cholesterol was identified, constituting similar to 5% of the total lipid mixture. A synthetic melanin, incubated with putamen homogenate, bound tissue peptides with an amino acid content quite close to that of neuromelanin. The same synthetic melanin adsorbed a lower amount of lipids from the putamen homogenate compared with neuromelanin. The sulfur content of neuromelanin was also reproducible even using different isolation procedures. A nonpigmented tissue like corpus callosum was used as a control and extracted by the method used for neuromelanin isolation; a total elimination of tissue components was found, thus demonstrating the capability of the reported procedures to isolate neuromelanin alone. The presence of a peptide component in the neuromelanin structure and the selective affinity for lipid molecules suggest new aspects of the functional role and metabolic pathway of neuromelanin.

Interaction of human substantia nigra neuromelanin with lipids and peptides / L. Zecca, P. Costi, C. Mecacci, S. Ito, M. Terreni, S. Sonnino. - In: JOURNAL OF NEUROCHEMISTRY. - ISSN 0022-3042. - 74:4(2000), pp. 1758-1765.

Interaction of human substantia nigra neuromelanin with lipids and peptides

S. Sonnino
Ultimo
2000

Abstract

Neuromelanin was isolated from human substantia nigra using different procedures. in the pigment isolated by any of these procedures a peptide component covalently bound to the melanic structure was found, as shown by treatment with reagents known to eliminate noncovalently bound proteins. The amino acid content of such a peptide component was reproducible and corresponded to similar to 15% of the neuromelanin weight. Neuromelanin also showed the ability to absorb specifically lipid molecules, similar to 20% of its weight, and among these lipids cholesterol was identified, constituting similar to 5% of the total lipid mixture. A synthetic melanin, incubated with putamen homogenate, bound tissue peptides with an amino acid content quite close to that of neuromelanin. The same synthetic melanin adsorbed a lower amount of lipids from the putamen homogenate compared with neuromelanin. The sulfur content of neuromelanin was also reproducible even using different isolation procedures. A nonpigmented tissue like corpus callosum was used as a control and extracted by the method used for neuromelanin isolation; a total elimination of tissue components was found, thus demonstrating the capability of the reported procedures to isolate neuromelanin alone. The presence of a peptide component in the neuromelanin structure and the selective affinity for lipid molecules suggest new aspects of the functional role and metabolic pathway of neuromelanin.
Neuromelanin; Parkinson's disease; Substantia nigra
Settore BIO/10 - Biochimica
2000
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/189295
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