High-performance liquid chromatography purification followed by mass spectrometry analyses highlighted that human senile cataractous lens includes a 8182 Da species which is absent in the normal lens, whereas a 8566/8583 Da species is present in both lenses. Western blot analysis identified both species as ubiquitin. The species at lower molecular weight is a shorter form due to the cleavage of the C-terminal residues 73-76. As it is the last amino acid of ubiquitin which is involved in the protein degradation mechanism, we suggest that this structure modification compromises the function of ubiquitin and consequently the physiologically occurring degradation of the lens proteins.
Alteration in the ubiquitin structure and function in the human lens: a possible mechanism of senile cataractogenesis / P., Stiuso; T., Libondi; A. M., Facchiano; P., Colicchio; Ferranti, Pasquale; S., Lilla; G., Colonna. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 531:2(2002), pp. 162-167.
Alteration in the ubiquitin structure and function in the human lens: a possible mechanism of senile cataractogenesis
FERRANTI, PASQUALE;
2002
Abstract
High-performance liquid chromatography purification followed by mass spectrometry analyses highlighted that human senile cataractous lens includes a 8182 Da species which is absent in the normal lens, whereas a 8566/8583 Da species is present in both lenses. Western blot analysis identified both species as ubiquitin. The species at lower molecular weight is a shorter form due to the cleavage of the C-terminal residues 73-76. As it is the last amino acid of ubiquitin which is involved in the protein degradation mechanism, we suggest that this structure modification compromises the function of ubiquitin and consequently the physiologically occurring degradation of the lens proteins.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
