Alteration in the ubiquitin structure and function in the human lens: a possible mechanism of senile cataractogenesis

FEBS Letters

Colicchio, P¹  Colonna, G²  Stiuso, P²  Lilla, S³  Libondi, T²  Facchiano, A.M²  Ferranti, P³ 

[1] Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli, via Costantinopoli 16, 80138 Naples, Italy;CRISCEB, Seconda Università di Napoli, via Costantinopoli 16, 80138 Naples, Italy;Istituto di Scienze dell'Alimentazione, CNR, via Roma 52, 83100 Avellino, Italy

关键词: Senile cataract;    Ubiquitin;    Protein degradation;   

DOI  :  10.1016/S0014-5793(02)03494-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown