Alteration in the ubiquitin structure and function in the human lens: a possible mechanism of senile cataractogenesis.
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.
Stiuso
P
P
CRISCEB, Seconda Università di Napoli, via Costantinopoli 16, Naples, Italy. paola.stiuso@unina2.it
Libondi
T
T
Facchiano
A M
AM
Colicchio
P
P
Ferranti
P
P
Lilla
S
S
Colonna
G
G
D000368:Aged; D002386:Cataract / Q000209:etiology* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D007908:Lens, Crystalline / Q000737:chemistry*; D008958:Models, Molecular; D008970:Molecular Weight; D010449:Peptide Mapping; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D025801:Ubiquitin / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology*
D025801:Ubiquitin