Regular ArticleStudies on Trypsin-modified Bovine and Human Lens Acylpeptide Hydrolase
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Cited by (7)
Lens crystallin modifications and cataract in transgenic mice overexpressing acylpeptide hydrolase
2014, Journal of Biological ChemistryCitation Excerpt :KKS5 and mutant lines did not show cleavage of APH. It is plausible that the 57-kDa APH fragment possesses hydrolytic activity against crystallins, similar to our previous observation made in vitro with a 55-kDa APH fragment (47). In support of this view, we saw an increased accumulation of crystallin fragments in mouse lens expressing active APH even before the development of cataract.
Acylaminoacyl-Peptidase
2013, Handbook of Proteolytic EnzymesEffect of short-term exposure to dichlorvos on synaptic plasticity of rat hippocampal slices: Involvement of acylpeptide hydrolase and α<inf>7</inf> nicotinic receptors
2009, Toxicology and Applied PharmacologyCitation Excerpt :For example, it has been reported that in bovine and human lens, ACPH catalytic subunit of 75 kDa removes N-acetylated amino acid residues from the αA-crystallin, and a truncated form of 55 kDa has an endoprotease activity that could play a role in the age-related cleavage of βB2-crystallins (Senthilkumar et al., 2001). Interestingly, the total ACPH activity was found to be decreased in human cataract lenses, (Senthilkumar et al., 2001) and this may contribute to the accumulation of N-terminally blocked peptides in the lens nucleus (Sharma and Kester, 1996). More relevant to our results is the finding reported by Yamin et al. (2007) indicating that ACPH degrades Aβ1–40 in vitro and that Alzheimer's disease brains express lower levels of ACPH mRNA than brains of age-matched controls (Yamin et al., 2007).
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Author for correspondence: K. Krishna Sharma, Mason Eye Institute, University of Missouri, One Hospital Drive, Columbia, MO 65212, U.S.A. E-mail: [email protected]