Rabbit Anti-Human CRYAA Polyclonal antibody

Investigations of genetic diseases such as cystic fibrosis, alpha-1-antitrypsin deficiency, phenylketonuria, mitochondrial acyl-CoA dehydrogenase deficiencies, and many others have shown that enhanced proteolytic degradation of mutant proteins is a common molecular pathological mechanism. Detailed studies of the fate of mutant proteins in some of these diseases have revealed that impaired or aberrant folding of mutant polypeptides typically results in prolonged interaction with molecular chaperones and degradation by intracellular proteases before the functional conformation is acquired. This appears to be the case for many missense mutations and short in-frame deletions or insertions that represent a major fraction of the mutations detected in genetic diseases. In some diseases, or under some circumstances, the degradation system is not efficient. Instead, aberrant folding leads to accumulation of protein aggregates that damage the cell. Mechanisms by which misfolded proteins are selected for degradation have first been delineated for the endoplasmatic reticulum; this process has been termed "protein quality control." Similar mechanisms appear to be operative in all cellular compartments in which proteins fold. Within the context of genetic diseases, we review knowledge on the molecular processes underlying protein quality control in the various subcellular compartments, The important impact of such systems for variability of the expression of genetic deficiencies is emphasised. Hum Mutat 14:186-198, 1999. (C) 1999 Wiley-Liss, Inc.

Background The mechanism of diabetes and cataracts is complicated. Considering our increasing acknowledge of exosomes, exosomal miRNAs isolated from aqueous humour (AH) may play an important role in the mechanism of diabetes and cataracts. Our study aimed to isolate exosomes from human aqueous humour and study the functions of exosomal miRNAs on human lens epithelial cells (HLECs). Results MiRNA sequencing revealed that 295 miRNAs were upregulated and 138 miRNAs were downregulated in exosomes of the diabetes and cataracts group (DMC) compared with the age-related cataracts group (ARC), among which miR-551b was highly expressed with a log2 fold change of 5.99. GO and KEGG analyses indicated that the predicted genes were mainly involved in cadherin binding, proteoglycans in cancer and AGE-RAGE signalling pathway in diabetic complications. We then examined the function of miR-551b and found that miR-551b reduced the viability and increased the apoptosis of HLECs by downregulating CRYAA expression. Conclusions Exosomes isolated from human aqueous humour contained abundant miRNAs. A highly expressed miRNA, miR-551b, could regulate the functions of HLEC by targeting CRYAA. Methods We pooled all the aqueous humour of each group into one sample and isolated exosomes from human aqueous humour by ultracentrifugation, measured the size and concentration of exosomes by nanoparticle tracking analysis (NTA), observed the morphology of exosomes by transmission electron microscopy (TEM), and sequenced exosomal miRNAs. We performed bioinformatic analysis of the sequencing results, including GO analysis and KEGG pathway enrichment. We then examined CRYAA mRNA expression levels and protein levels by quantitative real-time PCR and Western blot. Cell Counting Kit-8 and flow cytometry were applied to examine cell viability, proliferation and apoptosis.