background: the aim of this study is to create an ex vivo model to examine the expression of two heat shock protein 70 (hsp70) family members, heat shock protein 72 (hsp72) and heat shock constitute protein 70 (hsc70), at the mrna and protein levels in differentiating corneal cells from air exposed limbal stem cells. materials and methods: limbal biopsies were cultured as explants on a cellular...

The sequence relationship between the small heat shock proteins and the eye lens protein alpha-crystallin (Ingolia, T. D., and E. E. Craig, 1982, Proc. Natl. Acad. Sci. USA, 79: 2360-2364) prompted us to subject rat lenses in organ culture to heat shock and other forms of stress. The effects on protein synthesis were followed by labeling with [35S]methionine and analysis by one- and two-dimensi...

Many features of the chaperone action of clusterin are similar to those of the intracellular small heat shock proteins (sHSPs) that, like clusterin, exist in solution as heterogeneous aggregates. Increased temperature induces dissociation of some sHSP aggregates and an enhanced chaperone action, suggesting that a dissociated form is the active chaperone species. We recently reported that cluste...

The α-crystallin domain (ACD) is an ancient domain conserved among all kingdoms. Plant ACD proteins have roles in abiotic stresses, transcriptional regulation, inhibiting virus movement, and DNA demethylation. An exhaustive in-silico analysis using Hidden Markov Model-based conserved motif search of the tomato proteome yielded a total of 50 ACD proteins that belonged to four groups, sub-divided...

Small heat shock proteins usually exhibit increased chaperone-like activity either at high temperatures or after preheating. However, the activation mechanism is still unclear. In the current study, we investigated the preheating-activation process of Mj HSP16.5, using various biophysical methods. Although Mj HSP16.5 was reported to be the most monodispersed sHSPs, we found that the newly purif...

Native α-crystallin [1], by far the most abundant protein found in the lens, is a hetero-oligomeric polydisperse complex about 700-800 kDa in size [2]. The oligomer is composed of about 35-40 noncovalent subunits in a 3:1 mixture of two highly homologous 20 kDa proteins, αA-crystallin and αB-crystallin, respectively. Tertiary structure is thought to be similar to that of other small heat shock ...