To characterize heat-shock proteins (HSPs) of the 70-kDa family in the crayfish medial giant axon (MGA), we analyzed axoplasmic proteins separately from proteins of the glial sheath. Several different molecular weight isoforms of constitutive HSP 70s that were detected on immunoblots were approximately 1-3% of the total protein in the axoplasm of MGAs. To investigate inducible HSPs, MGAs were h...

Proteins are essential components of cellular life, as building blocks, but also to guide and execute all cellular processes. Proteins require a three-dimensional folding, which is constantly being challenged by their environment. Challenges including elevated temperatures or redox changes can alter this fold and result in misfolding of proteins or even aggregation. Cells are equipped with seve...

CD4+CD25+ Tregs regulate immunity, but little is known about their own regulation. We now report that the human 60-kDa heat shock protein (HSP60) acts as a costimulator of human Tregs, both CD4+CD25int and CD4+CD25hi. Treatment of Tregs with HSP60, or its peptide p277, before anti-CD3 activation significantly enhanced the ability of relatively low concentrations of the Tregs to downregulate CD4...

The influence of two different stocking densities (0.20 m2/animal and 0.40 m2/animal) in transit under the hot, humid tropical conditions on heat shock protein (hsp) 70 induction was investigated in 60 Boer does. The animals were road transported for 3 h and the control group was kept under normal conditions in the farm. Irrespective of stocking density, transportation significantly increased h...

The 70-kDa heat shock cognate (Hsc70) chaperone plays a crucial role in protein (re-)folding and triage in the mammalian cytosol. Here we study, by NMR, the 44-kDa nucleotide-binding domain (NBD) of this molecule, which allosterically regulates, by binding either ADP or ATP in a cleft between the two main lobes, the chaperoning affinity of the attached substrate-binding domain. The NBD is also ...

Molecular chaperones and their co-chaperones are crucial for the facilitation of efficient protein folding, and prevention of denaturation and aggregation of nascent polypeptides. Hsp70/Hsp90 organizing protein (Hop), a co-chaperone of the two major molecular chaperones, heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90), facilitates their interaction by acting as an adaptor betwee...

A new diarylheptanoid containing a chalcone moiety, katsumain H (1), was isolated from the seeds of Alpinia katsumadai. The structure was elucidated using a combination of 1D/2D NMR spectroscopy and mass spectrometry data analysis. The absolute configurations of C-3, C-5, and C-7 in 1 were assigned based on its optical rotation and after comparing its NMR chemical shifts with those of its diast...