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- W180655802 startingPage "193" @default.
- W180655802 abstract "Molecular chaperons of the heat shock protein (HSP) family are conserved proteins that modulate intracellular protein folding. By binding to unfolded or folding intermediate polypeptides, chaperons prevent misfolding and aggregation, and promote folding and translocation [1]. Human and microbial HSP70 consist of an N-terminal ATPase fragment of 44 kD and a C-terminal peptide-binding fragment of 28.5 kD. HSP70 is a highly conserved protein among various species and there is about 60% homology between human and mycobacterial and 70% between E. coli (Dnak) and mycobacterial HSP70. However, it should be noted that a homology plot between human and E. coli HSP70 shows differences along the molecule between 20 and 80% [2]. This variation must be taken into account when considering HSP70 epitopes. Mammalian HSP70 is found in all nucleated cells as a constitutive protein in the cytosol, but can be induced by a variety of stress stimuli (e.g., heat, toxic elements, infection) to give rise to the inducible HSP70. Another type of HSP70 (BiP) is found in the endoplasmic reticulum. Microbial HSP70 is found in bacteria, fungi, parasites and viruses. The gut associated lymphoid tissue is activated not only by LPS which are found exclusively in Gram-negative bacteria, but also HSP70 found in both Gram-positive and negative bacteria. Hence, T- and B-cells in Peyer’s patches of the gut are activated by HSP70 and LPS of gut bacteria. Some of the properties of HSPs are summarised in Table 1, but this review will emphasize the novel findings of HSP70." @default.
- W180655802 created "2016-06-24" @default.
- W180655802 creator A5035182164 @default.
- W180655802 creator A5056755963 @default.
- W180655802 creator A5089007009 @default.
- W180655802 date "2003-01-01" @default.
- W180655802 modified "2023-09-23" @default.
- W180655802 title "Heat shock protein receptors, functions and their effect on monocytes and dendritic cells" @default.
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