E. Muller et al., HEAT-SHOCK PROTEINS HSP25, HSP60, HSP72, HSP73 IN ISOOSMOTIC CORTEX AND HYPEROSMOTIC MEDULLA OF RAT-KIDNEY, Pflugers Archiv, 431(4), 1996, pp. 608-617
The distribution of heat shock proteins (HSP) HSP60, HSP73, HSP72 and
HSP25 in the isoosmotic cortex and the hyperosmotic medulla of the rat
kidney was investigated using Western blot analysis and immunohistoch
emistry. HSP73 was homogeneously distributed throughout the whole kidn
ey. The level of HSP60 was high in the renal cortex and low in the med
ulla. HSP25 and HSP72 were present in large amounts in the medulla. On
ly low levels of HSP25 and almost undetectable amounts of HSP72 were f
ound in the cortex. HSP25 exists in one nonphosphorylated and several
phosphorylated isoforms. Western blot analysis preceded by isoelectric
focussing showed that HSP25 predominates in its nonphosphorylated for
m in the outer medulla but in its phosphorylated form in cortex and in
ner medulla. Although this intrarenal distribution pattern was not cha
nged during prolonged anaesthesia (thiobutabarbital sodium), a shift f
rom the nonphosphorylated to the phosphorylated isoforms of HSP25 occu
rred in the medulla. The characteristic intrarenal distribution of the
constitutively expressed HSPs (HSP73, HSP60, HSP25) may reflect diffe
rent states of metabolic activity in the isoosmotic (cortex) and hyper
osmotic (medulla) zones of the kidney. The high content of inducible H
SP72 in the medulla most likely is a consequence of the osmotic stress
imposed upon the cells by the high urea and salt concentrations in th
e hyperosmotic medullary environment.