T. Gudi et Cm. Gupta, HSP 70-LIKE PROTEIN IN RHESUS ERYTHROCYTE CYTOSOL AND ITS INTERACTIONS WITH MEMBRANE SKELETON UNDER HEAT AND PATHOLOGICAL STRESS, The Journal of biological chemistry, 268(28), 1993, pp. 21344-21350
The rhesus erythrocytes were examined for the presence of protein(s) s
imilar to the 70-kDa class of heat shock proteins (hsp 70). Also, inte
ractions of these proteins with the erythrocyte membrane were studied
under heat stress. These cells in their cytosol contained at least two
proteins of about 70 kDa molecular mass; one of which closely resembl
ed the hsp 70 family of proteins. This protein under normal conditions
localized mainly in the cytosol, but it had a strong tendency to bind
the membrane under heat stress. The binding was almost exclusively re
stricted to the membrane skeleton and seemed to involve primarily the
hydrophobic interactions. A 70-kDa protein immunologically similar to
the above protein(s) was detected also in the membranes of rhesus eryt
hrocytes harboring the schizont stage of the simian malarial parasite
Plasmodium knowlesi. From these results, we conclude that hsp 70-like
proteins in the mature mammalian erythrocytes could perhaps play an im
portant role in protecting the cells under stress by stabilizing the m
embrane skeleton through their interactions with skeletal proteins.