Abstract：
:Heat shock (HS) proteins (HSP) are a family of molecular chaperones induced by environmental stresses such as oxidative injury, and contribute to protection from and adaptation to cellular stress. We investigated in human monocytes the expression and subcellular distribution of hsp70 and hsc70 after HS and inflammation-related stresses leading to generation of reactive oxygen species by these cells, such as the phorbol ester PMA and erythrophagocytosis (E phi). By combining immunofluorescent staining and Western blot on subcellular fractions, we found that all three stress factors resulted in an increased hsp70 expression, however the subcellular distribution pattern was different depending on the type of stress. While HS induced a rapid translocation of hsp70 into the nucleus, no nuclear translocation of hsp70 was observed after PMA or E phi. Neither of the examined stresses induced membrane expression of hsp70. The observed differences in subcellular distribution pattern might relate to distinct regulation and specific functions of hsp70 in inflammation.
journal_name
Inflammationjournal_title
Inflammationauthors
Mariéthoz E,Jacquier-Sarlin MR,Multhoff G,Healy AM,Tacchini-Cottier F,Polla BSdoi
10.1023/a:1027338323296subject
Has Abstractpub_date
1997-12-01 00:00:00pages
629-42issue
6eissn
0360-3997issn
1573-2576journal_volume
21pub_type
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