TY - JOUR
T1 - Heat shock and proinflammatory stressors induce differential localization of heat shock proteins in human monocytes
AU - Mariéthoz, Ewa
AU - Jacquier-Sarlin, Muriel R.
AU - Multhoff, Gabriele
AU - Healy, Aileen M.
AU - Tacchini-Cottier, Fabienne
AU - Polla, Barbara S.
N1 - Funding Information:
Acknowledgments—Ewa Mariethoz was supported by a grant from the Fonds Marie Heimt Vogtlin. BSP is supported by INSERM. Research described here was supported in part by the Fonds National Suisse de la Recherche Scientifique and the Communaute de 1'Industrie Suisse de la Cigarette (CISC). This paper being coauthored by women scientists all trained by women scientists, we would like to acknowledge them as essential role models and dedicate them this paper: Laurie Glim-cher, from Harvard School of Public Health, Boston, USA; Dolores J. Schendel, from the Institute of Immunology, Munich, Germany; Fran9oise Gabert from University Joseph Fourier, Grenoble, France; and Patricia Jones from Stanford University, USA.
PY - 1997
Y1 - 1997
N2 - 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 (Eφ). 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 Eφ. 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.
AB - 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 (Eφ). 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 Eφ. 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.
UR - http://www.scopus.com/inward/record.url?scp=0031470026&partnerID=8YFLogxK
U2 - 10.1023/A:1027338323296
DO - 10.1023/A:1027338323296
M3 - Article
C2 - 9429910
AN - SCOPUS:0031470026
SN - 0360-3997
VL - 21
SP - 629
EP - 642
JO - Inflammation
JF - Inflammation
IS - 6
ER -