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Heat shock protein 60 involvement in vascular smooth muscle cell proliferation

JF. Deniset, TE. Hedley, M. Hlaváčková, MN. Chahine, E. Dibrov, K. O'Hara, GG. Maddaford, D. Nelson, TG. Maddaford, R. Fandrich, E. Kardami, GN. Pierce,

. 2018 ; 47 (-) : 44-51. [pub] 20180326

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc19035323

Grantová podpora
CIHR - Canada

AIM: Heat shock protein 60 (Hsp60) is a mediator of stress-induced vascular smooth muscle cell (VSMC) proliferation. This study will determine, first, if the mitochondrial or cytoplasmic localization of Hsp60 is critical to VSMC proliferation and, second, the mechanism of Hsp60 induction of VSMC proliferation with a focus on modification of nucleocytoplasmic trafficking. METHODS AND RESULTS: Hsp60 was overexpressed in primary rabbit VSMCs with or without a mitochondrial targeting sequence (AdHsp60mito-). Both interventions induced an increase in VSMC PCNA expression and proliferation. The increase in VSMC PCNA expression and growth was not observed after siRNA-mediated knockdown of Hsp60 expression. Nuclear protein import in VSMC was measured by fluorescent microscopy using a microinjected fluorescent import substrate. Nuclear protein import was stimulated by both AdHsp60 and AdHsp60mito- treatments. AdHsp60 treatment also induced increases in nucleoporin (Nup) 62, Nup153, importin-α, importin-β and Ran expression as well as cellular ATP levels compared to control. AdHsp60mito- treatment induced an up-regulation in importin-α, importin-β and Ran expression compared to control. Hsp60 knockdown did not change nuclear protein import nor the expression of any nuclear transport receptors or nucleoporins. Both heat shock treatment and Hsp60 overexpression promoted the interaction of Ran with Hsp60. CONCLUSIONS: VSMC proliferation can be modulated via an Hsp60 dependent, cytosol localized mechanism that in part involves a stimulation of nuclear protein import through an interaction with Ran. This novel cellular signaling role for Hsp60 may be important in growth-based vascular pathologies like atherosclerosis and hypertension.

Citace poskytuje Crossref.org

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$a AIM: Heat shock protein 60 (Hsp60) is a mediator of stress-induced vascular smooth muscle cell (VSMC) proliferation. This study will determine, first, if the mitochondrial or cytoplasmic localization of Hsp60 is critical to VSMC proliferation and, second, the mechanism of Hsp60 induction of VSMC proliferation with a focus on modification of nucleocytoplasmic trafficking. METHODS AND RESULTS: Hsp60 was overexpressed in primary rabbit VSMCs with or without a mitochondrial targeting sequence (AdHsp60mito-). Both interventions induced an increase in VSMC PCNA expression and proliferation. The increase in VSMC PCNA expression and growth was not observed after siRNA-mediated knockdown of Hsp60 expression. Nuclear protein import in VSMC was measured by fluorescent microscopy using a microinjected fluorescent import substrate. Nuclear protein import was stimulated by both AdHsp60 and AdHsp60mito- treatments. AdHsp60 treatment also induced increases in nucleoporin (Nup) 62, Nup153, importin-α, importin-β and Ran expression as well as cellular ATP levels compared to control. AdHsp60mito- treatment induced an up-regulation in importin-α, importin-β and Ran expression compared to control. Hsp60 knockdown did not change nuclear protein import nor the expression of any nuclear transport receptors or nucleoporins. Both heat shock treatment and Hsp60 overexpression promoted the interaction of Ran with Hsp60. CONCLUSIONS: VSMC proliferation can be modulated via an Hsp60 dependent, cytosol localized mechanism that in part involves a stimulation of nuclear protein import through an interaction with Ran. This novel cellular signaling role for Hsp60 may be important in growth-based vascular pathologies like atherosclerosis and hypertension.
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$a Hedley, Thomas E $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Departments of Physiology and Pathophysiology, Canada.
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$a Hlaváčková, Markéta $u Institute of Physiology, Czech Academy of Sciences, Prague, Czech Republic.
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$a Chahine, Mirna N $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Departments of Physiology and Pathophysiology, Canada.
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$a Dibrov, Elena $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Departments of Physiology and Pathophysiology, Canada.
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$a Maddaford, Graham G $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Departments of Physiology and Pathophysiology, Canada.
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$a Nelson, David $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Departments of Physiology and Pathophysiology, Canada.
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$a Fandrich, Robert $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Anatomy and Cell Biology, Rady Faculty of Health Sciences, University of Manitoba, Winnipeg, MB, Canada.
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$a Kardami, Elissavet $u Institute of Cardiovascular Sciences, Albrechtsen Research Centre, St Boniface Hospital, Canada; Anatomy and Cell Biology, Rady Faculty of Health Sciences, University of Manitoba, Winnipeg, MB, Canada.
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