Heat-shock protein 90 complexes in resting and thrombin-activated platelets

Suttitanamongkol, Sudawadee; Polanowska-Grabowska, Renata; Gear, Adrian R.L.

doi:10.1016/s0006-291x(02)02138-1

Cited by 18 publications

(10 citation statements)

References 23 publications

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“…Human platelets are known to contain HSP90 and HSP70. 40,41 In the present study, we could also detect FKBP51 and FKBP52 in a physical association with GR. However, the dynamic of HSP interaction with GR was different from that reported for PBMCs and other cell types.…”

Section: Discussionsupporting

confidence: 70%

Ligand-specific glucocorticoid receptor activation in human platelets

Moraes

Paul-Clark

Rickman

et al. 2005

Blood

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Section: Discussionsupporting

confidence: 70%

Ligand-specific glucocorticoid receptor activation in human platelets

Moraes

Paul-Clark

Rickman

et al. 2005

Blood

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“…CHIP belongs to the group of really interesting new gene (RING) and RING‐related E3 ligases, and it contains a tetratricopeptide repeat domain involved in Hsp70 and Hsp90 association (Ballinger et al ., ). Hsp90 exists as a complex with Hsc70 and the α and β subunits of CK2 (Suttitanamongkol et al ., ). We showed that CHIP interacted with CK2β (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…CHIP belongs to the group of really interesting new gene (RING) and RING-related E3 ligases, and it contains a tetratricopeptide repeat domain involved in Hsp70 and Hsp90 association (Ballinger et al, 1999). Hsp90 exists as a complex with Hsc70 and the a and b subunits of CK2 (Suttitanamongkol et al, 2002). We showed that CHIP interacted with HEK 293 cells were transfected with or without TGFBRI CA along with Myc-CK2b and then treated with OA (2 nM) for 12 h. Western blot analysis was performed with the indicated antibodies.…”

Section: Discussionmentioning

confidence: 99%

Protein kinase CK2 activation is required for transforming growth factor β‐induced epithelial–mesenchymal transition

et al. 2018

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Transforming growth factor β (TGFβ) is overexpressed in advanced cancers and promotes tumorigenesis by inducing epithelial–mesenchymal transition (EMT), which enhances invasiveness and metastasis. Although we previously reported that EMT could be induced by increasing CK2 activity alone, it is not known whether CK2 also plays an essential role in TGFβ‐induced EMT. Therefore, in the present study, we investigated whether TGFβ signaling could activate CK2 and, if so, whether such activation is required for TGFβ‐induced EMT. We found that CK2 is activated by TGFβ treatment, and that activity peaks at 48 h after treatment. CK2 activation is dependent on TGFβ receptor (TGFBR) I kinase activity, but independent of SMAD4. Inhibition of CK2 activation through the use of either a CK2 inhibitor or shRNA against CSNK2A1 inhibited TGFβ‐induced EMT. TGFβ signaling decreased CK2β but did not affect CK2α protein levels, resulting in a quantitative imbalance between the catalytic α and regulatory β subunits, thereby increasing CK2 activity. The decrease in CK2β expression was dependent on TGFBRI kinase activity and the ubiquitin–proteasome pathway. The E3 ubiquitin ligases responsible for TGFβ‐induced CK2β degradation were found to be CHIP and WWP1. Okadaic acid (OA) pretreatment protected CK2β from TGFβ‐induced degradation, suggesting that dephosphorylation of CK2β by an OA‐sensitive phosphatase might be required for CK2 activation in TGFβ‐induced EMT. Collectively, our results suggest CK2 as a therapeutic target for the prevention of EMT and metastasis of cancers.

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“…Low-molecular-weight HSP is released from vessel walls in response to endothelial injury, binds to platelets, and acts as an inhibitor of platelet aggregation (14). In contrast, thrombin-stimulated platelet activation is accelerated by the presence of HSP90 (31). Moreover, geldanamycin, an HSP90 antagonist, inhibits the formation of thrombosis induced by platelet activation (16).…”

Section: Discussionmentioning

confidence: 99%

<b>Heat-shock protein 72 promotes platelet aggregation induced by various platelet activators in </b><b>rats </b>

Suzuki¹,

Kosuge²,

Kobayashi³

et al. 2017

Biomed. Res.

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Increase of thrombus in the coronary arteries is positively correlated with the level of heat-shock protein 72 (HSP72) in the blood of patients with acute myocardial infarction (AMI). Platelet aggregation participates in thrombus formation on ruptured plaque in AMI. In this study, we aimed to clarify the role of HSP72 in thrombus formation by evaluating the effects of HSP72 on platelet aggregation. Platelet aggregation activities were measured in platelet-rich plasma obtained from male Sprague-Dawley rats with or without the platelet activators, such as adenosine diphosphate (ADP), collagen, thrombin receptor-activating peptide-6 (TRAP-6), ristocetin, and arachidonic acid. Changes in aggregation were estimated by the co-addition of recombinant HSP72 and anti-HSP72 antibodies. Our results showed that addition of HSP72 increased platelet aggregation in the presence of low concentrations of ADP, collagen, TRAP-6, ristocetin, and arachidonic acid. Increased platelet aggregation stimulated by ADP and HSP72 was reduced by the co-addition of anti-HSP72 antibodies. Thus, these findings suggested that HSP72 was released extracellularly in response to stress, promoting thrombus formation and AMI. Additionally, treatment with anti-HSP72 antibodies may control platelet aggregation induced by extracellular HSP72.

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Heat-shock protein 90 complexes in resting and thrombin-activated platelets

Cited by 18 publications

References 23 publications

Ligand-specific glucocorticoid receptor activation in human platelets

Ligand-specific glucocorticoid receptor activation in human platelets

Protein kinase CK2 activation is required for transforming growth factor β‐induced epithelial–mesenchymal transition

<b>Heat-shock protein 72 promotes platelet aggregation induced by various platelet activators in </b><b>rats </b>

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