The Endoplasmic Reticulum-Resident Chaperone Heat Shock Protein 47 Protects the Golgi Apparatus from the Effects of O-Glycosylation Inhibition

Miyata, Sumiko; Mizuno, Tokuo; Koyama, Yoshihisa; Katayama, Taiichi; Tohyama, Masaya

doi:10.1371/journal.pone.0069732

Cited by 52 publications

(58 citation statements)

References 83 publications

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“…These observations indicated that HSP47 may be a potential therapeutic target in LSCC and indirectly supported the concept that low HSP47 expression is correlated with short survival and poor prognosis in LSCC. As shown in previous studies, HSP47 plays an important regulatory role in various types of tumours (39)(40)(41) and has a close relationship with tumour apoptosis (40,42). However, the mechanism of HSP47-mediated Hep-2 cell apoptosis is still unknown.…”

Section: Discussionmentioning

confidence: 62%

HSP47 is associated with the prognosis of laryngeal squamous cell carcinoma by inhibiting cell viability and invasion and promoting apoptosis

et al. 2017

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Abstract. Heat shock protein 47 (HSP47) is a 47 kDa collagen binding protein that has a close relationship with the development and progression of tumours. However, little is known concerning the expression profile of HSP47 in laryngeal squamous cell carcinoma (LSCC) patients and there is still insufficient data concerning the underlying mechanisms. The aim of the present study was to explore the expression of HSP47 in LSCC and provide an overview of its association with tumourigenicity and clinical prognosis. The expression of HSP47 in LSCC and adjacent non-cancerous laryngeal tissues was assessed via western blotting and immunohistochemical studies. The prognostic significance of HSP47 expression was analysed using a Kaplan-Meier survival curve. To investigate the influence of HSP47 on the viability, invasion and apoptosis of a LSCC cell line, we performed an in vitro analysis with plasmid vectors and small interfering RNA (siRNA). Our results showed that HSP47 protein expression in the LSCC tissues was markedly decreased compared to that noted in the adjacent non-cancerous tissues, and low expression of HSP47 was correlated with poor prognosis in LSCC patients. Upregulation of HSP47 via plasmid vectors inhibited the proliferation, reduced the invasive ability, increased the sensitivity to cisplatin chemotherapy, promoted apoptosis, and induced the G1 phase arrest of LSCC cells in vitro. The expression of apoptosis-regulating proteins was also altered when HSP47 was upregulated, involving increased expression of cleaved caspase-7/-8/-9, PARP, and Bax and decreased expression of Bcl-2. Our present data suggest that HSP47 is an important prognostic factor and an attractive therapeutic target in LSCC due to its influence on the biological behaviour of LSCC cells.

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Section: Discussionmentioning

confidence: 62%

HSP47 is associated with the prognosis of laryngeal squamous cell carcinoma by inhibiting cell viability and invasion and promoting apoptosis

et al. 2017

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“…Although HSP47 is an ER chaperone, its expression is not induced by ER stress inducers such as tunicamycin or thapsigargin but is increased by heat stress. Of note, HSP47 expression is induced by BG as well as monensin treatment (Miyata et al, 2013), suggesting its close link to Golgi function, and although HSP47 is constitutively localized in the ER, it does not translocate to the Golgi upon BG treatment.…”

Section: Hsp47 Pathwaymentioning

confidence: 97%

“…When expression of HSP47 was suppressed by RNA interference, BG treatment resulted in expansion and fragmentation of the Golgi apparatus as well as activation of caspase-2 and apoptosis (Miyata et al, 2013). On the contrary, when HSP47 was overexpressed, BG-induced apoptosis was attenuated.…”

Section: Hsp47 Pathwaymentioning

confidence: 99%

“…The second pathway of the mammalian Golgi stress response is the HSP47 pathway, which was elucidated by Tohyama and colleagues (Miyata et al, 2013) (Fig. 3).…”

Section: Hsp47 Pathwaymentioning

confidence: 99%

“…The molecular mechanism of the Golgi stress response has been less analyzed compared with that of the ER stress response, but recent studies revealed an important part of the regulatory mechanism, including the TFE3, HSP47, and CREB3 pathways (Fig. 3) (Miyata et al, 2013;Oku et al, 2011;Reiling et al, 2013;Taniguchi et al, 2015Taniguchi et al, , 2016.…”

Section: Introductionmentioning

confidence: 99%

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TFE3, HSP47, and CREB3 Pathways of the Mammalian Golgi Stress Response

Taniguchi

Yoshida

2017

Cell Struct. Funct.

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ABSTRACT. The capacity of each organelle in eukaryotic cells is tightly regulated in accordance with cellular demands by specific regulatory systems, which are generically termed organelle autoregulation. The Golgi stress response is one of the systems of organelle autoregulation and it augments the capacity of Golgi function if this becomes insufficient (Golgi stress). Recently, several pathways of the mammalian Golgi stress response have been identified, specifically the TFE3, HSP47, and CREB3 pathways. This review summarizes the essential parts of the Golgi stress response from the perspective of the organelle autoregulation.

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Golgi stress response and organelle zones

Sasaki

Yoshida

2019

FEBS Letters

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Organelles have been studied traditionally as single units, but a novel concept is now emerging: each organelle has distinct functional zones that regulate specific functions. The Golgi apparatus seems to have various zones, including zones for: glycosylphosphatidylinositol‐anchored proteins; proteoglycan, mucin and lipid glycosylation; transport of cholesterol and ceramides; protein degradation (Golgi membrane‐associated degradation); and signalling for apoptosis. The capacity for these specific functions and the size of the corresponding zones appear to be tightly regulated by the Golgi stress response to accommodate cellular demands. For instance, the proteoglycan and mucin zones seem to be separately augmented during the differentiation of chondrocytes and goblet cells, respectively. The mammalian Golgi stress response consists of several response pathways. The TFE3 pathway regulates the general function of the Golgi, such as structural maintenance, N‐glycosylation and vesicular transport, whereas the proteoglycan pathway increases the expression of glycosylation enzymes for proteoglycans. The CREB3 and HSP47 pathways regulate pro‐ and anti‐apoptotic functions, respectively. These observations indicate that the Golgi is a dynamic organelle, the capacity of which is upregulated according to cellular needs.

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The Endoplasmic Reticulum-Resident Chaperone Heat Shock Protein 47 Protects the Golgi Apparatus from the Effects of O-Glycosylation Inhibition

Cited by 52 publications

References 83 publications

HSP47 is associated with the prognosis of laryngeal squamous cell carcinoma by inhibiting cell viability and invasion and promoting apoptosis

HSP47 is associated with the prognosis of laryngeal squamous cell carcinoma by inhibiting cell viability and invasion and promoting apoptosis

TFE3, HSP47, and CREB3 Pathways of the Mammalian Golgi Stress Response

Golgi stress response and organelle zones

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