Expression of a Small Heat Shock Protein 27 (HSP27) in Mouse Skin Tumors Induced by UVB-Irradiation.

Kiriyama, Misao T.; Oka, Mutsuo; Takehana, Makoto; Kobayashi, Shizuko

doi:10.1248/bpb.24.197

Cited by 19 publications

(20 citation statements)

References 25 publications

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“…The data obtained from these studies indicate that Hsp27 expression is strictly correlated to keratinocyte differentiation, suggesting that the absence of this protein in epidermal cells could be regarded as a marker of epidermal malignancy in all the species so far investigated (Trautinger et al 1995;Kiriyama et al 2001;Romanucci et al 2005). As a matter of fact, canine Hsp27 is also very similar to the human form with its primary structure deduced from nucleotide sequence revealing a 209 amino acid protein sharing 86-89% homology with human, mouse, rat and hamster small Hsp (Larsen et al 1995).…”

Section: Introductionmentioning

confidence: 96%

Heat shock proteins in animal neoplasms and human tumours—a comparison

Romanucci

Bastow

Salda

2008

Cell Stress and Chaperones

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Heat shock proteins (HSPs) are implicated in all phases of cancer from proliferation, impaired apoptosis and sustained angiogenesis to invasion and metastasis. The presence of abnormal HSP levels in several human tumours suggests that these proteins could be used as diagnostic and/or prognostic markers, whilst the direct correlation between HSP expression and drug resistance in neoplastic tissues means they could also be used to predict cancer response to specific treatment. HSPs have also been successfully targeted in clinical trials modifying their expression or chaperone activity. Preliminary studies in veterinary medicine have also demonstrated the presence of altered HSP expression in neoplasms, and the study of carcinogenesis and the role of HSPs in animal models will surely be an additional source of information for clinical cancer research.

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Section: Introductionmentioning

confidence: 96%

Heat shock proteins in animal neoplasms and human tumours—a comparison

Romanucci

Bastow

Salda

2008

Cell Stress and Chaperones

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“…However, little is known about the molecular mechanism regulating the conversion of cellular conditions such as proliferation, differentiation or cell death. In recent studies a family of heat shock proteins (HSP) has been suggested to regulate or switch the proliferation vs. differentiation or the proliferation vs. cell death [17, 31]. …”

Section: Introductionmentioning

confidence: 99%

Localization of Heat Shock Protein 27 (Hsp27) in the Rat Gingiva and its Changes with Tooth Eruption

Sasaki

Yamada

Inoue

et al. 2011

Acta Histochem. Cytochem

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Heat shock protein 27 kDa (Hsp27) functions as a molecular chaperon to prevent apoptosis as well as to contribute to the regulation of cell proliferation and differentiation during development. In the present study, the localization of Hsp27 in the oral epithelium of rats and its expression change during formation of the gingiva with the tooth eruption were examined immunohistochemically to elucidate the roles of Hsp27 in the oral mucosa.In adult rats, Hsp27-immunoreactivity was localized in the prickle and granular layers but absent in the basal and horny layers of the oral epithelium. On the other hand, in the outer and sulcular epithelia of the free gingival, Hsp27-immunoreactivity was detected in the whole layers, while it was not found in the proliferation zone of the junctional epithelium immunoreactive for Ki67. In immature rats on 10th postnatal day, Hsp27-immunoreactivity was intense in the prickle and granular layers of the oral epithelium, but was not detected in its basal layer. In rats at the eruptive phase on 15th postnatal day, Hsp27-immunoreactivity was detected in sites of the basal layer adjacent to where the dental cusps penetrated through the oral epithelium. Although the immunoreactivity for Ki67 was found in the basal layer of the oral epithelium, it was not localized in the Hsp27-immunopositive sites of tooth-penetration in the basal layer. Just after the tooth-eruption on 20th postnatal day, Hsp27-immunoreactivity was not found in the stratified squamous epithelium at the dentogingival junction, whereas it was intense in a single layer of cuboidal epithelial cells attached to the tooth neck. Ki67-positive cells were scattered in the stratified squamous epithelium at the dentogingival junction, whereas no positive cells were found in the portion of a single layer of cuboidal epithelial cells.These findings suggest that the outer and sulcular epithelia of the free gingiva have a relatively slower rate of proliferation than other gingival and oral epithelia, and that Hsp27 might inhibit the proliferation of the basal cells. Such specific phenomenon in the free gingiva occurred immediately after the dental cusps were exposed to the oral cavity.

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“…The 27-kD HSP (HSP27, small heat shock protein was originally named as HSP25 in mice; in this manuscript the molecule will be termed HSP27) form large oligomers that can act as molecular chaperones and can protect cells from heat shock and oxidative stress in vitro . Also, expression of HSP27 is reduced or absent in basal cell carcinoma (BCC), squamous cell carcinoma (SCC) and other malignancies arising from keratinocytes, suggesting that the lack of HSP27 might be a marker of epidermal malignancy (7, 8). Another relevant HSP family is the 70-kD family.…”

Section: Introductionmentioning

confidence: 99%

Heat Shock Proteins HSP27 and HSP70 Are Present in the Skin and Are Important Mediators of Allergic Contact Hypersensitivity

Yusuf

Nasti²,

Huang³

et al. 2009

The Journal of Immunology

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Proteomic analysis of murine skin has shown that a variety of heat shock proteins (HSPs) are constitutively expressed in the skin. Using murine allergic contact hypersensitivity as a model, we investigated the role of two heat shock proteins – HSP27 and HSP70 – in the induction of cutaneous cell-mediated immune responses. Immunohistochemical examination of skin specimens showed that HSP27 was present in the epidermis and HSP70 was present in both the epidermis and dermis. Inhibition of HSP27 and HSP70 produced a reduction in the DNFB contact hypersensitivity response and resulted in the induction of antigen specific unresponsiveness. Treatment of dendritic cell cultures with recombinant HSP27 caused in the upregulation of IL-1β, TNF-α, IL-6, IL-12p70 and IL-12p40 but not IL-23p19, which was inhibited when antibodies to HSP27 were added. DNFB conjugated dendritic cells that had been treated with HSP27 had an increased capacity to initiate contact hypersensitivity responses compared to control dendritic cells. This augmented capacity required TLR4 signaling because neither cytokine production by dendritic cells nor the increased induction of contact hypersensitivity responses occurred in TLR4 deficient C3H/HeJ mice. Our findings indicate that a cascade of events occurs following initial interaction of hapten with the skin that includes increased activity of heat shock proteins, their interaction with TLR4 and, in turn, increased production of cytokines that are known to enhance antigen presentation by T-cells. The results suggest that heat shock proteins form a link between adaptive and innate immunity during the early stages of contact hypersensitivity.

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Expression of a Small Heat Shock Protein 27 (HSP27) in Mouse Skin Tumors Induced by UVB-Irradiation.

Cited by 19 publications

References 25 publications

Heat shock proteins in animal neoplasms and human tumours—a comparison

Heat shock proteins in animal neoplasms and human tumours—a comparison

Localization of Heat Shock Protein 27 (Hsp27) in the Rat Gingiva and its Changes with Tooth Eruption

Heat Shock Proteins HSP27 and HSP70 Are Present in the Skin and Are Important Mediators of Allergic Contact Hypersensitivity

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