Expression of Heat Shock Proteins in Mouse Skin During Wound Healing

Laplante, Alain; Moulin, Véronique J.; Auger, François A.; Landry, Jacques; Li, Hui; Morrow, Geneviève; Tanguay, Robert M.; Germain, Lucie

doi:10.1177/002215549804601109

Cited by 160 publications

(131 citation statements)

References 77 publications

(92 reference statements)

Supporting

Mentioning

114

Contrasting

Unclassified

Order By: Relevance

“…During mouse embryonic development, Hsp27 is transiently expressed at the onset of myogenic differentiation in the cardiac primordium and in the myotomes (Gernold et al, 1993;Loones et al, 1997), as well as in certain neurons of the central nervous system (Gernold et al, 1993;Arrigo and Mehlen, 1994). Also, the expression of Hsp27 in some renewing cell populations of adult mice and rats, including chondrocytes of the growth plate (Tiffee et al, 2000), keratinocytes of the epidermis and other stratified squamous epithelia (Laplante et al, 1998;Wakayama and Iseki, 1998), and testicular germ cells (Wakayama and Iseki, 1999) is indicative of the involvement of Hsp27 in cell differentiation. In the present study, we have demonstrated a transient expression of Hsp27 in the differentiating acinar components of rat submandibular gland during postnatal development, providing further in vivo evidence for the role of Hsp27 in cellular transition from proliferation to differentiation.…”

Section: Discussionmentioning

confidence: 99%

Transient occurrence of 27 kDa heat‐shock protein in the terminal tubule cells during postnatal development of the rat submandibular gland

et al. 2001

View full text Add to dashboard Cite

It has been suggested that the 27 kDa heat-shock protein (Hsp27) plays a role at crucial cellular checkpoints for proliferation, apoptosis, and differentiation. We examined the immunolocalization of Hsp27 in the rat submandibular gland during postnatal development, wherein acinar cells proliferate and differentiate at earlier postnatal periods. At 2 weeks of age, weak Hsp27 immunoreactivity was distributed diffusely over all gland components. At 3 weeks, Hsp27 immunoreactivity disappeared in most parts of the acini and ducts, but was intensely accumulated in a small cell population located in the acinar center. This population was composed mostly of terminal tubule (TT) type I cells. At 4 weeks, the Hsp27-immunopositive cell population in the acinar center was composed primarily of immature (type II) acinar cells, partly of immature (granulated) intercalated duct (ID) cells, and occasionally of apoptotic cells. After 5 weeks, all acinar components became mature and were no longer immunoreactive for Hsp27. When acinar cell differentiation was accelerated by administration of isoproterenol to 3-week-old rats for 7 days, the number of Hsp27-positive cells was significantly lower than in the control gland at 4 weeks, confirming that Hsp27 expression is downregulated in mature acinar cells. These results suggest that at around 3-4 weeks in postnatal development, the centroacinar TT cells stop proliferating and begin to differentiate into acinar and ID cells, and occasionally undergo apoptosis. Hsp27 is transiently expressed in the centroacinar TT cells during this critical period, and thus may play a role in their differentiation into the immediate descendants. Anat Rec 264: 358 -366, 2001. Key words: small heat-shock protein; submandibular gland; terminal tubule cell; differentiation; immunohistochemistry; electron microscopy; rat (Wistar)The heat-shock proteins (HSPs) are highly conserved proteins in organisms ranging from prokaryotes to mammals which are induced by various physicochemical stresses and act in cellular protection (Lindquist and Craig, 1988). Moreover, HSPs are produced in significant amounts in a variety of nonstressed cells, implying a physiological role for these proteins in normal cell functions. HSPs have been classified into several families based on their molecular weights. The 27 kDa heat-shock protein (Hsp27) of rats and humans, and its mouse homolog Hsp25, belong to the family of small (20 -30 kDa) HSPs

show abstract

Section: Discussionmentioning

confidence: 99%

Transient occurrence of 27 kDa heat‐shock protein in the terminal tubule cells during postnatal development of the rat submandibular gland

et al. 2001

View full text Add to dashboard Cite

show abstract

“…In addition, it has been reported that hsp70 and hsp90 are constitutively expressed in the epidermis. 104,105 These two heat-shock proteins are both able to inhibit the apoptosome formation, 106,107 and hsp70 can also antagonize the proapoptotic effects of apoptosis-inducing factor. 108 Overexpression of hsp70 can prevent UVB-induced apoptosis in an epidermal carcinoma line, 109 and hsp70-deficient mice are more susceptible to UVB-induced apoptosis.…”

Section: Mitochondrial Factors and Apoptosome Formationmentioning

confidence: 99%

Death penalty for keratinocytes: apoptosis versus cornification

et al. 2005

View full text Add to dashboard Cite

Homeostasis implies a balance between cell growth and cell death. This balance is essential for the development and maintenance of multicellular organisms. Homeostasis is controlled by several mechanisms including apoptosis, a process by which cells condemned to death are completely eliminated. However, in some cases, total destruction and removal of dead cells is not desirable, as when they fulfil a specific function such as formation of the skin barrier provided by corneocytes, also known as terminally differentiated keratinocytes. In this case, programmed cell death results in accumulation of functional cell corpses. Previously, this process has been associated with apoptotic cell death. In this overview, we discuss differences and similarities in the molecular regulation of epidermal programmed cell death and apoptosis. We conclude that despite earlier confusion, apoptosis and cornification occur through distinct molecular pathways, and that possibly antiapoptotic mechanisms are implicated in the terminal differentiation of keratinocytes.

show abstract

“…Since TAMs show enhanced activity upon activation hsp70, as our observations confirm, this might be preactivated or raged macrophages, which could be of relevance in immunotherapeutic protocols against malignancies. Normally, most of the hsp70 that are constitutively synthesized and localized in the cytosol are expressed and induced in inflammatory conditions (28)(29)30) such as in malignancies and other diseases. Necrosis of these inflamed cells provides highly local concentration ofhsp70 in extra cellular microenvironment for stimulation of an immune response.…”

Section: Effect Ofh~p 70 On Inos Gene Expressionmentioning

confidence: 99%

HSP70 Modulates the Enhanced Production of Reactive Intermediate Metabolites and a Proinflammatory Cytokine TNF-α Expression in a T Cell Lymphoma

2006

View full text Add to dashboard Cite

Heat shock proteins are intracellular soluble proteins expressed consecutively in all cells. They are immunogenic proteins able to activate antigen-presenting cells by binding through the CD91 receptor and activate both CD4+ and CD8+ T-cells. Macrophage plays a pivotal role in innate immune response and secretes a number of regulatory molecules upon activation. In the present study, we investigate the activation of normal and tumor-associated macrophage to produce the effector molecules which have a role in immunomodulation, especially in the killing of the transformed or tumor cells. In vitro and in vivo treatment of NMO and TAMs (from T-Cell Lymphoma) with optimum dose 10 μg of hsp70 produce effector molecules such as nitric oxide (NO), hydrogen peroxide (H2O2) and tumor necrosis factor-α (TNF α). The results of our experiments reveal that the production of effector molecules is dose-dependent, and the result of immunoblots also confirms the increased expression of iNOS. These findings suggest that autologous hsp70 are highly immunogenic and potent activating agents for the enhanced production of effector molecules in NMO and TAMs in a T-cell lymphoma.

show abstract

Expression of Heat Shock Proteins in Mouse Skin During Wound Healing

Cited by 160 publications

References 77 publications

Transient occurrence of 27 kDa heat‐shock protein in the terminal tubule cells during postnatal development of the rat submandibular gland

Transient occurrence of 27 kDa heat‐shock protein in the terminal tubule cells during postnatal development of the rat submandibular gland

Death penalty for keratinocytes: apoptosis versus cornification

HSP70 Modulates the Enhanced Production of Reactive Intermediate Metabolites and a Proinflammatory Cytokine TNF-α Expression in a T Cell Lymphoma

Contact Info

Product

Resources

About