Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion

Favet, Noelle; Duverger, Olivier; Mt, Loones; Poliard, Anne; Kellermann, Odile; Morange, Michel

doi:10.1038/sj.cdd.4400847

Cited by 23 publications

(20 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Further evidence supporting this hypothesis has been obtained using ex vivo approaches (Spector et al 1994;Mehlen et al 1997;Davidson and Morange 2000;Favet et al 2001;Duverger et al 2004). Skin is one of the organs containing high levels of Hsp25, both in the adult and during embryonic development.…”

Section: Introductionmentioning

confidence: 68%

Heat shock protein 25 plays multiple roles during mouse skin development

Duverger¹,

Morange²

2005

Cell Stress Chaper

View full text Add to dashboard Cite

Heat shock protein (Hsp) 25 is a member of the small Hsp family. High levels of Hsp25 can be detected in skin. During adult epidermis differentiation, the concentration of Hsp25 increases as the distance of keratinocytes from the basal layer increases, in parallel with the extent of keratinization. We previously showed that Hsp25, mouse keratin (MK) 5, and MK14 participated in the formation of characteristic ring-shaped aggregates during the differentiation of the PAM212 keratinocyte cell line. We suggested that Hsp25 was involved in the disorganization of the MK5-MK14 keratin network before the establishment of the MK1-MK10 keratin network at the beginning of epidermis stratification. In this study, we have investigated the distribution of Hsp25 and keratins throughout skin development. We demonstrate that the distribution of Hsp25 and MK5 in the epidermis at the beginning of stratification and before keratinization is similar to that observed in PAM212 keratinocytes. These results indicate that there is a strong correlation between the mechanism we described ex vivo and the events taking place in vivo. Moreover, we show that Hsp25 is produced in different cell types in the epidermis and in the hair follicle at different stages of their development. Thus, our results suggest that Hsp25 is involved in more than one process during skin development.

show abstract

Section: Introductionmentioning

confidence: 68%

Heat shock protein 25 plays multiple roles during mouse skin development

Duverger¹,

Morange²

2005

Cell Stress Chaper

View full text Add to dashboard Cite

show abstract

“…Intriguingly, enhancing chondrocyte Hsp25 lowers growth rate, modifies morphology, lessens adhesion and disrupts differentiation, but leaves actin distribution unaffected. These observations have implications for metastatic potential as reduced adhesion leads to cell release from tumors and spreading throughout the organism [144].…”

Section: Shsps and Cancermentioning

confidence: 99%

The small heat shock proteins and their role in human disease

2005

View full text Add to dashboard Cite

Within the molecular chaperone family, sHSPs constitute a structurally divergent group characterized by a conserved sequence of 80-100 amino acid residues termed the a-crystallin domain [1][2][3][4][5][6][7][8]. The a-crystallin domain, duplicated in the unusual example of parasitic flatworms (Platyhelminthes) [9], is located toward a highly flexible, variable, C-terminal extension, and is usually preceded by a poorly conserved N-terminal region. The molecular mass of sHSP subunits ranges from 12 to 43 kDa, and they assemble into large, dynamic complexes up to 1 MDa. sHSP secondary structure is dominated by b-strands with limited a-helical content, and b-sheets within the a-crystallin domain mediate dimer formation. Crystallization of two sHSPs has contributed significantly to the description of oligomerization, quaternary structure, subunit exchange, and chaperone activity. Characterization of a highly conserved arginine is also an important outcome of crystallization and related studies because mutation of this residue has profound effects on sHSP function and contributes to certain diseases [10][11][12][13][14][15][16].The sHSPs are molecular chaperones, storing aggregation prone proteins as folding competent intermediates and conferring enhanced stress resistance on cells by suppressing aggregation of denaturing proteins, actions associated with oligomerization and subunit exchange [17][18][19][20]. Functional studies of the sHSPs are

show abstract

“…On the other hand, heterologous overexpression of sHSPs was reported to increase the tolerance of host cells against various stresses [16][17][18][19][20][21][22][23]. Physiologically, the sHSPs of animals, as exampled by fly Hsp22, mammalian aA-crystallin and aB-crystallin, mouse Hsp25, human Hsp27 and Hsp22, have been linked to cell differentiation [24], apoptosis [25], and longevity [26], and their dysfunction has been related to many diseases such as cancer development [27], cardiovascular diseases [28,29], cataracts [30], myopathy [31], and neuron diseases [32,33].…”

Section: Introductionmentioning

confidence: 99%

Chaperone function and mechanism of small heat-shock proteins

Fu¹

2014

ABBS

View full text Add to dashboard Cite

Small heat-shock proteins (sHSPs) are ubiquitous ATP-independent molecular chaperones that play crucial roles in protein quality control in cells. They are able to prevent the aggregation and/or inactivation of various non-native substrate proteins and assist the refolding of these substrates independently or under the help of other ATP-dependent chaperones. Substrate recognition and binding by sHSPs are essential for their chaperone functions. This review focuses on what natural substrate proteins an sHSP protects and how it binds the substrates in cells under fluctuating conditions. It appears that sHSPs of prokaryotes, although being able to bind a wide range of cellular proteins, preferentially protect certain classes of functional proteins, such as translation-related proteins and metabolic enzymes, which may well explain why they could increase the resistance of host cells against various stresses. Mechanistically, the sHSPs of prokaryotes appear to possess numerous multi-type substrate-binding residues and are able to hierarchically activate these residues in a temperature-dependent manner, and thus act as temperature-regulated chaperones. The mechanism of hierarchical activation of substrate-binding residues is also discussed regarding its implication for eukaryotic sHSPs.

show abstract

Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion

Cited by 23 publications

References 61 publications

Heat shock protein 25 plays multiple roles during mouse skin development

Heat shock protein 25 plays multiple roles during mouse skin development

The small heat shock proteins and their role in human disease

Chaperone function and mechanism of small heat-shock proteins

Contact Info

Product

Resources

About