scholarly journals Influence of Heating and Cyclic Tension on the Induction of Heat Shock Proteins and Bone-Related Proteins by MC3T3-E1 Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-16 ◽  
Author(s):  
Eunna Chung ◽  
Alana Cherrell Sampson ◽  
Marissa Nichole Rylander
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tensile Stress ◽  
Bone Cells ◽  
Cyclic Strain ◽  
Fold Increase ◽  
Shock Proteins ◽  
Related Proteins ◽  
The Impact

Stress conditioning (e.g., thermal, shear, and tensile stress) of bone cells has been shown to enhance healing. However, prior studies have not investigated whether combined stress could synergistically promote bone regeneration. This study explored the impact of combined thermal and tensile stress on the induction of heat shock proteins (HSPs) and bone-related proteins by a murine preosteoblast cell line (MC3T3-E1). Cells were exposed to thermal stress using a water bath (44°C for 4 or 8 minutes) with postheating incubation (37°C for 4 hours) followed by exposure to cyclic strain (equibiaxial 3%, 0.2 Hz, cycle of 10-second tensile stress followed by 10-second rest). Combined thermal stress and tensile stress induced mRNA expression of HSP27 (1.41 relative fold induction (RFI) compared to sham-treated control), HSP70 (5.55 RFI), and osteopontin (1.44 RFI) but suppressed matrix metalloproteinase-9 (0.6 RFI) compared to the control. Combined thermal and tensile stress increased vascular endothelial growth factor (VEGF) secretion into the culture supernatant (1.54-fold increase compared to the control). Therefore, combined thermal and mechanical stress preconditioning can enhance HSP induction and influence protein expression important for bone tissue healing.

Effects of Growth Factors and Stress Conditioning on the Induction of Heat Shock Proteins and Osteogenesis

2009 ◽  
Author(s):  
Eunna Chung ◽  
Marissa Nichole Rylander
Keyword(s):  
Tissue Engineering ◽  
Growth Factors ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tensile Stress ◽  
Bone Regeneration ◽  
Tissue Regeneration ◽  
Stress Conditioning ◽  
Shock Proteins ◽  
Related Proteins

Tissue engineering is an emerging field that focuses on development of methods for repairing and regenerating damaged or diseased tissue. Successful development of engineered tissues is often limited by insufficient cellular proliferation and insufficient formation of extracellular matrix. To induce effective bone regeneration, many research groups have investigated the cellular response and capability for tissue regeneration associated with bioreactor conditions and addition of growth factors [1]. Bioreactors in tissue engineering have been developed to expose cells to a similar stress environment as found within the body or induce elevated stress levels for potential induction of specific cellular responses associated with tissue regeneration. Native bone encounters a diverse array of dynamic stresses such as shear, tensile, and compression daily. Stress conditioning protocols in the form of thermal or tensile stress have been shown to induce up-regulation of molecular chaperones called heat shock proteins (HSPs) and bone-related proteins like MMP13 (matrix metallopeptidase 13) [2] and OPG (osteoprotegerin) [3, 4]. HSPs have important roles in enhancing cell proliferation and collagen synthesis. Osteogenic growth factors such as TGF-β1 (transforming growth factor beta 1) and BMP-2 (bone morphogenetic protein 2) are related to bone remodeling and osteogenesis as well as HSP induction [5]. Therefore, identification of effective preconditioning using growth factors and stress protocols that enhance HSP expression could substantially advance development of bone regeneration. The purpose of this research was to identify preconditioning protocols using osteogenic growth factors and tensile stress applied through a bioreactor system to enhance expression of HSPs and bone-related proteins while minimizing cellular injury for ultimate use for bone regeneration.

scholarly journals Expression pattern of heat shock proteins during acute thermal stress in the Antarctic sea urchin, Sterechinus neumayeri

2016 ◽  
Vol 89 (1) ◽  
Author(s):  
Karina González ◽  
Juan Gaitán-Espitia ◽  
Alejandro Font ◽  
César A. Cárdenas ◽  
Marcelo González-Aravena
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Expression Pattern ◽  
Sea Urchin ◽  
Sterechinus Neumayeri ◽  
Shock Proteins ◽  
The Antarctic

scholarly journals Small heat shock proteins target mutant cystic fibrosis transmembrane conductance regulator for degradation via a small ubiquitin-like modifier–dependent pathway

2013 ◽  
Vol 24 (2) ◽  
pp. 74-84 ◽  
Author(s):  
Annette Ahner ◽  
Xiaoyan Gong ◽  
Bela Z. Schmidt ◽  
Kathryn W. Peters ◽  
Wael M. Rabeh ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Airway Epithelial Cells ◽  
Small Heat Shock Proteins ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Shock Proteins ◽  
The Impact ◽  
Cystic Fibrosis Transmembrane

Small heat shock proteins (sHsps) bind destabilized proteins during cell stress and disease, but their physiological functions are less clear. We evaluated the impact of Hsp27, an sHsp expressed in airway epithelial cells, on the common protein misfolding mutant that is responsible for most cystic fibrosis. F508del cystic fibrosis transmembrane conductance regulator (CFTR), a well-studied protein that is subject to cytosolic quality control, selectively associated with Hsp27, whose overexpression preferentially targeted mutant CFTR to proteasomal degradation. Hsp27 interacted physically with Ubc9, the small ubiquitin-like modifier (SUMO) E2 conjugating enzyme, implying that F508del SUMOylation leads to its sHsp-mediated degradation. Enhancing or disabling the SUMO pathway increased or blocked Hsp27’s ability to degrade mutant CFTR. Hsp27 promoted selective SUMOylation of F508del NBD1 in vitro and of full-length F508del CFTR in vivo, which preferred endogenous SUMO-2/3 paralogues that form poly-chains. The SUMO-targeted ubiquitin ligase (STUbL) RNF4 recognizes poly-SUMO chains to facilitate nuclear protein degradation. RNF4 overexpression elicited F508del degradation, whereas Hsp27 knockdown blocked RNF4’s impact on mutant CFTR. Similarly, the ability of Hsp27 to degrade F508del CFTR was lost during overexpression of dominant-negative RNF4. These findings link sHsp-mediated F508del CFTR degradation to its SUMOylation and to STUbL-mediated targeting to the ubiquitin–proteasome system and thereby implicate this pathway in the disposal of an integral membrane protein.

scholarly journals Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe

2015 ◽  
Vol 21 (2) ◽  
pp. 327-338 ◽  
Author(s):  
Attila Glatz ◽  
Ana-Maria Pilbat ◽  
Gergely L. Németh ◽  
Katalin Vince-Kontár ◽  
Katalin Jósvay ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Schizosaccharomyces Pombe ◽  
Stress Management ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress.

1993 ◽  
Vol 120 (3) ◽  
pp. 639-645 ◽  
Author(s):  
R Klemenz ◽  
A C Andres ◽  
E Fröhli ◽  
R Schäfer ◽  
A Aoyama
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Eye Lens ◽  
Physiological Conditions ◽  
Normal Tissues ◽  
3T3 Fibroblasts ◽  
Shock Proteins ◽  
Related Proteins ◽  
Nih 3T3

Stress induces the synthesis of several large and small heat shock proteins (hsp's). Two related small hsp's, hsp25 and alpha B crystallin exist in mice. alpha B crystallin is an abundant protein in several tissues even in the absence of stress. Particularly high amounts accumulate in the eye lens. Here we show that hsp25 is likewise constitutively expressed in many normal adult tissues. In the absence of stress the protein is most abundant in the eye lens, heart, stomach, colon, lung, and bladder. The stress-independent expression pattern of the two small hsp's is distinct. In several tissues the amount of hsp25 exceeds that accumulating in NIH 3T3 fibroblasts in response to heat stress. hsp25, like alpha B crystallin, exists in a highly aggregated form in the eye lens. The expression of hsp25 and alpha B crystallin in normal tissues suggests an essential, but distinct function of the two related proteins under standard physiological conditions.

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