scholarly journals Sperm activation by heat shock protein 70 supports the migration of sperm released from sperm storage tubules in Japanese quail (Coturnix japonica)

Reproduction ◽  
2014 ◽  
Vol 147 (2) ◽  
pp. 167-178 ◽  
Author(s):  
Gen Hiyama ◽  
Mei Matsuzaki ◽  
Shusei Mizushima ◽  
Hideo Dohra ◽  
Keisuke Ikegami ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Sperm Motility ◽  
Heat Shock Protein 70 ◽  
Sperm Storage ◽  
Female Reproductive Tract ◽  
Voltage Dependent Anion Channel ◽  
Sperm Surface ◽  
Recombinant Hsp70 ◽  
Sperm Storage Tubules

Systems for maintaining the viability of ejaculated sperm in the female reproductive tract are widespread among vertebrates and invertebrates. In birds, this sperm storage function is performed by specialized simple tubular invaginations called sperm storage tubules (SSTs) in the uterovaginal junction (UVJ) of the oviduct. Although the incidence and physiological reasons for sperm storage in birds have been reported extensively, the mechanisms of sperm uptake by the SSTs, sperm maintenance within the SSTs, and control of sperm release from the SSTs are poorly understood. In this study, we demonstrated that the highly conserved heat shock protein 70 (HSP70) stimulates sperm motility in vitro and also that HSP70 expressed in the UVJ may facilitate the migration of sperm released from the SSTs. Quantitative RT-PCR analysis demonstrated that the expression of HSP70 mRNA in the UVJ increases before ovulation/oviposition. Gene-specific in situ hybridization and immunohistochemical analysis with a specific antibody to HSP70 demonstrated that HSP70 is localized in the surface epithelium of the UVJ. Furthermore, injection of anti-HSP70 antibody into the vagina significantly inhibited fertilization in vivo. In addition, we found that recombinant HSP70 activates flagellar movement in the sperm and that the binding of recombinant HSP70 to the sperm surface is mediated through an interaction with voltage-dependent anion channel protein 2 (VDAC2). Our results suggest that HSP70 binds to the sperm surface by interacting with VDAC2 and activating sperm motility. This binding appears to play an important role in sperm migration within the oviduct.

Exogenous heat shock protein-70 inhibits cigarette smoke-induced intimal thickening

2008 ◽  
Vol 295 (4) ◽  
pp. R1320-R1327 ◽  
Author(s):  
Michiaki Matsumoto ◽  
Paul C. Dimayuga ◽  
Charles Wang ◽  
Jonathan Kirzner ◽  
Miha Cercek ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cigarette Smoke ◽  
Heat Shock Protein 70 ◽  
Nuclear Antigen ◽  
Cigarette Smoke Exposure ◽  
Hsp70 Expression ◽  
Intimal Thickening ◽  
Hsp70 Mrna ◽  
Recombinant Hsp70

Cigarette smoke is associated with increased carotid intimal thickening or stroke. Preliminary work showed that exposure to smoke resulted in a 4.5-fold reduction of heat shock protein-70 (HSP70) expression in spleens of mice using gene microarray analysis. In the current study, we investigated the role of extracellular HSP70 in carotid intimal thickening of mice exposed to cigarette smoke. Intimal thickening was induced by placement of a cuff around the right carotid artery of mice. Cuff injury resulted in increased HSP70 mRNA expression in carotid arteries that persisted for 21 days. Cigarette smoke exposure decreased arterial HSP70 expression and significantly increased intimal thickening compared with mice exposed to air. Treatment of mice exposed to cigarette smoke with intravenous recombinant HSP70 attenuated intimal thickening through reduced phosphorylated extracellular signal-regulated kinase (pERK) expression in the arterial wall. In vitro experiments with rat aortic smooth muscle cells confirmed that recombinant HSP70 decreases pERK and proliferating cell nuclear antigen (PCNA) expression in cells exposed to cigarette smoke extract and H2O2. Our study suggests that decreased expression of arterial HSP70 is an important mechanism by which exposure to cigarette smoke augments intimal thickening. The effects of recombinant HSP70 suggest a role for extracellular HSP70.

scholarly journals Flagellin Contamination of Recombinant Heat Shock Protein 70 Is Responsible for Its Activity on T Cells

2006 ◽  
Vol 282 (7) ◽  
pp. 4479-4484 ◽  
Author(s):  
Zhiyong Ye ◽  
Yunn-Hwen Gan
Keyword(s):  
Escherichia Coli ◽  
T Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Burkholderia Pseudomallei ◽  
Jurkat T Cells ◽  
Recombinant Hsp70 ◽  
Shock Proteins

Heat shock proteins (Hsp) 60 and 70 have been intensively studied for their ability to activate innate immunity. Heat shock proteins had been shown to induce the activation of dendritic cells, T cells, and B cells. However, the possible contamination of endotoxin in heat shock protein preparations makes their function as an activator of immune system ambiguous. Here, we examined the ability of bacterial Hsp60 and Hsp70 to activate Jurkat T cells and primary T cells. We found that Burkholderia pseudomallei Hsp70 and Mycobacterium tuberculosis Hsp70 could costimulate Jurkat T cells to make IL-2 and signal through TLR5. This costimulatory activity is not due to endotoxin or contaminants signaling via TLR2 nor TLR4. However, recombinant Hsp70 expressed in Escherichia coli ΔfliC strain completely lost its ability to costimulate T cells. Thus, the activation of T cells by recombinant Hsp70 is ascribed to flagellin contamination.

Ammonia aggravates emotional stress-induced gastric mucosal oxidative injury through the cancellation of heat shock protein 70 (HSP70)

2001 ◽  
Vol 120 (5) ◽  
pp. A152-A152
Author(s):  
H SUZUKI ◽  
S NAGAHASHI ◽  
M MIYAZAWA ◽  
M MORI ◽  
H NAGATA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Emotional Stress ◽  
Heat Shock Protein 70 ◽  
Oxidative Injury
Sign in / Sign up

Export Citation Format

Share Document