Heat-shock protein A8 restores sperm membrane integrity by increasing plasma membrane fluidity

Moein-Vaziri, Najmeh; Phillips, I.J; Smith, Simon; Almiñana, Carmen; Maside, Carolina; Gil, M.A.; Roca, Jordi; Rodríguez‐Martínez, H.; Holt, William V.; Pockley, A. Graham; Fazeli, Alireza

doi:10.1530/rep-13-0631

Cited by 45 publications

(32 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The repair of membrane damage is mediated via increase in sperm membrane fluidity. The ability of HSPA8 to influence membrane stability and fluidity, alongside its conserved nature among mammalian species, supports the idea that this protein protects sperm survival through membrane repair mechanisms (121). Ongoing studies are elucidating the mechanisms that are involved in these protective effects and their potential impact on reproductive success and potential.…”

Section: Extracellular Cell Stress Proteins In Cancermentioning

confidence: 77%

“…Hsc70 appears to interact with components of the sperm cell surface membrane (117,118) and exposure to Hsc70 prolongs the survival of boar, bull and ram sperm (117,120). Studies have now shown that a recombinant form of Hsc70 (HSPA8) rapidly promotes the viability of uncapacitated spermatozoa, the ability of spermatozoa to bind to oviductal epithelial cells, enhances the performance of in vitro fertilisation procedures, and decreases sperm mitochondrial activity (121). The repair of membrane damage is mediated via increase in sperm membrane fluidity.…”

Section: Extracellular Cell Stress Proteins In Cancermentioning

confidence: 99%

See 1 more Smart Citation

Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview

Pockley

Henderson

2017

Phil. Trans. R. Soc. B

117

View full text Add to dashboard Cite

Contribution to a theme issue 'Heat shock proteins in health and disease: integrating knowledge to better understand the role of heat shock proteins as therapeutic targets and disease modulators' Keywords:Heat shock (stress) proteins, extracellular, immunity Author for correspondence:A. Graham Pockley, PhD e-mail: graham.pockley@ntu.ac.ukHeat shock proteins in health and disease: integrating knowledge to better understand the role of heat shock proteins as therapeutic targets and disease modulators 2 | P a g e Abstract Extracellular cell stress proteins are highly conserved phylogenetically and have been shown to act as powerful signalling agonists and receptors for selected ligands in several different settings. They also act as immunostimulatory "danger signals" for the innate and adaptive immune systems. Other studies have shown that cell stress proteins and the induction of immune reactivity to self-cell stress proteins can attenuate disease processes. Some proteins (e.g. Hsp60, Hsp70, gp96) exhibit both inflammatory and anti-inflammatory properties, depending on the context in which they encounter responding immune cells.The burgeoning literature reporting the presence of stress proteins in a range of biological fluids in healthy individuals / non-diseased settings, the association of extracellular stress protein levels with a plethora of clinical and pathological conditions and the selective expression of a membrane form of Hsp70 on cancer cells now supports the concept that extracellular cell stress proteins are involved in maintaining / regulating organismal homeostasis and in disease processes and phenotype. Cell stress proteins therefore form a biologically complex extracellular cell stress protein network having diverse biological, homeostatic and immunomodulatory properties, the understanding of which offers exciting opportunities for delivering novel approaches to predict, identify, diagnose, manage and treat disease.Heat shock proteins in health and disease: integrating knowledge to better understand the role of heat shock proteins as therapeutic targets and disease modulators 3 | P a g e 1. Background 'Chance favours the prepared mind ' -Louis Pasteur (1822 -1895 The presence of additional new 'puffs' in the polytene chromosomes of cultured Drosophila larva which were induced following their incubation at an inadvertently high temperature and observed by Ferruccio Ritossa (25 th February 1936 -9 th January 2014) in the early 1960s was unexpected and puzzling. He realised the potential importance of this first evidence that stress can influence gene transcription and induce the synthesis of new proteins, yet found it surprisingly difficult to publish this discovery. It was eventually published in Experientia (1, 2).Ritossa's findings were extended and expanded upon during the next decade and by the mid-to-late 1960s it was clear that exposure of cells containing polytene chromosomes to a variety of environmental stressors resulted in the transcription of novel genes and, presumably, in the synthesi...

show abstract

Section: Extracellular Cell Stress Proteins In Cancermentioning

confidence: 77%

Section: Extracellular Cell Stress Proteins In Cancermentioning

confidence: 99%

Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview

Pockley

Henderson

2017

Phil. Trans. R. Soc. B

117

View full text Add to dashboard Cite

show abstract

“…The recombinant HSPA8 used in this study was prepared at the University of Sheffield's laboratory; the preparation and purification method has been described in detail by Moein-Vaziri et al [10]. An aliquot of the protein, dissolved in PBS and stored at À80 C, was thawed, diluted in more PBS to achieve the concentrations required by the experimental designs, and stored at À20 C before use.…”

Section: Source Of Heat Shock Protein A8mentioning

confidence: 99%

“…Although it often functions at the intracellular level, it has also been detected in the extracellular space, where it exerts protective effects on cell viability, apparently possessing both proapoptotic and antiapoptotic properties depending on the situation [3,4]. Within the context of sperm biology, recent studies have shown that HSPA8 is produced by oviductal epithelial cells during sperm transport [5,6] and enhances boar, ram, and bull sperm survival [7][8][9][10] in vitro.…”

Section: Introductionmentioning

confidence: 99%

“…The mechanisms involved in the protection of spermatozoa by HSPA8 remain somewhat unclear, but detailed studies have shown both a dependence on the presence of membrane cholesterol and that the protein increases plasma membrane fluidity provided the spermatozoa uncapacitated [10]. Moreover, extracellular HSPA8 acts as a cell signaling molecule in many situations [11][12][13], and among other properties, it is known to increase intracellular cAMP concentrations in boar spermatozoa.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Heat shock protein A8 stabilizes the bull sperm plasma membrane during cryopreservation: Effects of breed, protein concentration, and mode of use

Holt¹,

Valle²,

Fazeli³

2015

Theriogenology

View full text Add to dashboard Cite

Viable and morphologically normal boar spermatozoa alter the expression of heat‐shock protein genes in oviductal epithelial cells during co‐culture in vitro

Yeste

Holt

Bonet

et al. 2014

Molecular Reproduction Devel

View full text Add to dashboard Cite

The principal aim of this study was to determine if boar spermatozoa influence the expression of four selected chaperone and heat-shock protein (HSP) genes-namely clusterin (CLU), HSP90AA1, HSPA5, and HSPA8-in oviductal epithelial cells (OECs) during in vitro co-culture. All corresponding proteins of these genes were previously identified in a sperm-interacting, 70-kDa soluble fraction derived from apical plasma membranes of OECs. The present study also sought to determine whether or not: (i) spermatozoa must directly bind to OEC for an effect on gene expression to be elicited and (ii) reproductive and nonreproductive epithelial cell types (LLC-PK1, pig kidney) respond equivalently, in terms of alterations in chaperone and HSP gene expression, during co-culture with sperm. Spermatozoa induced a significant upregulation (P < 0.05) in HSP90AA1 and HSPA5 in OECs after 3 hr, and in HSPA8 after 6 hr of co-culture when they were in direct contact with epithelial cells. Conversely, no upregulation of HSP transcription was observed when spermatozoa did not directly bind to OECs. Spermatozoa also induced a significant upregulation (P < 0.05) of the same three genes when in direct contact with LLC-PK1 cells, but the timing occurred later than with OECs. Interestingly, the extent of HSP gene upregulation induced by direct contact of spermatozoa with epithelial cells was dependent on sperm-binding index and on the viability and morphological quality of the bound sperm population. In conclusion, the upregulation of HSP genes caused by direct contact between spermatozoa and OECs, rather than nonreproductive epithelial cells, suggests HSPs could play an integral role in the modulation of sperm function in the oviductal reservoir.

show abstract

Heat-shock protein A8 restores sperm membrane integrity by increasing plasma membrane fluidity

Cited by 45 publications

References 50 publications

Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview

Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview

Heat shock protein A8 stabilizes the bull sperm plasma membrane during cryopreservation: Effects of breed, protein concentration, and mode of use

Viable and morphologically normal boar spermatozoa alter the expression of heat‐shock protein genes in oviductal epithelial cells during co‐culture in vitro

Contact Info

Product

Resources

About