Heat‐shock protein 70 expression in the equine cornea

Peterson, Curt M.; Driskell, Elizabeth A.; Wilkie, David A.; Premanandan, Christopher; Hamor, Ralph E.

doi:10.1111/vop.12432

Cited by 3 publications

(2 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HSPs are ubiquitous proteins that serve critical functions in the response to biotic and abiotic stresses (24). A previous study by Peterson et al (25) demonstrated that HSPs promote epithelial wound healing in various tissues, whereas reduced HSP70 expression may potentially prolong the healing process in the pathologic cornea of animals. Certain HSP70s, including molecular chaperones, serve a pivotal function in various biological processes, including the regulation of protein folding, interactions between proteins and translocation and degradation across membranes (26).…”

Section: Discussionmentioning

confidence: 97%

Thermal pretreatment promotes the protective effect of HSP70 against tendon adhesion in tendon healing by increasing HSP70 expression

2019

View full text Add to dashboard Cite

Tendon adhesion is a substantial challenge for tendon repair. Thermal pretreatment (TP) may decrease inflammation by upregulating heat shock proteins (HSPs). The present study intends to identify the function that TP serves when combined with HSP70 overexpression in tendon healing and adhesion in rats. Sprague-Dawley male rats were used to establish a surgically ablative tendon postoperative suture model, and the positive expression of the HSP70 protein was measured using immunohistochemistry. Changes to the blood vessels and collagenous fiber, in addition to the maximum tensile strength and the tendon sliding distance, were detected under a microscope. Finally, HSP70, tumor growth factor β (TGF-β), and insulin-like growth factor 1 (IGF-1) mRNA and protein levels were all determined by employing reverse transcription-quantitative polymerase chain reaction and western blot analysis methods. The positive expression of the HSP70 protein increased following TP. Furthermore, TP reduced the infiltration of inflammatory cells and improved the collagenous arrangement, accompanied by an increased maximum tensile force and tendon gliding distance following surgery. In addition, TP increased the mRNA and protein expression levels of HSP70, TGF-β and IGF-1. Altogether, TP increases HSP70 expression, thereby reducing postoperative traumatic inflammation and establishing tendon adhesion and promoting tendon healing. Thus, TP may be a potential strategy for the treatment of tendon adhesion.

show abstract

Section: Discussionmentioning

confidence: 97%

Thermal pretreatment promotes the protective effect of HSP70 against tendon adhesion in tendon healing by increasing HSP70 expression

2019

View full text Add to dashboard Cite

show abstract

“…In the horse, two HSP90 isoforms (HSP90α and HSP90β) have been described (Pratt, 1997), encoded by the HSP90AB1 gene (César Cortés‐González, Ramírez‐González, Ariza, & Bobadilla, 2008). This gene is expressed in cerebellum, testis, embryo, cornea, blood and muscle (Coleman, Zeng, Hestand, Liu, & Macleod, 2013; Peterson, Driskell, Wilkie, Premanandan, & Hamor, 2017; Avenatti, McKeever, Horohov, & Malinowski, 2018).…”

Section: Introductionmentioning

confidence: 99%

Heat shock protein HSP90 immunoexpression in equine endometrium during oestrus, dioestrus and anoestrus

Benítez

Vasconcellos

Lombide

et al. 2020

Anat Histol Embryol

View full text Add to dashboard Cite

Heat shock proteins play a crucial role in cellular development, proliferation, differentiation and apoptosis. Heat shock protein 90 (HSP90) has been localised in the human endometrium, where its immunoexpression changes during the menstrual cycle. Similar studies have not been done for the equid species, so the present study aimed to describe endometrial HSP90 immunoexpression in mare endometrium. Endometrial biopsies were formalin‐fixed and paraffin‐embedded, and sections were stained with haematoxylin–eosin in preparation for HSP90 immunohistochemistry. Immunostaining and morphometric analyses were performed on the epithelial lining, endometrial glands and connective stroma during oestrus, dioestrus phase and anoestrus period (n = 7 per phase or period). Immunoexpression was localised in the basal region of the epithelial cells lining the lumen. Immunoexpression was greater during oestrus than during either dioestrus or anoestrus. During anoestrus, there was little immunostaining in the endometrium, suggesting that HSP90 is involved in the functional modulation of sex steroid receptors in cyclic mares. Indeed, the function of HSP90 as a chaperone in the folding of proteins, such as steroid receptors, might explain the greater intensity of immunostaining during the oestrus and dioestrus phases, compared the anoestrus period. We conclude that, in the mare, HSP90 plays a role in endometrial function and that further studies are needed to test whether it is important in pathological conditions as endometritis.

show abstract

Effects of water-filtered infrared A and visible light (wIRA/VIS) radiation on heat- and stress-responsive proteins in the retina and cornea of guinea pigs

Frohns¹,

Stojanović²,

Barisani-Asenbauer³

et al. 2021

Journal of Photochemistry and Photobiology B: Biology

View full text Add to dashboard Cite

Heat‐shock protein 70 expression in the equine cornea

Abstract: These findings suggest the expression of HSP70 is induced in the normal equine cornea during re-epithelialization and may be altered in sterile keratopathies.

Cited by 3 publications

References 21 publications

Thermal pretreatment promotes the protective effect of HSP70 against tendon adhesion in tendon healing by increasing HSP70 expression

Thermal pretreatment promotes the protective effect of HSP70 against tendon adhesion in tendon healing by increasing HSP70 expression

Heat shock protein HSP90 immunoexpression in equine endometrium during oestrus, dioestrus and anoestrus

Effects of water-filtered infrared A and visible light (wIRA/VIS) radiation on heat- and stress-responsive proteins in the retina and cornea of guinea pigs

Contact Info

Product

Resources

About