Aquaporins and (in)fertility: More than just water transport

Ribeiro, João C.; Alves, Marco G.; Yeste, Marc; Cho, Yoon S.; Calamita, Giuseppe; Oliveira, Pedro F.

doi:10.1016/j.bbadis.2020.166039

Cited by 22 publications

(19 citation statements)

References 140 publications

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“…Spermatozoa from cockerels presented better viability and motility after controlled-rate slow freeze than vitrification [97]. Opposite to oocytes and embryos, sperm cells have highly permeable plasmatic membranes as well as small volume which prevents the formation of ice crystals during controlled-rate slow freezing cryopreservation [98]. Moreover, the use of high concentrations of CPAs characteristic of the vitrification process is toxic for sperm cells.…”

Section: Controlled-rated Slow Freezing Versus Vitrification: Advanta...mentioning

confidence: 99%

Aquaporins and Animal Gamete Cryopreservation: Advances and Future Challenges

Ribeiro

Carrageta

Bernardino

et al. 2022

Animals

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Cryopreservation is globally used as a method for long-term preservation, although freeze-thawing procedures may strongly impair the gamete function. The correct cryopreservation procedure is characterized by the balance between freezing rate and cryoprotective agents (CPAs), which minimizes cellular dehydration and intracellular ice formation. For this purpose, osmoregulation is a central process in cryopreservation. During cryopreservation, water and small solutes, including penetrating cryoprotective agents, cross the plasma membrane. Aquaporins (AQPs) constitute a family of channel proteins responsible for the transport of water, small solutes, and certain gases across biological membranes. Thirteen homologs of AQPs (AQP0-12) have been described. AQPs are widely distributed throughout the male and female reproductive systems, including the sperm and oocyte membrane. The composition of the male and female gamete membrane is of special interest for assisted reproductive techniques (ART), including cryopreservation. In this review, we detail the mechanisms involved in gamete cryopreservation, including the most used techniques and CPAs. In addition, the expression and function of AQPs in the male and female gametes are explored, highlighting the potential protective role of AQPs against damage induced during cryopreservation.

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Section: Controlled-rated Slow Freezing Versus Vitrification: Advanta...mentioning

confidence: 99%

Aquaporins and Animal Gamete Cryopreservation: Advances and Future Challenges

Ribeiro

Carrageta

Bernardino

et al. 2022

Animals

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“…Aquaporins (AQPs) are water channel molecules that are chiefly localized at plasma membrane in various cell types, including testis, efferent ductules, and epididymis in the male reproductive tract (Verkman & Mitra, 2000;Da Silva et al, 2006). AQPs have 6 membrane-spanning domains in structure and contribute to water movement across plasma membrane (Verkman & Mitra, 2000;Ribeiro et al, 2021). The AQPs have at least 13 isoforms in mammalian cells, and expression and localization of different types of AQPs in the male reproductive tract have been extensively examined (Da Silva et al, 2006;Ribeiro et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

“…AQPs have 6 membrane-spanning domains in structure and contribute to water movement across plasma membrane (Verkman & Mitra, 2000;Ribeiro et al, 2021). The AQPs have at least 13 isoforms in mammalian cells, and expression and localization of different types of AQPs in the male reproductive tract have been extensively examined (Da Silva et al, 2006;Ribeiro et al, 2021). AQPs are also capable of transporting ammonia or hydrogen peroxide, depending on types of AQPs (Da Silva et al, 2006;Ribeiro et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

“…The AQPs have at least 13 isoforms in mammalian cells, and expression and localization of different types of AQPs in the male reproductive tract have been extensively examined (Da Silva et al, 2006;Ribeiro et al, 2021). AQPs are also capable of transporting ammonia or hydrogen peroxide, depending on types of AQPs (Da Silva et al, 2006;Ribeiro et al, 2021). There are at least 8 types of AQPs expressing in the epididymis, and specific expression of different AQP types has been detected along the epididymis (Ribeiro et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

“…AQPs are also capable of transporting ammonia or hydrogen peroxide, depending on types of AQPs (Da Silva et al, 2006;Ribeiro et al, 2021). There are at least 8 types of AQPs expressing in the epididymis, and specific expression of different AQP types has been detected along the epididymis (Ribeiro et al, 2021). For examples, expression of AQP1 is found in smooth muscle and endothelial cells adjacent to epididymal epithelial cells (Brown et al, 1993), and AQP9 is exclusively localized at the apical microvilli of principal cells throughout the entire epididymal region (Pastor-Soler et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

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Expressional Modulation of Aquaporin 1 and 9 in the Rat Epididymis by an Anabolic-Androgenic Steroid, Nandrolone Decanoate

Lee¹

2021

Dev. Reprod.

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The spermatozoa become mature in the epididymis which is divided into initial segment and caput, corpus, and cauda epididymis. The water movement across the epididymal epithelium is important for creating luminal microenvironment for sperm maturation. Aquaporins (Aqps) are water channel proteins, and expression of Aqps is regulated by androgens. The current research was focused to examine expressional regulation of Aqp1 and Aqp9 by an androgenic-anabolic steroid, nandrolone decanoate (ND). The ND at the low dose (2 mg/ kg body weight/week) or high dose (10 mg) was subcutaneously administrated into male rats for 2 or 12 weeks. Transcript levels of Aqp1 and Aqp9 were determined by quantitative real-time polymerase chain reaction (PCR) analyses. In the initial segment, level of Aqp1 was decreased with 12 week-treatment, while Aqp9 level was decreased by the high dose treatment for 12 weeks. In the caput epididymis, Aqp9 expression was decreased by the low dose treatment. The 2 week-treatment resulted in an increase of Aqp1 level but a decrease of Aqp9 expression in the corpus epididymis. In the corpus epididymis, the 12 week-treatment at the low dose caused the reduction of Aqp1 and Aqp9 levels, but the high dose treatment resulted in an increase of Aqp1 expression and a decrease of Aqp9 level. In the cauda epididymis, Aqp1 expression was decreased by 2 and 12 week-treatments, while increases of Aqp9 levels was detected with the high dose treatment for 2 weeks and with 12 week-treatment. These findings indicate differential regulation of Aqp1 and Aqp9 expression among epididymal segments by ND.

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Aqp4a and Trpv4 mediate regulatory cell volume increase for swimming maintenance of marine fish spermatozoa

Castro-Arnau,

Chauvigné,

Toft-Bertelsen

et al. 2024

Cell. Mol. Life Sci.

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Volume regulation is essential for cell homeostasis and physiological function. Amongst the sensory molecules that have been associated with volume regulation is the transient receptor potential vanilloid 4 (TRPV4), which is a non-selective cation channel that in conjunction with aquaporins, typically controls regulatory volume decrease (RVD). Here we show that the interaction between orthologous AQP4 (Aqp4a) and TRPV4 (Trpv4) is important for regulatory volume increase (RVI) in post-activated marine fish spermatozoa under high osmotic stress. Based upon electrophysiological, volumetric, and in vivo and ex vivo functional experiments using the pharmacological and immunological inhibition of Aqp4a and Trpv4 our model suggests that upon ejaculation and exposure to the hypertonic seawater, spermatozoon shrinkage is initially mediated by water efflux through Aqp1aa in the flagellar tail. The shrinkage results in an increase in intracellular Ca2+ concentration, and the activation of sperm motility and a Na+/K+/2Cl− (NKCC1) cotransporter. The activity of NKCC1 is required for the initiation of cell swelling, which secondarily activates the Aqp4a-Trpv4 complex to facilitate the influx of water via Aqp4a-M43 and Ca2+ via Trpv4 and L-type channels for the mediation of RVI. The inhibitory experiments show that blocking of each of these events prevents either shrinkage or RVI. Our data thus reveal that post-activated marine fish spermatozoa are capable of initiating RVI under a high hypertonic stress, which is essential for the maintenance of sperm motility.

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Aquaporins and (in)fertility: More than just water transport

Cited by 22 publications

References 140 publications

Aquaporins and Animal Gamete Cryopreservation: Advances and Future Challenges

Aquaporins and Animal Gamete Cryopreservation: Advances and Future Challenges

Expressional Modulation of Aquaporin 1 and 9 in the Rat Epididymis by an Anabolic-Androgenic Steroid, Nandrolone Decanoate

Aqp4a and Trpv4 mediate regulatory cell volume increase for swimming maintenance of marine fish spermatozoa

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