Human Sperm Capacitation Involves the Regulation of the Tyr-Phosphorylation Level of the Anion Exchanger 1 (AE1)

Donà, Gabriella; Tibaldi, Elena; Andrisani, Alessandra; Ambrosini, Guido; Sabbadin, Chiara; Pagano, Mario A.; Brunati, Anna Maria; Armanini, Decio; Ragazzi, Eugenio; Bordin, Luciana

doi:10.3390/ijms21114063

Cited by 15 publications

(20 citation statements)

References 43 publications

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“…CFTRs have been reported to be present in mammalian spermatozoa [ 118 , 119 , 120 , 121 ]. The role of CFTRs in sperm motility is not insignificant.…”

Section: Chloride Channelsmentioning

confidence: 99%

Structure and Function of Ion Channels Regulating Sperm Motility—An Overview

Nowicka-Bauer

Szymczak-Cendlak

2021

IJMS

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Sperm motility is linked to the activation of signaling pathways that trigger movement. These pathways are mainly dependent on Ca2+, which acts as a secondary messenger. The maintenance of adequate Ca2+ concentrations is possible thanks to proper concentrations of other ions, such as K+ and Na+, among others, that modulate plasma membrane potential and the intracellular pH. Like in every cell, ion homeostasis in spermatozoa is ensured by a vast spectrum of ion channels supported by the work of ion pumps and transporters. To achieve success in fertilization, sperm ion channels have to be sensitive to various external and internal factors. This sensitivity is provided by specific channel structures. In addition, novel sperm-specific channels or isoforms have been found with compositions that increase the chance of fertilization. Notably, the most significant sperm ion channel is the cation channel of sperm (CatSper), which is a sperm-specific Ca2+ channel required for the hyperactivation of sperm motility. The role of other ion channels in the spermatozoa, such as voltage-gated Ca2+ channels (VGCCs), Ca2+-activated Cl-channels (CaCCs), SLO K+ channels or voltage-gated H+ channels (VGHCs), is to ensure the activation and modulation of CatSper. As the activation of sperm motility differs among metazoa, different ion channels may participate; however, knowledge regarding these channels is still scarce. In the present review, the roles and structures of the most important known ion channels are described in regard to regulation of sperm motility in animals.

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“…CFTRs have been reported to be present in mammalian spermatozoa [ 118 , 119 , 120 , 121 ]. The role of CFTRs in sperm motility is not insignificant.…”

Section: Chloride Channelsmentioning

confidence: 99%

Structure and Function of Ion Channels Regulating Sperm Motility—An Overview

Nowicka-Bauer

Szymczak-Cendlak

2021

IJMS

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“…The main sites of mammalian band 3 gene expression are erythroid cells and the kidney, but it is also expressed in the heart ( 132 ), and there is recent evidence that band 3 is involved in sperm capacitation ( 133 ). In the kidney, the band 3 gene is transcribed with an alternate promoter ( 134 , 135 ) resulting in an NH 2 terminus that is 65 residues shorter than red cell band 3 ( 136 ).…”

Section: Band 3 Structurementioning

confidence: 99%

Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1

Jennings

2021

American Journal of Physiology-Cell Physiology

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The major transmembrane protein of the red blood cell, known as band 3, AE1, and SLC4A1, has two main functions: 1) catalysis of Cl-/HCO3- exchange, one of the steps in CO2 excretion; 2) anchoring the membrane skeleton. This review summarizes the 150 year history of research on red cell anion transport and band 3 as an experimental system for studying membrane protein structure and ion transport mechanisms. Important early findings were that red cell Cl- transport is a tightly coupled 1:1 exchange and band 3 is labeled by stilbenesulfonate derivatives that inhibit anion transport. Biochemical studies showed that the protein is dimeric or tetrameric (paired dimers) and that there is one stilbenedisulfonate binding site per subunit of the dimer. Transport kinetics and inhibitor characteristics supported the idea that the transporter acts by an alternating access mechanism with intrinsic asymmetry. The sequence of band 3 cDNA provided a framework for detailed study of protein topology and amino acid residues important for transport. The identification of genetic variants produced insights into the roles of band 3 in red cell abnormalities and distal renal tubular acidosis. The publication of the membrane domain crystal structure made it possible to propose concrete molecular models of transport. Future research directions include improving our understanding of the transport mechanism at the molecular level and of the integrative relationships among band 3, hemoglobin, carbonic anhydrase, and gradients (both transmembrane and subcellular) of HCO3-, Cl-, O2, CO2, pH, and NO metabolites during pulmonary and systemic capillary gas exchange.

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“…phosphorylated tyrosine levels in the head of human sperm, which is critical for AR (Dona et al, 2020). Other researchers have also found that protein tyrosine phosphorylation in the sperm head region is relevant to AR (Dona et al, 2011;Andrisani et al, 2015).…”

Section: Discussionmentioning

confidence: 93%

KCNQ1 Potassium Channel Expressed in Human Sperm Is Involved in Sperm Motility, Acrosome Reaction, Protein Tyrosine Phosphorylation, and Ion Homeostasis During Capacitation

Gao

Liang

et al. 2021

Front. Physiol.

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Potassium channels are involved in membrane hyperpolarization and ion homeostasis regulation during human sperm capacitation. However, the types of potassium channels in human sperm remain controversial. The voltage-gated ion channel KCNQ1 is ubiquitously expressed and regulates key physiological processes in the human body. In the present study, we investigated whether KCNQ1 is expressed in human sperm and what role it might have in sperm function. The expression and localization of KCNQ1 in human sperm were evaluated using Western blotting and indirect immunofluorescence. During capacitation incubation, human sperm were treated with KCNQ1- specific inhibitor chromanol 293B. Sperm motility was analyzed using a computer-assisted sperm analyzer. The acrosome reaction was studied using fluorescein isothiocyanate-conjugated Pisum sativum agglutinin staining. Protein tyrosine phosphorylation levels and localization after capacitation were determined using Western blotting and immunofluorescence. Intracellular K+, Ca2+, Cl−, pH, and membrane potential were analyzed using fluorescent probes. The results demonstrate that KCNQ1 is expressed and localized in the head and tail regions of human sperm. KCNQ1 inhibition reduced sperm motility, acrosome reaction rates, and protein tyrosine phosphorylation but had no effect on hyperactivation. KCNQ1 inhibition also increased intracellular K+, membrane potential, and intracellular Cl−, while decreasing intracellular Ca2+ and pH. In conclusion, the KCNQ1 channel plays a crucial role during human sperm capacitation.

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Human Sperm Capacitation Involves the Regulation of the Tyr-Phosphorylation Level of the Anion Exchanger 1 (AE1)

Cited by 15 publications

References 43 publications

Structure and Function of Ion Channels Regulating Sperm Motility—An Overview

Structure and Function of Ion Channels Regulating Sperm Motility—An Overview

Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1

KCNQ1 Potassium Channel Expressed in Human Sperm Is Involved in Sperm Motility, Acrosome Reaction, Protein Tyrosine Phosphorylation, and Ion Homeostasis During Capacitation

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