The reactivation of demembranated human spermatozoa lacking outer dynein arms is independent of pH

Keskes, Leila; Giroux-Widemann, V.; Serres, Catherine; Pignot-Paintrand, Isabelle; Jouannet, Pierre; Feneux, D.

doi:10.1002/(sici)1098-2795(199804)49:4<416::aid-mrd9>3.0.co;2-q

Cited by 25 publications

(16 citation statements)

References 41 publications

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“…In fact, no change in the reactivation level of LODA spermatozoa was found when the pH was increased from 7.1 to 7.8 unlike normal spermatozoa, whose reactivation level was significantly increased at pH 7.8 (Keskes et al 1998). However, the motility of LODA spermatozoa could be partially reinitiated with appropriate concentrations of Mg 2C -ATP and removal of the free Ca 2C with EGTA, concluding that reactivation of LODA spermatozoa is pH-independent but Ca-dependent (Keskes et al 1998). These data and our results (Table 2) could support the idea that the dyneins present a 'pH sensor' located in the inner dynein arm (IDA), and a 'Ca 2C sensor' located in the ODA.…”

Section: Discussionmentioning

confidence: 77%

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ATPases, ion exchangers and human sperm motility

Peralta-Arias¹,

Vívenes²,

Camejo³

et al. 2015

Reproduction

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Human sperm has several mechanisms to control its ionic milieu, such as the Na,K-ATPase (NKA), the Ca-ATPase of the plasma membrane (PMCA), the Na C /Ca 2C -exchanger (NCX) and the NaOn the other hand, the dynein-ATPase is the intracellular motor for sperm motility. In this work, we evaluated NKA, PMCA, NHE, NCX and dynein-ATPase activities in human sperm and investigated their correlation with sperm motility. Sperm motility was measured by Computer Assisted Semen Analysis. It was found that the NKA activity is inhibited by ouabain with two K i (7.9!10 K9 and 9.8!10 K5 M), which is consistent with the presence of two isoforms of a subunit of the NKA in the sperm plasma membranes (a1 and a4), being a4 more sensitive to ouabain. The decrease in NKA activity is associated with a reduction in sperm motility. In addition, sperm motility was evaluated in the presence of known inhibitors of NHE, PMCA and NCX, such as amiloride, eosin, and KB-R7943, respectively, as well as in the presence of nigericin after incubation with ouabain. Amiloride, eosin and KB-R7943 significantly reduced sperm motility. Nigericin reversed the effect of ouabain and amiloride on sperm motility. Dynein-ATPase activity was inhibited by acidic pH and micromolar concentrations of Ca 2C. We explain our results in terms of inhibition of the dynein-ATPase in the presence of higher cytosolic H C and Ca 2C, and therefore inhibition of sperm motility.

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Section: Discussionmentioning

confidence: 77%

“…It is important to mention a study on human sperm from patients with a pathology known as lacking ODAs (LODA; Keskes et al 1998). This condition is associated with a lower percentage of motile spermatozoa in semen, due to the absence of external dynein arms.…”

Section: Discussionmentioning

confidence: 99%

ATPases, ion exchangers and human sperm motility

Peralta-Arias¹,

Vívenes²,

Camejo³

et al. 2015

Reproduction

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“…Recently, one study demonstrated that sperm lacking outer dynein arms do not increase motility in response to an increase in pH, which stimulates normal sperm, but produce a low level of constant motility at an acidic pH where normal sperm are relatively inactive. These data suggest that the outer dynein arms contain a pH-sensitive regulatory mechanism (40). Therefore, in an acidic environment, dynein outer arms may inhibit flagellar activity, whereas in more alkaline conditions, dynein outer arms activate flagellar activity and motility.…”

Section: Discussionmentioning

confidence: 83%

“…Structurally, the sperm tail is a flagellum, a cellular component composed of microtubules whose movement is powered by the ATPase motor, dynein (30). In flagella, the outer and inner dynein arms are the axonemal structures involved in the production of the stroke necessary for the sliding of adjacent microtubules (40). Recently, one study demonstrated that sperm lacking outer dynein arms do not increase motility in response to an increase in pH, which stimulates normal sperm, but produce a low level of constant motility at an acidic pH where normal sperm are relatively inactive.…”

Section: Discussionmentioning

confidence: 99%

Sperm Motility Is Dependent on a Unique Isoform of the Na,K-ATPase

Woo

James

Lingrel³

2000

Journal of Biological Chemistry

146

164

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The Na,K-ATPase, a member of the P-type ATPases, is composed of two subunits, ␣ and ␤, and is responsible for translocating Na ؉ out of the cell and K ؉ into the cell using the energy of hydrolysis of one molecule of ATP. The electrochemical gradient it generates is necessary for many cellular functions, including establishment of the plasma membrane potential and transport of sugars and ions in and out of the cell. Families of isoforms for both the ␣ and ␤ subunits have been identified, and specific functional roles for individual isoforms are just beginning to emerge. The ␣4 isoform is the most recently identified Na,K-ATPase ␣ isoform, and its expression has been found only in testis. Here we show that expression of the ␣4 isoform in testis is localized to spermatozoa and that inhibition of this isoform alone eliminates sperm motility. These data describe for the first time a biological function for the ␣4 isoform of the Na,KATPase, revealing a critical role for this isoform in sperm motility.

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“…35 However, it is not known whether this effect is caused by modulation of kinase activity, even though an acidic pH has been shown to inhibit PKA function, 46 or the direct activation of ODAs of the axoneme. 47 Temperature has also been shown in many investigations to influence CBF, most likely through protein kinase C modulation., 36,37,48 Lower temperature tends to slow CBF. 36 CBF is also regulated by mechanical factors.…”

Section: Dynamic Regulationmentioning

confidence: 99%

Acquired Cilia Dysfunction in Chronic Rhinosinusitis

Gudis

Zhao

Cohen

2012

Am J Rhinol�Allergy

153

136

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Background: Cilia are complex and powerful cellular structures of the respiratory mucosa that play a critical role in airway defense. Respiratory epithelium is lined with cilia that perform an integrated and coordinated mechanism called mucociliary clearance. Mucociliary clearance is the process by which cilia transport the mucus blanket overlying respiratory mucosa to the gastrointestinal tract for ingestion. It is the primary means by which the airway clears pathogens, allergens, debris, and toxins. The complex structure and regulatory mechanisms that dictate the form and function of normal cilia are not entirely understood, but it is clear that ciliary dysfunction results in impaired respiratory defense.Methods: A literature review of the current knowledge of cilia dysfunction in chronic rhinosinsusitis was conducted.Results: Ciliary dysfunction may be primary, the result of genetic mutations resulting in abnormal cilia structure, or, more commonly, secondary, the result of environmental, infectious, or inflammatory stimuli that disrupt normal motility or coordination. Patients with chronic rhinosinusitis (CRS) have been found to have impaired mucociliary clearance. Many biochemical, environmental, and mechanical stimuli have been shown to influence ciliary beat frequency, and common microbial pathogens of respiratory mucosa such as Pseudomonas aeruginosa and Haemophilus influenzae have developed toxins that appear to interrupt normal mucociliary function. Furthermore, inflammatory mediators known to be present in patients with CRS appear to impair secondarily mucociliary clearance. Conclusion:The goal of this article is to summarize the recent developments in the understanding of cilia dysfunction and mucociliary clearance in CRS.

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The reactivation of demembranated human spermatozoa lacking outer dynein arms is independent of pH

Cited by 25 publications

References 41 publications

ATPases, ion exchangers and human sperm motility

ATPases, ion exchangers and human sperm motility

Sperm Motility Is Dependent on a Unique Isoform of the Na,K-ATPase

Acquired Cilia Dysfunction in Chronic Rhinosinusitis

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