A Tyrosine-Phosphorylated 55-Kilodalton Motility-Associated Bovine Sperm Protein is Regulated by Cyclic Adenosine 3′,5′-Monophosphates and Calcium1

Vijayaraghavan, Srinivasan; Trautman, Kevin D.; Goueli, Said A.; Carr, Daniel W.

doi:10.1095/biolreprod56.6.1450

Cited by 85 publications

(77 citation statements)

References 42 publications

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“…2). Some specific protein targets of tyrosine phosphorylation in sperm have been suggested and phosphorylation of these proteins has been closely linked to the onset of motility in bovine sperm (Vijayaraghavan et al 1997b(Vijayaraghavan et al , 2000.…”

Section: Motilitymentioning

confidence: 99%

Moving to the beat: a review of mammalian sperm motility regulation

Turner¹

2006

Reprod. Fertil. Dev.

245

184

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Abstract. Because it is generally accepted that a high percentage of poorly motile or immotile sperm will adversely affect male fertility, analysis of sperm motility is a central part of the evaluation of male fertility. In spite of its importance to fertility, poor sperm motility remains only a description of a pathology whose underlying cause is typically poorly understood. The present review is designed to bring the clinician up to date with the most current understanding of the mechanisms that regulate sperm motility and to raise questions about how aberrations in these mechanisms could be the underlying causes of this pathology.

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Section: Motilitymentioning

confidence: 99%

Moving to the beat: a review of mammalian sperm motility regulation

Turner¹

2006

Reprod. Fertil. Dev.

245

184

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“…Moreover, these authors describe the presence of both the a and b GSK3 isoforms in bovine epididymal spermatozoa (Vijayaraghavan et al , 1997 and discovered a 55 kDa protein whose tyrosine phosphorylation was closely correlated to the motility state of epididymal bovine spermatozoa and the treatment of these cells with motility activators, like isobutylmethylxanthine or 8Br-cAMP, resulted in increased tyrosine phosphorylation of this protein (Vijayaraghavan et al 1997). The same authors showed a correlation between the 55 kDa tyrosine phosphorylation motility-associated protein and the GSK3 and suggested that GSK3, which is also regulated by tyrosine phosphorylation, could be an important key underlying motility initiation in the epididymis (Vijayaraghavan et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3α

Aparicio¹,

Bragado²,

Gil³

et al. 2007

Reproduction

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Sperm functions are critically controlled through the phosphorylation state of specific proteins. Glycogen synthase kinase-3 (GSK3) is a serine/threonine kinase with two different isoforms (a and b), the enzyme activity of which is inhibited by serine phosphorylation. Recent studies suggest that GSK3 is involved in the control of bovine sperm motility. Our aim was to investigate whether GSK3 is present in porcine spermatozoa and its role in the function of these cells. This work shows that both isoforms of GSK3 are present in whole cell lysates of porcine sperm and are phosphorylated on serine in spermatozoa stimulated with the cAMP analog, 8Br-cAMP. A parallel increase in serine phosphorylation of the isoform GSK3a, but not in the isoform GSK3b, is observed after treatments that also induce a significant increase in porcine sperm velocity parameters. Therefore, a significant positive correlation among straight-line velocity, circular velocity, average velocity, rapid-speed spermatozoa, and GSK3a serine phosphorylation levels exists. Inhibition of GSK3 activity by alsterpaullone leads to a significant increase in the percentage of rapid-and medium-speed spermatozoa as well as in all sperm velocity parameters and coefficients. Moreover, pretreatment of porcine spermatozoa with alsterpaullone significantly increased the percentage of capacitated porcine spermatozoa and presents no effect in the number of acrosome-reacted porcine spermatozoa. Our work suggests that the isoform GSK3a plays a negative role in the regulation of porcine sperm motility and points out the possibility that sperm motile quality might be modulated according the activity state of GSK3a. Reproduction (2007) 134 435-444

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“…Since the FS and ODFs taper, the flagellum is not uniform in stiffness, becoming progressively less stiff in the distal region. In addition to the mechanical role of the sheath and ODFs, it is also well documented that the sheath and ODFs are also the site of many enzymes that support metabolism and signaling in mammalian sperm (Vijayaraghavan et al, 1997;Eddy, 2007), but these functions are beyond the scope of this review. Much of the initial description of the unique ultrastructural anatomy of the mammalian sperm was first compiled by Phillips (Fawcett, 1958, 1975; Phillips, 1969, 1970;Phillips, 1972Phillips, , 1997).…”

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confidence: 99%

Functional anatomy of the mammalian sperm flagellum

2016

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The eukaryotic flagellum is the organelle responsible for the propulsion of the male gamete in most animals. Without exception, sperm of all mammalian species use a flagellum for swimming. The mammalian sperm has a centrally located 9 1 2 arrangement of microtubule doublets and hundreds of accessory proteins that together constitute an axoneme. However, they also possess several characteristic peri-axonemal structures that make the mammalian sperm tail function differently. These modifications include nine outer dense fibers (ODFs) that are paired with the nine outer microtubule doublets of the axoneme, and are anchored in a structure called the connecting piece located at the base. The presence of the ODFs and connecting piece, and the absence of a basal body, dictate that physical forces generated by the dynein motors are transmitted to the base of the flagellum through the ODFs. Mammalian sperm flagella also possess a mitochondrial and a fibrous sheath that encircle most of the axoneme. These sheaths and the ODFs add mechanical rigidity to the flagellum creating the functional effect of increasing bend wavelength, which requires the entrainment of more dynein motors in the production of a single wave. The sheaths also act as a retinaculum and maintain the integrity of the central axoneme when large bending torques are generated by dynein. Large torque production is crucial to the process of hyperactivation and the unique motility transitions associated with effective fertilizing capacity. Consequently, these specialized anatomical features are essential for the effective interaction of sperm with the female reproductive tract and ovum. V C 2016 Wiley Periodicals, Inc.Key Words: axoneme; outer dense fibers; fibrous sheath; outer doublets; dynein; connecting piece; hyperactivation; sperm motility Introduction E ukaryotic cilia and flagella are highly conserved and ubiquitous organelles present in most animals, as well as many lower plants and eukaryotic protozoa. In the vertebrate lineage, the eukaryotic flagellum is universally employed to propel the male gamete. In the mammalian branch of the vertebrates, the sperm tail is always a modified flagellum with some characteristic accessory features that are added onto the basic 9 1 2 axoneme of microtubules found in most cilia and flagella. Figure 1 shows transmission electron micrographs (TEMs) of a mouse sperm flagellum in cross section at several positions along the length of the flagellum. The central axoneme is visible with its nine outer doublets surrounding a pair of single central microtubules (central pair or CP). Each of the outer microtubule doublets bears two rows of projections called the inner row and outer row of dynein arms. These arms are composed of the dynein motor proteins that power motility. The dynein arms are the source of the motive force that bends the flagellum. The dynein heavy chains (DHC) of the arms form bridges between the outer doublets and undergo a Mg-ATP driven power stroke that generates a sliding (or shearing) action between t...

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A Tyrosine-Phosphorylated 55-Kilodalton Motility-Associated Bovine Sperm Protein is Regulated by Cyclic Adenosine 3′,5′-Monophosphates and Calcium1

Cited by 85 publications

References 42 publications

Moving to the beat: a review of mammalian sperm motility regulation

Moving to the beat: a review of mammalian sperm motility regulation

Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3α

Functional anatomy of the mammalian sperm flagellum

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