Three male germline-specific aldolase A isozymes are generated by alternative splicing and retrotransposition

Vemuganti, Soumya; Bell, Timothy A.; Scarlett, Cameron O.; Parker, Carol E.; Villena, Fernando Pardo-Manuel de; O’Brien, Deborah A.

doi:10.1016/j.ydbio.2007.06.010

Cited by 46 publications

(68 citation statements)

References 85 publications

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“…Similar to that analysis, we have found that in mouse sperm, tubulin, VDAC, PDH E1 β chain, glutathione S-transferase, NADH dehydrogenase (ubiquinone) Fe-S protein 6, acrosin binding protein precursor, proteasome subunit alpha type 6b, and cytochrome b-c1 complex are phosphorylated in tyrosine residues. Interestingly, among the proteins phosphorylated on tyrosine residues we have identified two recently described testis-specific aldolases (Vemuganti et al, 2007). Aldolase is the fourth enzyme of glycolysis; in mouse sperm, this metabolic process is the main pathway for ATP production as was demonstrated using null mutants of other glycolytic enzymes (Miki et al, 2004).…”

Section: Characterization Of Proteins That Undergo Tyrosine Phosphorymentioning

confidence: 90%

Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation

Arcelay¹,

Salicioni²,

Wertheimer³

et al. 2008

Int. J. Dev. Biol.

135

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Mammalian sperm are not able to fertilize immediately upon ejaculation; they become fertilization-competent after undergoing changes in the female reproductive tract collectively termed capacitation. Although it has been established that capacitation is associated with an increase in tyrosine phosphorylation, little is known about the role of this event in sperm function. In this work we used a combination of two dimensional gel electrophoresis and mass spectrometry to identify proteins that undergo tyrosine phosphorylation during capacitation. Some of the identified proteins are the mouse orthologues of human sperm proteins known to undergo tyrosine phosphorylation. Among them we identified VDAC, tubulin, PDH E1 β β β β β chain, glutathione S-transferase, NADH dehydrogenase (ubiquinone) Fe-S protein 6, acrosin binding protein precursor (sp32), proteasome subunit alpha type 6b and cytochrome b-c1 complex. In addition to previously described proteins, we identified two testis-specific aldolases as substrates for tyrosine phosphorylation. Genomic and EST analyses suggest that these aldolases are retroposons expressed exclusively in the testis, as has been reported elsewhere. Because of the importance of glycolysis for sperm function, we hypothesize that tyrosine phosphorylation of these proteins can play a role in the regulation of glycolysis during capacitation. However, neither the Km nor the Vmax of aldolase changed as a function of capacitation when its enzymatic activity was assayed in vitro, suggesting other levels of regulation for aldolase function.

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Section: Characterization Of Proteins That Undergo Tyrosine Phosphorymentioning

confidence: 90%

Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation

Arcelay¹,

Salicioni²,

Wertheimer³

et al. 2008

Int. J. Dev. Biol.

135

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“…Glycolysis can therefore serve as supplier of ATP to the flagellar dynein ATPase for motility in mouse sperm; evidence that this is the case is presented below. The concept that the sperm-specific enzyme isoforms of the Embden-Meyerhof pathway are so constructed as to bind to this scaffold remains to be fully validated, but the number of these isoforms is impressive: phosphoglycerate kinase-2 (PGK2), GPI, phosphofructose kinase-1 (PFK1), and EN (see Vemuganti et al, 2007, for listing and references), and aldolase. The recent finding of Vemuganti et al (2007) that three sperm-specific isoforms of aldolase are localized in the mouse sperm flagellum, of which two have N-terminal extensions not found in the others.…”

Section: Glycolysis: Sugar As Friendmentioning

confidence: 99%

“…The concept that the sperm-specific enzyme isoforms of the Embden-Meyerhof pathway are so constructed as to bind to this scaffold remains to be fully validated, but the number of these isoforms is impressive: phosphoglycerate kinase-2 (PGK2), GPI, phosphofructose kinase-1 (PFK1), and EN (see Vemuganti et al, 2007, for listing and references), and aldolase. The recent finding of Vemuganti et al (2007) that three sperm-specific isoforms of aldolase are localized in the mouse sperm flagellum, of which two have N-terminal extensions not found in the others. These N-terminal extensions are tempting candidates for anchor sequences to the fibrous sheath of the flagellum, but have not yet won experimental confirmation.…”

Section: Glycolysis: Sugar As Friendmentioning

confidence: 99%

Mammalian sperm metabolism: oxygen and sugar, friend and foe

Storey¹

2008

Int. J. Dev. Biol.

290

260

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Mammalian spermatozoa expend energy, generated as intracellular ATP, largely on motility. If the sperm cell cannot swim by use of its flagellar motion, it cannot fertilize the egg. Studies of the means by which this energy is generated span a period of six decades. This review gives an overview of these studies, which demonstrate that both mitochondrial oxidative phosphorylation, for which oxygen is friend, and glycolysis, for which sugar is friend, can provide the energy, independent of one another. In mouse sperm, glycolysis appears to be the dominant pathway; in bull sperm, oxidative phosphorylation is the predominant pathway. In the case of bull sperm, the high activity of the glycolytic pathway would maintain the intracellular pH too low to allow sperm capacitation; here sugar is enemy. The cow's oviduct has very low glucose concentration, thus allowing capacitation to go forward. The choice of the pathway of energy generation in vivo is set by the conditions in the oviduct of the conspecific female. The phospholipids of the sperm plasma membrane have a high content of polyunsaturated fatty acids represented in their acyl moieties, rendering them highly susceptible to lipid peroxidation; in this case oxygen is enemy. But the susceptibility of the sperm membrane to lethal damage by lipid peroxidation allows the female oviduct to dispose of sperm that have overstayed their welcome, and so keep in balance sperm access to the egg and sperm removal once this has occurred.

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“…Aldolase B is highly expressed in both kidney and liver whereas aldolase C is found mainly in the nervous system, but has been also identified in bovine spermatozoa (Fiedler et al 2008). In addition, three novel aldolase A isoenzymes are expressed in mouse spermatozoa (Vemuganti et al 2007).…”

Section: Introductionmentioning

confidence: 99%

In guinea pig sperm, aldolase A forms a complex with actin, WAS, and Arp2/3 that plays a role in actin polymerization

Chiquete-Félix¹,

Hernández²,

Méndez³

et al. 2009

Reproduction

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Glycolytic enzymes have, in addition to their role in energy production, other functions in the regulation of cellular processes. Aldolase A has been reported to be present in sperm, playing a key role in glycolysis; however, despite its reported interactions with actin and WAS, little is known about a non-glycolytic role of aldolase A in sperm. Here, we show that in guinea pig spermatozoa, aldolase A is tightly associated to cytoskeletal structures where it interacts with actin, WAS, and Arp2/3. We show that aldolase A spermatozoa treatment increases their polymerized actin levels. In addition, we show that there is a direct correlation between the levels of polymerized actin and the levels of aldolase A-actin interaction. Our results suggest that aldolase A functions as a bridge between filaments of actin and the actin-polymerizing machinery.

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Three male germline-specific aldolase A isozymes are generated by alternative splicing and retrotransposition

Cited by 46 publications

References 85 publications

Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation

Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation

Mammalian sperm metabolism: oxygen and sugar, friend and foe

In guinea pig sperm, aldolase A forms a complex with actin, WAS, and Arp2/3 that plays a role in actin polymerization

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