Glucose and fructose utilization by rat spermatozoa within the uterine lumen

Leese, Henry J.; Astley, N. R.; Lambert, Donna L.

doi:10.1530/jrf.0.0610435

Cited by 15 publications

(5 citation statements)

References 1 publication

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“…Although the available data are consistent with the concept that human spermatozoa may be able to use glucose as a normal source of energy, this is still a matter of controversy. The glucose content in the female reproductive tract is similar to that present in serum and thus could be used as a source of energy by the spermatozoa [Leese et al, 1981;Weed and Carrera, 1970]. However, the glucose content of the seminiferous tubules is very low, and the data on seminal fluid indicate a great variability on its glucose content, from near zero to 5 mM [Patel et al, 1988;Paz et al, 1977;Tauber et al, 1975].…”

Section: Discussionmentioning

confidence: 99%

Hexose transporter expression and function in mammalian spermatozoa: Cellular localization and transport of hexoses and vitamin C

et al. 1998

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We analyzed the expression of hexose transporters in human testis and in human, rat, and bull spermatozoa and studied the uptake of hexoses and vitamin C in bull spermatozoa. Immunocytochemical and reverse transcription-polymerase chain reaction analyses demonstrated that adult human testis expressed the hexose transporters GLUT1, GLUT2, GLUT3, GLUT4, and GLUT5. Immunoblotting experiments demonstrated the presence of proteins of about 50-70 kD reactive with anti-GLUT1, GLUT2, GLUT3, and GLUT5 in membranes prepared from human spermatozoa, but no proteins reactive with GLUT4 antibodies were detected. Immunolocalization experiments confirmed the presence of GLUT1, GLUT2, GLUT3, GLUT5, and low levels of GLUT4 in human, rat, and bull spermatozoa. Each transporter isoform showed a typical subcellular localization in the head and the sperm tail. In the tail, GLUT3 and GLUT5 were present at the level of the middle piece in the three species examined, GLUT1 was present in the principal piece, and the localization of GLUT2 differed according of the species examined. Bull spermatozoa transported deoxyglucose, fructose, and the oxidized form of vitamin C, dehydroascorbic acid. Transport of deoxyglucose and dehydroascorbic acid was inhibited by cytochalasin B, indicating the direct participation of facilitative hexose transporters in the transport of both substrates by bull spermatozoa. Transport of fructose was not affected by cytochalasin B, which is consistent for an important role for GLUT5 in the transport of fructose in these cells. The data show that human, rat, and bull spermatozoa express several hexose transporter isoforms that allow for the efficient uptake of glucose, fructose, and dehydroascorbic acid by these cells.

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Section: Discussionmentioning

confidence: 99%

Hexose transporter expression and function in mammalian spermatozoa: Cellular localization and transport of hexoses and vitamin C

et al. 1998

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“…SDH lies within the polyol metabolic pathway in which glucose is reduced first to sorbitol by aldose reductase, and the resulting sorbitol is subsequently oxidixed by SDH to fructose (Hers, 1956;King and Mann, 1958). The polyol pathway has been reported in the testis (Kobayashi et al, 2002) and glucose, fructose and sorbitol are known energy sources for sperm metabolism (Frenkel et al, 1975;Leese et al, 1981). The glucose transporter isoform GLUT5 has been shown to function also as a fructose transporter and to be highly expressed in human testis and localized to the plasma membrane of mature spermatozoa including the entire sperm flagellum (Burant et al, 1992).…”

Section: Evidence Of Polyol and Lactate Pathways In The Fibrous Sheatmentioning

confidence: 99%

Compartmentalization of a unique ADP/ATP carrier protein SFEC (Sperm Flagellar Energy Carrier, AAC4) with glycolytic enzymes in the fibrous sheath of the human sperm flagellar principal piece

Kim

Haidl

Schaefer³

et al. 2007

Developmental Biology

102

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The longest part of the sperm flagellum, the principal piece, contains the fibrous sheath, a cytoskeletal element unique to spermiogenesis. We performed mass spectrometry proteomics on isolated human fibrous sheaths identifying a unique ADP/ATP carrier protein, SFEC [AAC4], seven glycolytic enzymes previously unreported in the human sperm fibrous sheath, and sorbitol dehydrogenase. SFEC, pyruvate kinase and aldolase were co-localized by immunofluorescence to the principal piece. A homology model constructed for SFEC predicted unique residues at the entrance to the nucleotide binding pocket of SFEC that are absent in other human ADP/ATP carriers, suggesting opportunities for selective drug targeting. This study provides the first evidence of a role for an ADP/ATP carrier family member in glycolysis. The co-localization of SFEC and glycolytic enzymes in the fibrous sheath supports a growing literature that the principal piece of the flagellum is capable of generating and regulating ATP independently from mitochondrial oxidation in the mid-piece. A model is proposed that the fibrous sheath represents a highly ordered complex, analogous to the electron transport chain, in which adjacent enzymes in the glycolytic pathway are assembled to permit efficient flux of energy substrates and products with SFEC serving to mediate energy generating and energy consuming processes in the distal flagellum, possibly as a nucleotide shuttle between flagellar glycolysis, protein phosphorylation and mechanisms of motility.

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“…The presence of abundant aldose reductase in uterine luminal fluids and term placenta has been detected by two-dimensional gel electrophoresis [109]. Although aldose reductase in conjunction with sorbitol dehydrogenase catalyzes the conversion of glucose to fructose, which can be the energy source for the spermatozoa [110], the quantity of aldose reductase appears to be in excess. Both enzymes are abundant in eggs and may participate in the production of fructose [72].…”

Section: Ros and Rnos In Fertilization And Early Development Of Embryomentioning

confidence: 99%

Fundamental roles of reactive oxygen species and protective mechanisms in the female reproductive system

Fujii

Iuchi

Okada

2005

Reprod Biol Endocrinol

229

120

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Controlled oxidation, such as disulfide bond formation in sperm nuclei and during ovulation, plays a fundamental role in mammalian reproduction. Excess oxidation, however, causes oxidative stress, resulting in the dysfunction of the reproductive process. Antioxidation reactions that reduce the levels of reactive oxygen species are of prime importance in reproductive systems in maintaining the quality of gametes and support reproduction. While anti-oxidative enzymes, such as superoxide dismutase and peroxidase, play a central role in eliminating oxidative stress, reduction-oxidation (redox) systems, comprised of mainly glutathione and thioredoxin, function to reduce the levels of oxidized molecules. Aldo-keto reductase, using NADPH as an electron donor, detoxifies carbonyl compounds resulting from the oxidation of lipids and proteins. Thus, many antioxidative and redox enzyme genes are expressed and aggressively protect gametes and embryos in reproductive systems.

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Glucose and fructose utilization by rat spermatozoa within the uterine lumen

Cited by 15 publications

References 1 publication

Hexose transporter expression and function in mammalian spermatozoa: Cellular localization and transport of hexoses and vitamin C

Hexose transporter expression and function in mammalian spermatozoa: Cellular localization and transport of hexoses and vitamin C

Compartmentalization of a unique ADP/ATP carrier protein SFEC (Sperm Flagellar Energy Carrier, AAC4) with glycolytic enzymes in the fibrous sheath of the human sperm flagellar principal piece

Fundamental roles of reactive oxygen species and protective mechanisms in the female reproductive system

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