Influence of temperature on hexose transport by round spermatids of rats

Hall, Peter F.; Nakamura, Mako

doi:10.1530/jrf.0.0630373

“…The data directly relate to the expression of GLUT1, GLUT2, and GLUT3 by bull spermatozoa and are consistent with results of previous studies indicating that human and rat spermatids and spermatozoa take up hexoses [Glander and Dettmer, 1978a,b;Grootegoed and den Boer, 1990;Hall and Nakamura, 1981;Hiipakka and Hammerstedt, 1978a,b;Mita and Hall, 1982;Nakamura et al, 1987;Peterson and Freund, 1975;Peterson et al, 1977]. The data directly relate to the expression of GLUT1, GLUT2, and GLUT3 by bull spermatozoa and are consistent with results of previous studies indicating that human and rat spermatids and spermatozoa take up hexoses [Glander and Dettmer, 1978a,b;Grootegoed and den Boer, 1990;Hall and Nakamura, 1981;Hiipakka and Hammerstedt, 1978a,b;Mita and Hall, 1982;Nakamura et al, 1987;Peterson and Freund, 1975;Peterson et al, 1977].…”

Section: Discussionsupporting

confidence: 91%

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

Angulo

¹

,

Rauch

²

,

Droppelmann

³

et al. 1998

View full text Add to dashboard Cite

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.

show abstract

“…The uptake data indicate that bull spermatozoa take up deoxyglucose and dehydroascorbic acid in a dose-dependent manner and that transport of both substrates was inhibited by cytochalasin B. The data directly relate to the expression of GLUT1, GLUT2, and GLUT3 by bull spermatozoa and are consistent with results of previous studies indicating that human and rat spermatids and spermatozoa take up hexoses [Glander and Dettmer, 1978a,b;Grootegoed and den Boer, 1990;Hall and Nakamura, 1981;Hiipakka and Hammerstedt, 1978a,b;Mita and Hall, 1982;Nakamura et al, 1987;Peterson and Freund, 1975;Peterson et al, 1977]. 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.…”

Section: Discussionsupporting

confidence: 89%

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

Angulo

¹

,

Rauch

²

,

Droppelmann

³

et al. 1998

View full text Add to dashboard Cite

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.

show abstract

“…Matsumura et al ( 22 ) and Sato et al ( 23 ) reported efficient spermatogenic differentiation of rodent testicular organ cultures at 34°C. To evaluate the effect of temperature on somatic cell and spermatogonial maturation, rat organoids were generated with OFM (72 hours: day 0 undifferentiated organoid) and then cultured with organoid differentiation medium (ODM) at 37°C and 34°C ( 22 , 42 ) for up to 28 days. Immunofluorescence analysis revealed no morphological differences between the two groups at day 28 ( Figure 2A ) and both cultures showed expression of Claudin 11, a component of Sertoli cell tight junctions ( Figure 2B ) ( 43 ).…”

Section: Resultsmentioning

confidence: 99%

Organotypic Rat Testicular Organoids for the Study of Testicular Maturation and Toxicology

Sakib

¹

,

Lara

²

,

Huynh

³

et al. 2022

View full text Add to dashboard Cite

An in vitro system to study testicular maturation in rats, an important model organism for reproductive toxicity, could serve as a platform for high-throughput drug and toxicity screening in a tissue specific context. In vitro maturation of somatic cells and spermatogonia in organ culture systems has been reported. However, this has been a challenge for organoids derived from dissociated testicular cells. Here, we report generation and maintenance of rat testicular organoids in microwell culture for 28 days. We find that rat organoids can be maintained in vitro only at lower than ambient O2 tension of 15% and organoids cultured at 34°C have higher somatic cell maturation and spermatogonial differentiation potential compared to cultures in 37°C. Upon exposure to known toxicants, phthalic acid mono-2-ethylhexyl ester and cadmium chloride, the organoids displayed loss of tight-junction protein Claudin 11 and altered transcription levels of somatic cell markers that are consistent with previous reports in animal models. Therefore, the microwell-derived rat testicular organoids described here can serve as a novel platform for the study of testicular cell maturation and reproductive toxicity in vitro.

show abstract

Influence of temperature on hexose transport by round spermatids of rats

Cited by 6 publications

References 11 publications

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

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

Organotypic Rat Testicular Organoids for the Study of Testicular Maturation and Toxicology

Contact Info

Product

Resources

About