Document Detail

Expression of key substrate cycle enzymes in rat spermatogenic cells: fructose 1,6 bisphosphatase and 6 phosphofructose 1-kinase.
MedLine Citation:
PMID:  17492776     Owner:  NLM     Status:  MEDLINE    
A substrate cycle composed of phosphofructo 1-kinase I (PFK) and fructose 1,6 bisphosphatase I (FBPase) has been proposed in rat spermatids. This substrate cycle can explain the ability of glucose to induce a decrease in intracellular ATP, a phenomenon that was related to regulation of [Ca(2+)]i in these cells. In spite of the importance of this metabolic cycle, the expression and activities of the enzymes that compose such cycle have not been systematically studied in spermatogenic cells. Here, we show that PFK and FBPase activities were present in pachytene spermatocytes and round spermatids extracts. Expression of PFK at the mRNA and protein levels showed a relatively similar expression in spermatogenic cells, but a stronger expression in Sertoli cells. Instead, expression of FBPase at the mRNA and protein levels was stronger in round and elongating spermatids as compared to other spermatogenic cells. A similar pattern was observed when evidencing FBPase activity by a NADPH-nitroblue tetrazolium-linked cytochemical assay in isolated pachytene spermatocytes and round spermatids. Rat spermatids also showed the ability to convert lactate to fructose- and glucose-6-P, indicating that both glycolytic and gluconeogenic fluxes are present in these cells. Our results indicate that a coordinated expression of key substrate cycle enzymes, at the level of PFK/FBPase, appear in the last stages of spermatogenic cell differentiation, suggesting that the co-regulation of these enzymes are required for the ability of these cells to respond to glucose and induce metabolic and Ca(2+) signals that can be important for sperm development and function.
Alejandro J Yáñez; Ximena Bustamante; Romina Bertinat; Enrique Werner; Maria Cecilia Rauch; Ilona I Concha; Juan G Reyes; Juan C Slebe
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cellular physiology     Volume:  212     ISSN:  0021-9541     ISO Abbreviation:  J. Cell. Physiol.     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-07-02     Completed Date:  2007-09-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0050222     Medline TA:  J Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  807-16     Citation Subset:  IM    
Instituto de Bioquímica, Facultad de Ciencias, Universidad Austral de Chile, Valdivia, Chile.
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MeSH Terms
Fructose-Bisphosphatase / genetics,  metabolism*
Fructosephosphates / metabolism
Gene Expression Regulation, Enzymologic*
Glucose / metabolism
Glucose-6-Phosphate / metabolism
Lactic Acid / metabolism
Phosphofructokinase-1, Muscle Type / genetics,  metabolism*
Pyruvate Kinase / genetics,  metabolism
RNA, Messenger / metabolism
Rats, Wistar
Sertoli Cells / enzymology
Spermatogenesis / physiology*
Spermatozoa / enzymology*
Substrate Cycling
Testis / cytology,  enzymology*
Reg. No./Substance:
0/Fructosephosphates; 0/RNA, Messenger; 50-21-5/Lactic Acid; 50-99-7/Glucose; 56-73-5/Glucose-6-Phosphate; 6814-87-5/fructose-6-phosphate; EC 2.7.1.-/Phosphofructokinase-1, Muscle Type; EC Kinase; EC

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