Expression and compartmentalisation of the glycolytic enzymes GAPDH and pyruvate kinase in boar spermatogenesis
Sandra Feiden A , Uwe Wolfrum B , Gerhard Wegener A and Günter Kamp A CA Institute of Zoology, Molecular Physiology Section, Johannes Gutenberg University Mainz, Becherweg 9-11, 55099 Mainz, Germany.
B Cell and Matrix Biology Section, Johannes Gutenberg University Mainz, Becherweg 9-11, 55099 Mainz, Germany.
C Corresponding author. Email: kamp@uni-mainz.de
Reproduction, Fertility and Development 20(6) 713-723 https://doi.org/10.1071/RD08004
Submitted: 8 January 2008 Accepted: 18 May 2008 Published: 9 July 2008
Abstract
Boar spermatozoa contain isoforms of both glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) and pyruvate kinase (PK, EC 2.7.1.40). The sperm-specific forms, GAPDH-S and PK-S, are tightly bound to cell structures. By immunofluorescence microscopy GAPDH-S and PK-S were localised in the principal piece of the boar sperm flagellum as well as in the acrosomal region of the sperm head and at the head–midpiece junction. The midpiece of the flagellum, however, contains isoforms of GAPDH and PK that were only recognised by antibodies against somatic GAPDH and PK, respectively, but not by the antibodies against GAPDH-S and PK-S. In sections of boar testis, GAPDH-S and PK-S were first detected in elongating spermatids when both the developing flagellum and the head were labelled with antibodies against GAPDH-S and PK-S. In contrast, antibodies against rabbit muscle GAPDH and PK labelled all developmental stages of germ cells and also neighbouring contractile cells. Thus, the structure-bound sperm-specific enzymes, GAPDH-S and PK-S, appeared only late in spermatogenesis simultaneously with the development of the structures to which they are bound. Anchoring glycolytic enzymes to structures in these mitochondria-free regions may secure ATP-production for both motility and acrosome function.
Additional keywords: glycolysis, PK, spermatozoa.
Acknowledgements
We thank Ms. Gabi Stern-Schneider for her excellent technical assistance. This work was supported by the Deutsche Forschungsgemeinschaft (Ka 583/7–4), and Sandra Feiden was the recipient of a scholarship (LGFG) from Rheinland-Pfalz.
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