title: Accumulation of the mitochondrial form of the sulphydryl oxidase Erv1p/Alrp during the early stages of spermatogenesis.
abstract: In this study, we investigated the expression of the mammalian FAD-dependent sulphydryl oxidase Erv1p/Alrp in the rat and mouse and during mouse spermatogenesis. Up to three forms of Alrp were identified in protein extracts from different tissues and organs, but very little enzyme was present in blood samples. The three forms of Alrp represent the full-length protein of 23 kDa and fragments of 21 kDa and 15 kDa. All forms of Alrp were assembled into dimers in vivo. In contrast to samples from other organs, the protein analysis of mouse testis identified predominantly full-length 23 kDa Alrp. This finding prompted us to investigate in more detail the expression of Alrp during spermatogenesis. Testis samples of individual mice from postnatal days 13-29 were probed with an antibody specific for mammalian Alrp. In addition, cells from whole testis preparations were fractionated on a bovine serum albumin column gradient. Protein expression of mouse Alrp was compared with those of testis-specific cyritestin, the cytoskeleton marker actin and mitochondrial subunit Vb of cytochrome oxidase and cytochrome c. These studies demonstrated a specific accumulation of full-length mouse Alrp during the early stages of spermatogenesis. The highest levels of Alrp were found in spermatogonia and primary spermatocytes. Levels of expression of Alrp did not correlate with the synthesis of components of the respiratory chain, indicating that full-length Alrp in the mitochondria of spermatogonia and spermatocytes has another function in addition to its role in oxidative phosphorylation.
authors.affiliation: Institut für Botanik, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse, D-40225 Düsseldorf, Germany.
authors.forename: Monika
authors.initials: M
authors.lastname: Klissenbauer
authors.forename: Silke
authors.initials: S
authors.lastname: Winters
authors.forename: Uwe A O
authors.initials: UA
authors.lastname: Heinlein
authors.forename: Thomas
authors.initials: T
authors.lastname: Lisowsky
mesh_terms: D051722:ADAM Proteins; D000375:Aging; D000818:Animals; D015153:Blotting, Western; D002458:Cell Fractionation; D003574:Cytochrome c Group / Q000032:analysis; D004268:DNA-Binding Proteins; D019281:Dimerization; D003576:Electron Transport Complex IV / Q000032:analysis; D005455:Fluorescent Antibody Technique; D007150:Immunohistochemistry; D008297:Male; D008562:Membrane Glycoproteins / Q000032:analysis; D008666:Metalloendopeptidases / Q000032:analysis; D051379:Mice; D008810:Mice, Inbred C57BL; D018613:Microscopy, Confocal; D008928:Mitochondria / Q000201:enzymology*; D009363:Neoplasm Proteins; D010088:Oxidoreductases / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D017208:Rats, Wistar; D013090:Spermatocytes / Q000201:enzymology / Q000648:ultrastructure; D013091:Spermatogenesis; D013093:Spermatogonia / Q000201:enzymology / Q000648:ultrastructure; D013737:Testis / Q000201:enzymology / Q000648:ultrastructure; D016610:Tissue Embedding; D050862:Oxidoreductases Acting on Sulfur Group Donors
chemical_list: D051722:ADAM Proteins; D003574:Cytochrome c Group; D004268:DNA-Binding Proteins; D003576:Electron Transport Complex IV; D008562:Membrane Glycoproteins; D008666:Metalloendopeptidases; D009363:Neoplasm Proteins; D010088:Oxidoreductases; D010446:Peptide Fragments; D050862:Oxidoreductases Acting on Sulfur Group Donors; C120898:KMT2D protein, human; C499566:ADAM3A protein, human; C485429:Adam3 protein, mouse