Regulation of the secretion and synthesis of rat Sertoli cell SGP-1, SGP-2 and CP-2 by elongate spermatids.
The aim of this study was to investigate the effect of the absence of elongate spermatids (ES) from the rat seminiferous epithelium on the quantitative secretion and synthesis of the three major Sertoli cell secretory proteins--SGP-1, SGP-2 and CP-2. Seminiferous tubules (ST) were isolated (a) from normal 28-day-old rats, in which the most mature germ cell type is the round spermatid, (b) from normal adult rats at stages IX-XIV of the spermatogenic cycle, i.e. after spermiation, or at stages I-V and VI-VIII, when ES are still attached to the Sertoli cell, and (c) at stages VI-VIII from normal adult rats and from rats treated with methoxyacetic acid (MAA) in order to specifically deplete ES at these stages. Two-dimensional SDS PAGE combined with computerized image analysis was used to analyse 35S-methionine-labelled intracellular and secreted proteins. In the case of SGP-1 and SGP-2, almost all of the protein synthesized by ST was secreted. The total amount of both SGP-1 and CP-2 secreted by unstaged ST from immature rats was significantly lower than that secreted by unstaged ST from adult rats. The total amount of SGP-1 and CP-2 secreted by adult ST at stages IX-XIV of the spermatogenic cycle also declined dramatically compared to ST at earlier stages. The proportion of the total CP-2 synthesized by ST which was secreted also declined in all situations in which ES were absent from the seminiferous epithelium. The synthesis of only SGP-2 was changed by ES depletion from ST at stages VI-VIII, which was almost doubled compared to synthesis of this protein by ST from control rats. Our results suggest strongly that the secretion of SGP-1 and SGP-2 is via the constitutive pathway, and that regulation of these two proteins by ES is at the level of protein synthesis. In contrast, the regulation of CP-2 by ES is predominantly at the level of secretion, suggesting that this protein is secreted via a regulated pathway. Our findings add to the evidence showing that ES play a major role in the regulation of Sertoli cell function.
McKinnell
C
C
MRC Reproductive Biology Unit, Edinburgh, UK.
Sharpe
R M
RM
D000085:Acetates / Q000494:pharmacology; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000096:biosynthesis* / Q000378:metabolism; D051152:Clusterin; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D004792:Enzyme Precursors / Q000096:biosynthesis; D004848:Epithelium; D006023:Glycoproteins / Q000096:biosynthesis* / Q000378:metabolism; D008297:Male; D018832:Molecular Chaperones; D011498:Protein Precursors / Q000096:biosynthesis; D051381:Rats; D017207:Rats, Sprague-Dawley; D017208:Rats, Wistar; D049231:Saposins; D012671:Seminiferous Tubules / Q000502:physiology; D012708:Sertoli Cells / Q000378:metabolism / Q000502:physiology*; D013087:Spermatids / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D013091:Spermatogenesis
D000085:Acetates; D051152:Clusterin; D004792:Enzyme Precursors; D006023:Glycoproteins; D018832:Molecular Chaperones; D011498:Protein Precursors; C483344:Psap protein, mouse; C483347:Psap protein, rat; D049231:Saposins; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; C534278:Ctsl protein, mouse; C534280:Ctsl protein, rat; C013598:methoxyacetic acid