Differential expression and localization of ADAM10 and ADAM17 during rat spermatogenesis suggest a role in germ cell differentiation.

Paulina Urriola-Muñoz,Carlos Lizama,Raúl Lagos-Cabré,Ricardo D Moreno,Juan G Reyes

doi:10.1186/0717-6287-47-31

Abstract

BackgroundExtracellular metolloproteases have been implied in different process such as cell death, differentiation and migration. Membrane-bound metalloproteases of the ADAM family shed the extracellular domain of many cytokines and receptor controlling auto and para/juxtacrine cell signaling in different tissues. ADAM17 and ADAM10 are two members of this family surface metalloproteases involved in germ cell apoptosis during the first wave of spermatogenesis in the rat, but they have other signaling functions in somatic tissues.ResultsIn an attempt to further study these two enzymes, we describe the presence and localization in adult male rats. Results showed that both enzymes are detected in germ and Sertoli cells during all the stages of spermatogenesis. Interestingly their protein levels and cell surface localization in adult rats were stage-specific, suggesting activation of these enzymes at particular events of rat spermatogenesis.ConclusionsTherefore, these results show that ADAM10 and ADAM17 protein levels and subcellular (cell surface) localization are regulated during rat spermatogenesis.

Highlights

Extracellular metolloproteases have been implied in different process such as cell death, differentiation and migration
Once germ cells undergoing meiosis reach the leptone stage they detach from the basal lamina, and on their survival and differentiation relies upon specific interaction with the Sertoli cell
Results showed that ADAM10 mRNA levels in Dark segments were significantly higher than Weak segments (Figure 1A,A’) but protein levels were similar in all studied segments (Figure 1C,C’)

Summary

Introduction

Extracellular metolloproteases have been implied in different process such as cell death, differentiation and migration. Membrane-bound metalloproteases of the ADAM family shed the extracellular domain of many cytokines and receptor controlling auto and para/juxtacrine cell signaling in different tissues. Once germ cells undergoing meiosis ( named spermatocytes) reach the leptone stage they detach from the basal lamina, and on their survival and differentiation relies upon specific interaction with the Sertoli cell. ADAM proteases are type 1 transmembrane proteins of approximately 70 to 120 kDa (mature proteins; the unprocessed precursors are about 20 kDa heavier due to their prodomain) They consist of a common modular ectodomain structure encompassing a variable transmembrane region; a cysteinerich domain that can interact with cell surface proteoglycans and in some cases contains a fusion peptide sequence; a disintegrin domain; a zinc-binding metalloprotease domain; and a prodomain that is cleaved off in the trans-Golgi network by protein convertases [9]. In the male reproductive tract, ADAMs are differentially expressed in testes, epidydymis, efferent duct and prostate suggesting their function is regulated according to requirements of each organ [10]

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Results

Discussion

Conclusion