Abstract

Adamts9 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 9) is one of a few metalloproteinases structurally conserved from C. elegans to humans and is indispensable in germ cell migration in invertebrates. However, adamts9′s roles in germ cell migration in vertebrates has not been examined. In the present study, we found zygotic expression of adamts9 started around the germ ring stage and reached peak levels at 3 days post fertilization (dpf) in zebrafish. The migration of primordial germ cells (PGC) was completed within 24 hours (h) in wildtype siblings, while a delay in PGC migration was found at 15 and 24-h post-fertilization (hpf) in the Adamts9 knockout (KO). However, the delayed PGC migration in Adamts9 KO disappeared at 48 hpf. Our study suggests a conserved function of Adamts9 in germ cell migration among invertebrates and vertebrates. In addition, our results also suggest that Adamts9 is not essential for germ cell migration as reported in C. elegans, possibly due to expansion of Adamts family members and compensatory roles from other metalloproteinases in vertebrates. Further studies are required in order to elucidate the functions and mechanisms of metalloproteinases in germ cell migration and gonad formation in vertebrates.

Highlights

  • Adamts[9] is one of a few metalloproteinases structurally conserved from C. elegans to humans and is indispensable in germ cell migration in invertebrates

  • Adamts[9] (NP_001244125) shares high sequence identities with its orthologs in C. elegans, Drosophila, mice and human (Fig.[1], supplemental Figs.[1] and 2, supplemental Tables 1–4)

  • Sequence identities (40-88%) between C. elegans and human were found in the metalloproteinase domain of Adamts[9] (Supplemental Table 2), while an amino acid motif (HELGHXXXXXHDD) for the Adamts[9] enzymatic activation site was completely conserved and aligned (Supplemental Fig. 1)

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Summary

Introduction

Adamts[9] (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 9) is one of a few metalloproteinases structurally conserved from C. elegans to humans and is indispensable in germ cell migration in invertebrates. Our study suggests a conserved function of Adamts[9] in germ cell migration among invertebrates and vertebrates. Further studies are required in order to elucidate the functions and mechanisms of metalloproteinases in germ cell migration and gonad formation in vertebrates. A functional, adult ovary or testis develops from a juvenile bipotential gonad via several physiological processes that include cell migration, apoptosis, proliferation, and tissue remodeling. These processes are regulated precisely by various cellular signaling molecules and proteinases. A delay in the migration of primordial germ cells was found during the gonadal development

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