Reference - Detail
| RRC ID | 54246 |
|---|---|
| Author | Saitoh Y, Katane M, Miyamoto T, Sekine M, Sakamoto T, Imai H, Homma H. |
| Title | Secreted d-aspartate oxidase functions in C. elegans reproduction and development. |
| Journal | FEBS J |
| Abstract |
d-Aspartate oxidase (DDO) is a degradative enzyme that acts stereospecifically on free acidic D-amino acids such as d-aspartate and d-glutamate. d-Aspartate plays an important role in regulating neurotransmission, developmental processes, hormone secretion, and reproductive functions in mammals. In contrast, the physiological role of d-glutamate in mammals remains unclear. In Caenorhabditis elegans, the enzyme responsible for in vivo metabolism of d-glutamate is DDO-3, one of the three DDO isoforms, which is also required for normal self-fertility, hatching, and lifespan. In general, eukaryotic DDOs localize to subcellular peroxisomes in a peroxisomal targeting signal type 1 (PTS1)-dependent manner. However, DDO-3 does not contain a PTS1, but instead has a putative N-terminal signal peptide (SP). In this study, we found that DDO-3 is a secreted DDO, the first such enzyme to be described in eukaryotes. In hermaphrodites, DDO-3 was secreted from the proximal gonadal sheath cells in a SP-dependent manner and transferred to the oocyte surface. In males, DDO-3 was secreted from the seminal vesicle into the seminal fluid in a SP-dependent manner during mating with hermaphrodites. In both sexes, DDO-3 was secreted from the cells where it was produced into the body fluid and taken up by scavenger coelomocytes. Full-length DDO-3 transgene rescued all phenotypes elicited by the deletion of ddo-3, whereas a DDO-3 transgene lacking the putative SP did not. Together, these results indicate that secretion of DDO-3 is essential for its physiological functions. |
| Volume | 286(1) |
| Pages | 124-138 |
| Published | 2019-1-1 |
| DOI | 10.1111/febs.14691 |
| PMID | 30387556 |
| MeSH | Animals Aspartic Acid / metabolism* Caenorhabditis elegans / embryology Caenorhabditis elegans / enzymology* Caenorhabditis elegans / growth & development* D-Aspartate Oxidase / genetics D-Aspartate Oxidase / metabolism* Embryo, Nonmammalian / cytology* Embryo, Nonmammalian / enzymology Embryo, Nonmammalian / physiology Fertility Longevity Mammals Nose / physiology Reproduction* |
| IF | 4.392 |
| Times Cited | 3 |
| Altmetric score |
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| C.elegans | tm2028 |