Participation of D-serine in the development and reproduction of the silkworm Bombyx mori

Minoru Tanigawa, Chihiro Suzuki, Kimio Niwano, Rensuke Kanekatsu, Hiroyuki Tanaka, Kihachiro Horiike, Kenji Hamase, Yoko Nagata

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The silkworm Bombyx mori contains high concentrations of free D-serine, an optical isomer of l-serine. To elucidate its function, we first investigated the localization of D-serine in various organs of silkworm larvae, pupae, and adult moths. Using immunohistochemical analysis with an anti-D-serine antibody, we found D-serine in the microvilli of midgut goblet and cylindrical cells and in peripheral matrix components of testicular and ovarian cells. By spectrophotometric analysis, D-serine was also found in the hemolymph and fat body. d-Alanine was not detected in the various organs by immunohistochemistry. Serine racemase, which catalyzes the inter-conversion of l- and D-serine, was found to co-localize with D-serine, and D-serine production from l-serine by intrinsic serine racemase was suggested. O-Phospho-L-serine is an inhibitor of serine racemase, and it was administered to the larvae to reduce the D-serine level. This reagent decreased the midgut caspase-3 level and caused a delay in spermatogenesis and oogenesis. The reagent also decreased mature sperm and egg numbers, suggesting D-serine participation in these processes. D-serine administration induced an increase in pyruvate levels in testis, midgut, and fat body, indicating conversion of D-serine to pyruvate. On the basis of these results, together with our previous investigation of ATP biosynthesis in testis, we consider the possible involvement of D-serine in ATP synthesis for metamorphosis and reproduction.

Original languageEnglish
Pages (from-to)20-29
Number of pages10
JournalJournal of insect physiology
Volume87
DOIs
Publication statusPublished - Apr 1 2016

All Science Journal Classification (ASJC) codes

  • Physiology
  • Insect Science

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