BmECM25, from the silkworm Bombyx mori, is an extracellular matrix protein

Insect Biochem Mol Biol. 2015 Oct:65:68-74. doi: 10.1016/j.ibmb.2015.06.004. Epub 2015 Jun 9.

Abstract

BmECM25 (previously reported as BmVMP25) was previously predicted as a gene encoding the vitelline membrane protein in silkworm, Bombyx mori. In this study, we investigated the detail temporal and spatial patterns of BmECM25 protein. Western blot results showed that BmECM25 was expressed in the follicular epithelium cells from stages -6 to +1, and was then secreted into the oocytes. However, the abundance of BmECM25 decreased during the subsequent oogenesis and finally disappeared in the mature follicles. Immunofluorescence detection showed that BmECM25 locates inside the VM layer and forms a discontinuous layer. These features of BmECM25 suggest that it is an oocyte membrane matrix protein, not a vitelline membrane protein.

Keywords: Bombyx mori; Follicular epithelium cell; Oogenesis; Vitelline membrane protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bombyx / genetics
  • Bombyx / growth & development
  • Bombyx / metabolism*
  • Extracellular Matrix Proteins / metabolism*
  • Female
  • Gene Expression Regulation, Developmental
  • Insect Proteins / genetics
  • Insect Proteins / metabolism*
  • Oocytes / metabolism
  • Oogenesis
  • Ovarian Follicle / metabolism
  • Vitelline Membrane / metabolism

Substances

  • Extracellular Matrix Proteins
  • Insect Proteins