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Biology of Reproduction, Vol 50, 835-844, Copyright © 1994 by Society for the Study of Reproduction
ARTICLES |
T Satoh, K Kobayashi, S Yamashita, M Kikuchi, Y Sendai and H Hoshi
Research Institute for the Functional Peptides, Yamagata, Japan.
Embryogenesis-stimulating activity (ESA) was found in serum-free conditioned media (CM) of bovine cumulus/granulosa cells (BGC) and bovine oviductal epithelial cells (BOEC). The CM of BGC (BGC-CM) contained two molecular species of ESA, one with a low molecular weight (M(r) 30,000) and another with a high molecular weight (M(r) 80,000); but only the activity with low molecular weight was detected in CM of BOEC by gel-permeation chromatography. The smaller ESA (embryogenin-1) in BGC-CM was purified to homogeneity, as a common activity in both CM by a combination of gel-permeation chromatography, ion-exchange chromatography, and reverse-phase HPLC. Embryogenin-1 has a molecular weight of 31,100 (reduced) and has been identified as a bovine tissue inhibitor of metalloproteinase-1 by NH2-terminal amino acid sequence analysis. Western blot analysis, anti-proteinase activities against metalloproteinases, and the nucleotide sequence of cDNA isolated from a lambda gt11 cDNA library of the bovine ovary by a polyclonal antibody against embryogenin-1. These data suggest that the tissue inhibitor of metalloproteinase-1 produced by BGC and BOEC is a major ESA for in vitro development of bovine embryos.
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