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Study of response of Swiss Webster mice to light subunit of mushroom tyrosinase.

Wangsa Tirta IsmayaA EfthyaniD S RetnoningrumX LaiBauke W DijkstraRaymond Rubianto TjandrawinataH Rachmawati
Published in: Biotechnic & histochemistry : official publication of the Biological Stain Commission (2017)
The light subunit of mushroom, Agaricus bisporus, tyrosinase (LSMT), has been identified as an extrinsic component of the enzyme. Its function is unknown, but it can cross an epithelial cell layer, which suggests that it can be absorbed by the intestine. A similar capability has been demonstrated for the HA-33 component of the progenitor toxin from Clostridium botulinum, which is the closest structural homolog of LSMT. Unlike HA-33, LSMT appears to be non-immunogenic as shown by preliminary tests in Swiss Webster mice. We investigated the immunogenicity and histopathology of LSMT in mice to determine its safety in vivo. LSMT did not evoke generation of antibodies after prolonged periods of intraperitoneal administration. Histopathological observations confirmed the absence of responses in organs after twelve weekly administrations of LSMT. We found that LSMT is not toxic and is less immunogenic than the C. botulinum HA-33 protein, which supports further research and development for pharmaceutical application.
Keyphrases
  • high fat diet induced
  • escherichia coli
  • wild type
  • mass spectrometry
  • adipose tissue
  • atomic force microscopy
  • high resolution