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Involvement of trypsin-digested silk peptides in the induction of RAW264.7 macrophage activation
Kyoung-Ho Pyo1, Min-Ki Kim1, Kwang-Soon Shin2
1Department of Parasitology and Tropical Medicine, Seoul National University College of Medicine and Institute of Endemic Diseases, Seoul National University Medical Research Center, Seoul 110-799, Republic of Korea.
Abstract:
The activation of macrophages by trypsin-digested silk peptides was investigated by considering CD1 lb and CD40 expression in the RAW264.7 cell, a murine macrophage. Silk protein hydrolysates were digested with trypsin, following by centrifugal purification using the Centriprep 30k concentrator. Trypsin-digested total silk peptides and its centrifugal fractions were tested for macrophage activation in vitro. The functional peptide of fractionated silk peptides was examined by LC/MS/MS analysis. Trypsin-digested and fractionated silk peptides of more than 30 kDa induced an increase in the activation markers CD1 lb and CD40 in RAW264.7 cells. These results are supported by morphological changes reflecting an increase in the number of dendrites in activated cells. The fractionated silk peptides examined by LC/MS/MS contained partial peptides of Bombyx mori fibroin. These results suggest that the activation of RAW264.7 macrophages may be induced not by sericin-derived peptides but by fibroin-derived ones.
