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2001 SEP 12 - (NewsRx.com & NewsRx.net) --
The endoplasmic reticulum resident chaperone protein calreticulin plays a surprising variety of roles in cell regulation, some of which make it particularly appealing for antitumor vaccination.
This protein can be cleaved in vivo to form the potent antiangiostatic factor vasostatin. In addition, when expressed in antigen-presenting cells, calreticulin interacts with the peptide processing machinery to facilitate loading of associated peptides with the Class I MHC complex.
Building on recent evidence that presentation of tumor-associated peptides through calreticulin can promote tumoricidal immune responses, Wen-Fang Cheng, of the National Taiwan University Hospital, and colleagues there and at the Johns Hopkins Medical Institutions have engineered a fusion gene encoding a known viral tumor antigen, linked directly to the chaperone.
They report in the September 2001 Journal of Clinical Investigation that mice exposed subdermally to this DNA construct enjoy seemingly complete resistance to tumor cells that express the viral antigen. Conversely, a simple ...
Source: HighBeam Research, DNA Vaccination Places Tumors In Double Jeopardy.(Brief Article)