Ocul Immunol Inflamm
October 2006
Purpose: Demonstration of experimental autoimmune uveitis (EAU) with extremely small, fragmented peptides (12-30 amino acid residues) of interphotoreceptor retinoid-binding protein (IRPB).
Method: Very small fragmented peptides (no. 854, 888, 907, and 1057) were conjugated to heat-killed Group A Streptococcus cells and administered as a single intravenous injection to Lewis rats.
Administration of a small dose (300 ng/mouse) of photofrin II (PII) to mice, followed by 4 days of exposure to only ambient fluorescent light in animal quarters, induced Fc-receptor-mediated phagocytic and superoxide-generating capacities of peritoneal macrophages by five- and seven-fold, respectively. When these mice were kept in the dark for 4 days, no activation of macrophages was observed. These results suggest that macrophage activation is a consequence of photodynamic activation.
View Article and Find Full Text PDFTo allow for structural analysis of the human acetylcholinesterase (hAChE) subunit, a series of eukaryotic vectors was designed for efficient expression. Several eukaryotic multicistronic expression vectors were tested in various mammalian cell lines. All expression vectors contained the selectable neo gene under control of a weak promoter, while the hAChE cDNA was under control of the cytomegalovirus (CMV) immediate-early or Rous sarcoma virus long terminal repeat (RSV LTR) or simian virus 40 (SV40) early promoters.
View Article and Find Full Text PDF1. Coding sequences for the human acetylcholinesterase (HuAChE; EC 3.1.
View Article and Find Full Text PDFPeritoneal macrophages treated in vivo with haematoporphyrin derivative (HPD) exhibited significant enhancement of Fc receptor mediated ingestion activity. To examine this process more rigorously, we studied photodynamic activation of macrophages by exposure in vitro of mouse peritoneal cell cultures (containing macrophages and B and T-lymphocytes) to HPD and red fluorescent light. A short (10 s) exposure of peritoneal cells in medium containing 0.
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