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Hirota K.,Tokyo University of Science | Nakagawa Y.,Morita Pharmaceutical Ind. Ltd. | Takeuchi R.,Morita Pharmaceutical Ind. Ltd. | Uto Y.,Tokushima University | And 3 more authors.
Anticancer Research | Year: 2013

Background: Group-specific component (Gc)- globulin-derived macrophage-activating factor (GcMAF) generated by a cascade of catalytic reactions with deglycosidase enzymes exerts antitumor activity. We hypothesized that degalactosyl Gc-globulin (DG3), a precursor of GcMAF, also plays a role in recovery from cancer as well as GcMAF due to progression of deglycosylation by generally resident sialidases and mannosidases. Materials and Methods: We prepared the subtypes of DG3, such as 1f1f and 1s1s and its 22 homodimers, by using vitamin D3-binding Sepharose CL-6B and examined their antitumor activity in mice bearing Lewis lung carcinoma cells, by counting the number of nodules formed in their lungs. Results: Antitumor activity of DG3 was observed regardless of its subtype, being equivalent to that of GcMAF. The injection route of DG3 affected its antitumor activity, with subcutaneous and intramuscular administration being more favorable than the intraperitoneal or intravenous route. In order to obtain significant antitumor activity, more than 160 ng/kg of DG3 were required. Conclusion: DG3 proved to be promising as an antitumor agent, similarly to GcMAF.


Uto Y.,Tokushima University | Yamamoto S.,Tokushima University | Mukai H.,Tokushima University | Ishiyama N.,Tokushima University | And 7 more authors.
Anticancer Research | Year: 2012

Background: The 1f1f subtype of the group-specific component (Gc) protein is converted into Gc proteinderived macrophage-activating factor (GcMAF) by enzymatic processing with β-galactosidase and sialidase. We previously demonstrated that preGc 1f1fMAF, a full Gc1f1f protein otherwise lacking a galactosyl moiety, can be converted to GcMAF by treatment with mouse peritoneal fluid. Here, we investigated the effects of the β-galactosidase-treated 1s1s and 22 subtypes of Gc protein ( preGc1s1sMAF and preGc22MAF) on the phagocytic activation of mouse peritoneal macrophages. Results: We demonstrated the presence of Gal-GalNAc disaccharide sugar structures in the Gc1s1s protein by western blotting using peanut agglutinin and Helix pomatia agglutinin lectin. We also found that preGc1s1sMAF and preGc22MAF significantly enhanced the phagocytic activity of mouse peritoneal macrophages in the presence and absence of mouse peritoneal fluid. Conclusion: We demonstrate that preGc1s1sMAF and preGc22MAF proteins can be used as effective macrophage activators.


Takeuchi R.,Tokushima University | Takeuchi R.,Morita Pharmaceutical Ind. Ltd. | Uto Y.,Tokushima University | Nakagawa Y.,Morita Pharmaceutical Ind. Ltd. | And 3 more authors.
Anticancer Research | Year: 2010

Aim: We performed a retrospective analysis of a calcium hydroxide-containing calcium agent (TACHIKAWA DENKAI CALCIUM™ : E-Ca) based on data of bone mineral density obtained by dual-energy X-ray absorptiometry (DXA) to clarify the relationship between bone mineral density and E-Ca intake on an empty stomach in those who regularly use E-Ca. Results: We found the percentage of volunteers with their age-matched (AM) values of above 100% to be 89%, and also a moderate positive correlation between AM values and the intake period of E-Ca. Conclusion: Our findings demonstrate that AM values can be used as an effective indicator assessing osteogenesis by regularly administrated calcium agents which exert their effects after long-term use.


Uto Y.,Tokushima University | Yamamoto S.,Tokushima University | Takeuchi R.,Tokushima University | Takeuchi R.,Morita Pharmaceutical Ind. Ltd. | And 6 more authors.
Anticancer Research | Year: 2011

Background: The 1f1f subtype of the Gc protein (Gc 1f1f-protein) was converted into Gc-derived macrophage-activating factor (GcMAF) by enzymatic processing in the presence of β-galactosidase of an activated B-cell and sialidase of a T-cell. We hypothesized that preGc 1f1fMAF, the only Gc1f1f protein lacking galactose, can be converted to GcMAF in vivo because sialic acid is cleaved by residual sialidase. Hence, we investigated the effect of preGc 1f1fMAF on the phagocytic activation of mouse peritoneal macrophages. Results: We examined the sugar moiety of preGc 1f1fMAF with a Western blot using peanut agglutinin (PNA) and Helix pomatia agglutinin (HPA) lectin. We also found that preGc 1f1fMAF significantly enhanced phagocytic activity in mouse peritoneal macrophages but only in the presence of the mouse peritoneal fluid; the level of phagocytic activity was the same as that observed for GcMAF. Conclusion: PreGc 1f1fMAF can be used as an effective macrophage activator in vivo.

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