Radioprotective properties of Cumaside, a complex of triterpene glycosides from the sea cucumber Cucumaria japonica and cholesterol.

The radioprotective activity has been studied of a new immunomodulatory lead material, Cumaside, which is a complex of monosulfated triterpene glycosides from the edible sea cucumber Cucumaria japonica and cholesterol. Female CD-1 strain mice administered with prophylactic doses of Cumaside were irradiated using a Gamma-therapeutic device with a 60Co source (exposure dose 6.5 Gy, dose rate 1.14 Gy/min) and the average life span of the mice was determined. The animals administrated with Cumaside and irradiated were killed by pervisceral dislocation on days 4 and 9. Peripheral blood cell composition indexes, blood forming function and cell number in blood-forming organs and the number of pluripotent blood-forming stem cells were determined using standard procedures and the results compared with those of non-treated irradiated mice. The survivability percentage and average life span of the irradiated mice that were not treated with Cumaside were decreased in comparison with the Cumaside-treated groups. Especially, the leukocyte and neutrophil numbers in the blood (bone marrow from hip), and the weight and cell number of lymphoid organs were higher in the Cumaside-treated groups compared with the non-treated irradiated mice. It was concluded that at low prophylactic doses Cumaside possesses moderate radioprotective properties.

Molecular characterization and therapeutic potential of a marine bacterium Pseudoalteromonas sp. KMM 701 alpha-galactosidase.

An alpha-galactosidase capable of converting B red blood cells into the universal blood type cells at the neutral pH was produced by a novel obligate marine bacterium strain KMM 701 (VKM B-2135 D). The organism is heterotrophic, aerobic, and halophilic and requires Na+ ions and temperature up to 34 degrees C for its growth. The strain has a unique combination of polysaccharide-degrading enzymes. Its single intracellular alpha-galactosidase exceeded other glycoside hydrolases in the level of expression up to 20-fold. The alpha-galactosidase was purified to determine the N-terminal amino acid sequences and new activities. It was found to inhibit Corynebacterium diphtheria adhesion to host buccal epithelium cell surfaces with high effectiveness. The nucleotide sequence of the homodimeric alpha-galactosidase indicates that its subunit is composed of 710 amino acid residues with a calculated Mr of 80,055. This alpha-galactosidase shares structural property with 36 family glycoside hydrolases. The properties of the enzyme are likely to be highly beneficial for medicinal purposes.