1. Antitumor and antimicrobial glycoproteins from sea hares
M Yamazaki Comp Biochem Physiol C Comp Pharmacol Toxicol. 1993 Jun;105(2):141-6. doi: 10.1016/0742-8413(93)90185-n.
1. Novel antitumor and antimicrobial glycoproteins were found in the sea hares. These glycoproteins were purified to apparent homogeneity from Aplysia kurodai, Aplysia juliana and Dolabella auricularia, and designated as aplysianins, julianins and dolabellanins, respectively. 2. The nine isolated glycoproteins lysed all the tumor cells tested but did not lyse normal white and red blood cells. 3. The glycoproteins completely inhibited the synthesis of DNA and RNA by tumor cells within 2 hr and caused tumor lysis within 15 hr. 4. Tumor lysis was inhibited by the presence of N-acetylneuraminic acid, suggesting that the recognition of the sugar moiety is a key step in the cytolysis by antitumor glycoproteins from sea hares. 5. These antitumor glycoproteins, except dolabellanin P, also showed antimicrobial activities. 6. The factors were active for Gram-positive and -negative bacteria and some fungi, and their action was not cytocidal but cytostatic. 7. They exerted the antibacterial action by inhibiting nucleic acid synthesis, as does a DNA-inhibiting chemotherapeutic drug. 8. The sequence of the N-terminal part of dolabellanin A was similar to other antibacterial peptides from arthropoda, amphibia and mammals, suggesting that dolabellanin-like antibacterial peptides are common throughout the animal kingdom.
2. Biopolymers from marine invertebrates. XIII. Characterization of an antibacterial protein, dolabellanin A, from the albumen gland of the sea hare, Dolabella auricularia
J Kisugi, H Ohye, H Kamiya, M Yamazaki Chem Pharm Bull (Tokyo). 1992 Jun;40(6):1537-9. doi: 10.1248/cpb.40.1537.
An antibacterial factor, dolabellanin A, was purified from the albumen gland of a sea hare, Dolabella auricularia. Purified dolabellanin A was a glycoprotein of 250 kilodaltons consisting of 4 subunits, and showed both antibacterial and antineoplastic activities. The two activities were lost in parallel on heating and at low and high pH. This factor was half-maximally active for gram-positive and -negative bacteria at 0.018-0.48 microgram/ml, and its action was not bactericidal but bacteriostatic. Dolabellanin A did not induce morphological elongation of bacteria or the release of adenosine triphosphate, but it completely inhibited the syntheses of deoxyribonucleic acid (DNA) and ribonucleic acid by E. coli within 6 min. These results suggest that dolabellanin A, which is found in a marine invertebrate, the sea hare, is a new antibacterial protein, and that it exerts its action by inhibiting nucleic acid synthesis, as does a DNA-inhibiting chemotherapeutic drug.
3. Purification and characterization of a cytolytic protein from purple fluid of the sea hare, Dolabella auricularia
M Yamazaki, S Tansho, J Kisugi, K Muramoto, H Kamiya Chem Pharm Bull (Tokyo). 1989 Aug;37(8):2179-82. doi: 10.1248/cpb.37.2179.
A novel cytolytic factor, dolabellanin P, was purified to apparent homogeneity from the purple fluid of the sea hare, Dolabella auricularia. Purified dolabellanin P is a single polypeptide of 60 kDa. The amino acid composition and the N-terminus of the factor were also determined. This factor nonspecifically lysed all the cells tested at 50-200 ng protein/ml. Dolabellanin P caused complete cytolysis within 2 h. The factor is distinct from antineoplastic glycoproteins previously isolated from eggs (aplysianin E) or albumen gland (aplysianin A) of Aplysia kurodai in terms of certain cytolytic properties. These results suggest that dolabellanin P, found in the sea hare, a marine invertebrate, is a new cytolytic factor.
