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Allergenic components of bald-faced hornet (V. maculata) venom
novel dimeric indole alkaloid with potent anti-implantation activity has been isolated from the roots of Murraya parriculesta and identified as a racemic mixture of 6ß-(3'-indolyl}7c,7ß,9-trimethyl6aß,7,8,10aß-tetrahydroindrnol[2,1-blindole and its enantiomer . YUEHCHUKENE, a
H.P .
KOLM
and BLUMENTHAL, K. M. (Department of Biological Chemistry, University of Cincinnati College of Medicine, Cincinnati, OH 43267-0322, U.S .A .) Structure and action of heteronemertine polypeptide toxins: importance of amphipathic helix for activity of Cerebratulus lacteus toxin A-III. Archs Biochem. Biophys. 236, 167 (1985) . DUMONT, J. A.
heteronemertine Cenbrestulus lacteus produces a family of protein cytolysins designated as Atoxins . Limited subtilisin digests of the most abundant homolog, toxin A-III, yield two major products which may be purified by high-performance liquid chromatography . One product is shown to represent residua 1- 86 and the other contains the rntire toxin sequence (1- 95). Both polypeptida are shown to lack internal protease nicks. The 1- 95 polypeptide retains full cytolytic activity in comparison to native toxin, whereas I - 86 has an activity that is approximately four times lower. Extensive treatment of A-Ill with carboxypeptidase Y yields a polypeptide containing residua 1- 75 which is totally devoid of hemolytic activity . Residua 63 - 95 of native AIII have been predicted to form a relatively hydrophobic c-helix which is potentially important for activity . The circular dichroism spectrum of 1- 93 is in excellent agreement with both experimental and Chou - Fasmanpredicted secondary structures of native A-III, while the spectra of 1- 86 and I - 75 indicate a loss of helicity quantitatively consistrnt with the removal of residua 87-95 and 76-93, respectively . Combined with our earlier data on bilayer penetration by N-terminal sequences [BLUMENTHAL, K. M . (1982) Biochemistry 21, 4229], the current results indicate a direct involvemrnt of both ends of A-III in lyric activity . The C-terminal region may function by contributing a membrane binding site in the form of an amphipathic helix. THE MARINE
(Author's abstract)
H.
P . KGLM
J. 1., NOBLE, R. W., AasvouNls, C. J . and REISMAN, R. E. (Allergy Research Laboratory, Buffalo General Hospital, Departmrnt of Medicine, Allergy Division, Department of Pathology, Departmrnt of Biochemistry and Department of Microbiology, State University of New York at Buffalo, Buffalo, N.Y ., U .S .A.) Allergrnic componrnts of balä-faced hornet (V. maculates) venom. lnt. Archs Allergy appl. Immun. 76, 1 (19ßS) . LITTLER, S., WYPYCH,
IV.maculata) venom collected by electrical stimulation was fractionated using molecular exclusion gel-filtration and ion-exchange chromatography . Four fractions were selected for in-depth analysis . These were analyzed for phospholipase, hyaluronidase and protease enzyme activities, antigrnicity as measured by reaction with anti-hornet vrnom rabbit serum and allergenic activity as determined by RAST reaction with sera from hornet-sensitive patients . The results of these studies suggest that the fractions containing phospholipase, hyaluronidase and protease possess allergenic activity . In addition, there appear to be other allergenic components in hornet venom. Allergic patients differ in their reactivity to the various allergenic componrnts in hornet venom and may have IgE antibodies to one or more of these components . BALD-FACED HORNET
(Author's abstract)
H. P.
KGLM
A. U., HORTOBAGYI, G. N., BODEY, G. P. and BLUMENSCHEIN, G. R . (Department of Medical Oncology, University of Texas, and M. D. Anderson Hospital and Tumor Institute at Houston, Houston, Texas, U.S .A .) A comparative randomized trial of Vinces alkaloids in patients with metastatic breast carcinoma. Cancer SS, 337 (1983) . YAU, J. C., YAP, Y .-Y., BUZDAR,
of vincristine, vinblastine and vindesine were evaluated in a prospective randomized trial in patients with metastatic breast carcinoma. All patients were refraaory to doxorubicin-containing chemotherapy . Vincristine was administered at 0.4 mg/M'/1/day by continuous infusion (Cl), vinblastine at 1 .7 mg/M'/1/day by Cl, and vindesine at 1 .2 mg/M'/1/day by CI or intermittent bolus (1B) over 5 days . The courses were administered at 2 week intervals for vincristine and 3 week intervals for vinblastine and vindesine. Ninety-nine patients were evaluable for response . The l5 patients treated with vincristine had no objective response . Of 23 patirnts treated with vinblastine, there were 2 complete raponsa (9010) and S partial responses (2290). Of 31 patients treated with CI vindesine, there were 6 partial responses (19010). Of 30 patients treated with IB vindesine, there were S partial responses (1790) . The median duration of disease control was 13 weeks (range 8-140+) for vinblastine, 18 weeks (range 8-34) for CI vindesine, and 20 weeks (range 12-47) for IB vindesine. These data illustrate that vinblastine (CI) and vindesine (CI or IB) have significant antitumor activity in patients with refractory metastatic breast carcinoma and that vincristine has no antitumor activity in similar patients . THE THERAPEUTIC efil(:aCy
(Author's abstract)
H.
P. KGLM
H.P .
KOLM
and BLUMENTHAL, K. M. (Department of Biological Chemistry, University of Cincinnati College of Medicine, Cincinnati, OH 43267-0322, U.S .A .) Structure and action of heteronemertine polypeptide toxins: importance of amphipathic helix for activity of Cerebratulus lacteus toxin A-III. Archs Biochem. Biophys. 236, 167 (1985) . DUMONT, J. A.
heteronemertine Cenbrestulus lacteus produces a family of protein cytolysins designated as Atoxins . Limited subtilisin digests of the most abundant homolog, toxin A-III, yield two major products which may be purified by high-performance liquid chromatography . One product is shown to represent residua 1- 86 and the other contains the rntire toxin sequence (1- 95). Both polypeptida are shown to lack internal protease nicks. The 1- 95 polypeptide retains full cytolytic activity in comparison to native toxin, whereas I - 86 has an activity that is approximately four times lower. Extensive treatment of A-Ill with carboxypeptidase Y yields a polypeptide containing residua 1- 75 which is totally devoid of hemolytic activity . Residua 63 - 95 of native AIII have been predicted to form a relatively hydrophobic c-helix which is potentially important for activity . The circular dichroism spectrum of 1- 93 is in excellent agreement with both experimental and Chou - Fasmanpredicted secondary structures of native A-III, while the spectra of 1- 86 and I - 75 indicate a loss of helicity quantitatively consistrnt with the removal of residua 87-95 and 76-93, respectively . Combined with our earlier data on bilayer penetration by N-terminal sequences [BLUMENTHAL, K. M . (1982) Biochemistry 21, 4229], the current results indicate a direct involvemrnt of both ends of A-III in lyric activity . The C-terminal region may function by contributing a membrane binding site in the form of an amphipathic helix. THE MARINE
(Author's abstract)
H.
P . KGLM
J. 1., NOBLE, R. W., AasvouNls, C. J . and REISMAN, R. E. (Allergy Research Laboratory, Buffalo General Hospital, Departmrnt of Medicine, Allergy Division, Department of Pathology, Departmrnt of Biochemistry and Department of Microbiology, State University of New York at Buffalo, Buffalo, N.Y ., U .S .A.) Allergrnic componrnts of balä-faced hornet (V. maculates) venom. lnt. Archs Allergy appl. Immun. 76, 1 (19ßS) . LITTLER, S., WYPYCH,
IV.maculata) venom collected by electrical stimulation was fractionated using molecular exclusion gel-filtration and ion-exchange chromatography . Four fractions were selected for in-depth analysis . These were analyzed for phospholipase, hyaluronidase and protease enzyme activities, antigrnicity as measured by reaction with anti-hornet vrnom rabbit serum and allergenic activity as determined by RAST reaction with sera from hornet-sensitive patients . The results of these studies suggest that the fractions containing phospholipase, hyaluronidase and protease possess allergenic activity . In addition, there appear to be other allergenic components in hornet venom. Allergic patients differ in their reactivity to the various allergenic componrnts in hornet venom and may have IgE antibodies to one or more of these components . BALD-FACED HORNET
(Author's abstract)
H. P.
KGLM
A. U., HORTOBAGYI, G. N., BODEY, G. P. and BLUMENSCHEIN, G. R . (Department of Medical Oncology, University of Texas, and M. D. Anderson Hospital and Tumor Institute at Houston, Houston, Texas, U.S .A .) A comparative randomized trial of Vinces alkaloids in patients with metastatic breast carcinoma. Cancer SS, 337 (1983) . YAU, J. C., YAP, Y .-Y., BUZDAR,
of vincristine, vinblastine and vindesine were evaluated in a prospective randomized trial in patients with metastatic breast carcinoma. All patients were refraaory to doxorubicin-containing chemotherapy . Vincristine was administered at 0.4 mg/M'/1/day by continuous infusion (Cl), vinblastine at 1 .7 mg/M'/1/day by Cl, and vindesine at 1 .2 mg/M'/1/day by CI or intermittent bolus (1B) over 5 days . The courses were administered at 2 week intervals for vincristine and 3 week intervals for vinblastine and vindesine. Ninety-nine patients were evaluable for response . The l5 patients treated with vincristine had no objective response . Of 23 patirnts treated with vinblastine, there were 2 complete raponsa (9010) and S partial responses (2290). Of 31 patients treated with CI vindesine, there were 6 partial responses (19010). Of 30 patients treated with IB vindesine, there were S partial responses (1790) . The median duration of disease control was 13 weeks (range 8-140+) for vinblastine, 18 weeks (range 8-34) for CI vindesine, and 20 weeks (range 12-47) for IB vindesine. These data illustrate that vinblastine (CI) and vindesine (CI or IB) have significant antitumor activity in patients with refractory metastatic breast carcinoma and that vincristine has no antitumor activity in similar patients . THE THERAPEUTIC efil(:aCy
(Author's abstract)
H.
P. KGLM