Biosynthesis of 3-methoxy-5-methyl naphthoic acid and its incorporation into the antitumor antibiotic azinomycin B

2010 ◽  
Vol 6 (6) ◽  
pp. 1071 ◽  
Author(s):  
Wei Ding ◽  
Wei Deng ◽  
Mancheng Tang ◽  
Qi Zhang ◽  
Gongli Tang ◽  
...  
Keyword(s):  
Antitumor Antibiotic ◽  
Naphthoic Acid ◽  
Azinomycin B

Characterization of NcsB2 as a Promiscuous Naphthoic Acid/Coenzyme A Ligase Integral to the Biosynthesis of the Enediyne Antitumor Antibiotic Neocarzinostatin

2007 ◽  
Vol 129 (25) ◽  
pp. 7728-7729 ◽  
Author(s):  
Heather A. Cooke ◽  
Jian Zhang ◽  
Meghan A. Griffin ◽  
Koichi Nonaka ◽  
Steven G. Van Lanen ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Antitumor Antibiotic ◽  
Naphthoic Acid ◽  
Coenzyme A Ligase

Novel interstrand cross-links induced by the antitumor antibiotic carzinophilin/azinomycin B

1992 ◽  
Vol 114 (8) ◽  
pp. 3144-3145 ◽  
Author(s):  
Robert W. Armstrong ◽  
Mark E. Salvati ◽  
Michael Nguyen
Keyword(s):  
Antitumor Antibiotic ◽  
Interstrand Cross Links ◽  
Cross Links ◽  
Azinomycin B

Pulse polarographic study of the behaviour of some o,o'-dihydroxyazo-compounds

1989 ◽  
Vol 54 (5) ◽  
pp. 1219-1226 ◽  
Author(s):  
Enric Casassas ◽  
Miquel Esteban ◽  
Santiago Alier
Keyword(s):  
Carboxylic Acid ◽  
Reaction Mechanisms ◽  
Sulphonic Acid ◽  
Base Catalysis ◽  
Polarographic Study ◽  
Acid Base ◽  
Eriochrome Black T ◽  
Naphthoic Acid ◽  
Calcon Carboxylic Acid

The reduction of several o,o'-dihydroxyazo-compounds is studied by means of pulse polarographic techniques (DPP, NPP and RPP). The compounds studied are the following: 2-(2'-hydroxyphenylazo)-phenol (o,o'-dihydroxyazobenzene), 1-(2'-hydroxy-1'-naphthylazo)-2-naphthol-4-sulphonic acid (calcon or Eriochrome Blue Black R), 1-(2'-hydroxy-4'-sulpho-1'-naphthylazo)-2-hydroxy-3-naphthoic acid (calcon carboxylic acid), and 1-(1'-hydroxy-2'-naphthylazo)-6-nitro-2-naphthol-4-sulphonic acid (Eriochrome Black T). Correlations between Ip and Epand experimental variables (pH, T, conc.) and instrumental parameters (dropping time, t, and pulse magnitude, ΔE) are established. Reaction mechanisms formerly proposed are discussed on the basis of the new obtained results, and the ranges are defined where adsorption and/or acid-base catalysis are operative.

scholarly journals A new antitumor antibiotic, dioxolamycin.

1984 ◽  
Vol 37 (6) ◽  
pp. 673-674 ◽  
Author(s):  
BAOQUAN ZHU ◽  
MOTO MORIOKA ◽  
HIKARU NAKAMURA ◽  
HIROSHI NAGANAWA ◽  
YASUHIKO MURAOKA ◽  
...  
Keyword(s):  
Antitumor Antibiotic

The modification of antitumor antibiotic daunomicin by selenium nanoparticles and polyvinylpyrrolidone

2020 ◽  
Author(s):  
O. A. Pisarev ◽  
A. V. Plyushchenko ◽  
L. N. Borovikova ◽  
I. V. Yakovlev
Keyword(s):  
Selenium Nanoparticles ◽  
Antitumor Antibiotic

scholarly journals Polyphosphate Reverses the Toxicity of the Quasi-Enzyme Bleomycin on Alveolar Endothelial Lung Cells In Vitro

Cancers ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 750
Author(s):  
Werner E. G. Müller ◽  
Meik Neufurth ◽  
Shunfeng Wang ◽  
Heinz C. Schröder ◽  
Xiaohong Wang
Keyword(s):  
Dna Damage ◽  
Human Lung ◽  
Dna Integrity ◽  
Lung Cells ◽  
Antitumor Antibiotic ◽  
Cell Toxicity ◽  
Inorganic Polyphosphate ◽  
Human Lung Cells ◽  
Anti Cancer

The anti-cancer antitumor antibiotic bleomycin(s) (BLM) induces athyminic sites in DNA after its activation, a process that results in strand splitting. Here, using A549 human lung cells or BEAS-2B cells lunc cells, we show that the cell toxicity of BLM can be suppressed by addition of inorganic polyphosphate (polyP), a physiological polymer that accumulates and is released from platelets. BLM at a concentration of 20 µg ml−1 causes a decrease in cell viability (by ~70%), accompanied by an increased DNA damage and chromatin expansion (by amazingly 6-fold). Importantly, the BLM-caused effects on cell growth and DNA integrity are substantially suppressed by polyP. In parallel, the enlargement of the nuclei/chromatin in BLM-treated cells (diameter, 20–25 µm) is normalized to ~12 µm after co-incubation of the cells with BLM and polyP. A sequential application of the drugs (BLM for 3 days, followed by an exposure to polyP) does not cause this normalization. During co-incubation of BLM with polyP the gene for the BLM hydrolase is upregulated. It is concluded that by upregulating this enzyme polyP prevents the toxic side effects of BLM. These data might also contribute to an application of BLM in COVID-19 patients, since polyP inhibits binding of SARS-CoV-2 to cellular ACE2.

Sign in / Sign up

Export Citation Format

Share Document