Cytotrienin A, a Novel Apoptosis Inducer in Human Leukemia HL-60 Cells.

Kakeya, Hideaki; Zhang, Huiping; Kobinata, Kimie; Onose, Rie; Onozawa, Chizuko; Kudo, Takuji; Osada, Hiroyuki

doi:10.7164/antibiotics.50.370

Cited by 51 publications

(24 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In our previous studies (11,12), we identified a novel anticancer drug, named cytotrienin A, which is an ansamycin with a unique 1-aminocyclopropane-1-carboxylic acid in the molecule. Moreover, cytotrienin A induces apoptosis in human leukemia HL-60 cells via activation of p36 MBP kinase, an active proteolytic fragment of MST/Krs proteins (13).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Activation of MST/Krs and c-Jun N-terminal Kinases by Different Signaling Pathways during Cytotrienin A-induced Apoptosis

Watabe

Kakeya

Onose

et al. 2000

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

“…1), a novel ansamycin antitumor agent, was isolated from Streptomyces sp. as an apoptosis inducer (11,12). Recently, we have found that JNK 1 and a 36-kDa kinase (termed p36 MBP kinase) are activated during the cytotrienin A-induced apoptosis in human promyelocytic leukemia HL-60 cells (13).…”

mentioning

confidence: 99%

Activation of MST/Krs and c-Jun N-terminal Kinases by Different Signaling Pathways during Cytotrienin A-induced Apoptosis

Watabe

Kakeya

Onose

et al. 2000

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

“…It is a building block of BZR-Cotoxin II [10], a depsipeptide metabolite of a plant pathogen, antibiotic CBS 154-94A [11], a depsipeptide protein farnesyl transferase inhibitor, and of cytotrienins [12], ansamycin type antibiotics.…”

Section: Structure Of Neoefrapeptin Amentioning

confidence: 99%

Structure Determination of Neoefrapeptins A to N: Peptides with Insecticidal Activity Produced by the Fungus Geotrichum candidum

et al. 2006

View full text Add to dashboard Cite

The structures of neoefrapeptins A to N, peptides with insecticidal activity, were elucidated. They showed a close similarity to efrapeptin. However, all neoefrapeptins contained the very rare amino acid 1-aminocyclopropane-carboxylic acid and some of them also contained (2S,3S)-3-methylproline. The neoefrapeptins are the first case, in which these amino acids are found as building blocks for linear peptides. They were identified by comparison of the silylated hydrolyzate to reference material by GC/MS (EI-mode). The sequence was elucidated using mass spectrometry (ESIϩ mode). Full scan spectra showed two fragments in high yield, even under mild ionization conditions. MS/MS spectra of these two fragments yielded fragment rich spectra from which the sequence of the compounds was determined almost completely. The proteolytic cleavage with the proteinase papain yielded products that allowed to prove the rest of the sequence and the identity of the C-terminus to efrapeptin. The proteolytic cleavage products allowed furthermore to determine the position of the isobaric amino acids, pipecolic acid and 3-methylproline in neoefrapeptin F, as well as the location of R-isovaline and S-isovaline. Papain digestion was such established as a tool for structure elucidation of peptides rich in a ,a -dialkylated amino acids. CD spectra suggested a 3 10 helical structure for neoefrapeptins A and F.

show abstract

“…AC 654 as an inhibitor of ER stressinduced XBP1 activation. Although many triene-ansamycin antibiotics, such as trienomycins [13], mycotrienins [14], cytotrienins [15], thiazinotrienomycins [16], TMC-135s [17], and UCF116s [18] have been isolated from the cultured broth of Actinomycete strains, they do not have a SCH 3 group in their structures; therefore, trierixin is a new member of the triene-ansamycin family.…”

Section: Discussionmentioning

confidence: 99%

Trierixin, a Novel Inhibitor of ER Stress-induced XBP1 Activation from Streptomyces sp.

et al. 2007

View full text Add to dashboard Cite

In the course of screening for an inhibitor of ER stress-induced XBP1 activation, we isolated a new member of the triene-ansamycin group compound, trierixin, from a culture broth of Streptomyces sp. AC 654. Trierixin was purified by column chromatography on silica gel and by HPLC. The molecular formula of trierixin is C 37 H 52 N 2 O 8 S. Trierixin inhibited thapsigargin-induced XBP1-luciferase activation in HeLa/XBP1-luc cells and endogenous XBP1 splicing in HeLa cells with an IC 50 of 14 ng/ml and 19 ng/ml, respectively. Moreover, in the process of isolating trierixin, we isolated structurally related mycotrienin II and trienomycin A as inhibitors of ER stress-induced XBP1 activation from a culture broth of a trierixin-producing strain. This study provides the first observation that triene-ansamycins have a novel inhibitory effect against XBP1 activation.

show abstract

Cytotrienin A, a Novel Apoptosis Inducer in Human Leukemia HL-60 Cells.

Cited by 51 publications

References 7 publications

Activation of MST/Krs and c-Jun N-terminal Kinases by Different Signaling Pathways during Cytotrienin A-induced Apoptosis

Activation of MST/Krs and c-Jun N-terminal Kinases by Different Signaling Pathways during Cytotrienin A-induced Apoptosis

Structure Determination of Neoefrapeptins A to N: Peptides with Insecticidal Activity Produced by the Fungus Geotrichum candidum

Trierixin, a Novel Inhibitor of ER Stress-induced XBP1 Activation from Streptomyces sp.

Contact Info

Product

Resources

About