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  1. Article: The application of the

    Kikuchi, Kyoko / Sugiura, Mika / Nishizawa-Harada, Chizuko / Kimura, Tadashi

    Biotechnology reports (Amsterdam, Netherlands)

    2015  Volume 7, Page(s) 17–23

    Abstract: Kv2.1, the voltage-gated ion channel, is ubiquitously expressed in variety of tissues and dysfunction of this ion channel is responsible for multiple diseases. Electrophysiological properties of ion channels are so far characterized with eukaryotic cells ...

    Abstract Kv2.1, the voltage-gated ion channel, is ubiquitously expressed in variety of tissues and dysfunction of this ion channel is responsible for multiple diseases. Electrophysiological properties of ion channels are so far characterized with eukaryotic cells using the manual patch clamp which requires skilful operators and expensive equipments. In this research, we created a simple and sensitive drug screen method using bacterial giant spheroplasts and the automated patch clamp which does not require special skills. We expressed a eukaryotic voltage-gated ion channel Kv2.1 in
    Language English
    Publishing date 2015-05-05
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2801018-8
    ISSN 2215-017X
    ISSN 2215-017X
    DOI 10.1016/j.btre.2015.04.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Development of an orally-administrable tumor vasculature-targeting therapeutic using annexin A1-binding D-peptides.

    Nonaka, Motohiro / Mabashi-Asazuma, Hideaki / Jarvis, Donald L / Yamasaki, Kazuhiko / Akama, Tomoya O / Nagaoka, Masato / Sasai, Toshio / Kimura-Takagi, Itsuko / Suwa, Yoichi / Yaegashi, Takashi / Huang, Chun-Teng / Nishizawa-Harada, Chizuko / Fukuda, Michiko N

    PloS one

    2021  Volume 16, Issue 1, Page(s) e0241157

    Abstract: We previously reported that IF7 peptide, which binds to the annexin A1 (ANXA1) N-terminus, functions as a tumor vasculature-targeted drug delivery vehicle after intravenous injection. To enhance IF7 stability in vivo, we undertook mirror-image peptide ... ...

    Abstract We previously reported that IF7 peptide, which binds to the annexin A1 (ANXA1) N-terminus, functions as a tumor vasculature-targeted drug delivery vehicle after intravenous injection. To enhance IF7 stability in vivo, we undertook mirror-image peptide phage display using a synthetic D-peptide representing the ANXA1 N-terminus as target. We then identified peptide sequences, synthesized them as D-amino acids, and designated the resulting peptide dTIT7, which we showed bound to the ANXA1 N-terminus. Whole body imaging of mouse brain tumor models injected with near infrared fluorescent IRDye-conjugated dTIT7 showed fluorescent signals in brain and kidney. Furthermore, orally-administered dTIT7/geldanamycin (GA) conjugates suppressed brain tumor growth. Ours is a proof-of-concept experiment showing that ANXA1-binding D-peptide can be developed as an orally-administrable tumor vasculature-targeted therapeutic.
    MeSH term(s) Administration, Oral ; Animals ; Annexin A1/antagonists & inhibitors ; Annexin A1/metabolism ; Brain Neoplasms/blood supply ; Brain Neoplasms/drug therapy ; Brain Neoplasms/metabolism ; Brain Neoplasms/pathology ; Drug Delivery Systems ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Neoplasm Proteins/antagonists & inhibitors ; Neoplasm Proteins/metabolism ; Neovascularization, Pathologic/drug therapy ; Neovascularization, Pathologic/metabolism ; Neovascularization, Pathologic/pathology ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/pharmacology ; Xenograft Model Antitumor Assays
    Chemical Substances ANXA1 protein, human ; Annexin A1 ; Neoplasm Proteins ; Peptides
    Language English
    Publishing date 2021-01-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0241157
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Overcoming the blood-brain barrier by Annexin A1-binding peptide to target brain tumours.

    Nonaka, Motohiro / Suzuki-Anekoji, Misa / Nakayama, Jun / Mabashi-Asazuma, Hideaki / Jarvis, Donald L / Yeh, Jiunn-Chern / Yamasaki, Kazuhiko / Akama, Tomoya O / Huang, Chun-Teng / Campos, Alexandre Rosa / Nagaoka, Masato / Sasai, Toshio / Kimura-Takagi, Itsuko / Suwa, Yoichi / Yaegashi, Takashi / Shibata, Toshiaki K / Sugihara, Kazuhiro / Nishizawa-Harada, Chizuko / Fukuda, Minoru /
    Fukuda, Michiko N

    British journal of cancer

    2020  Volume 123, Issue 11, Page(s) 1633–1643

    Abstract: Background: Annexin A1 is expressed specifically on the tumour vasculature surface. Intravenously injected IF7 targets tumour vasculature via annexin A1. We tested the hypothesis that IF7 overcomes the blood-brain barrier and that the intravenously ... ...

    Abstract Background: Annexin A1 is expressed specifically on the tumour vasculature surface. Intravenously injected IF7 targets tumour vasculature via annexin A1. We tested the hypothesis that IF7 overcomes the blood-brain barrier and that the intravenously injected IF7C(RR)-SN38 eradicates brain tumours in the mouse.
    Methods: (1) A dual-tumour model was generated by inoculating luciferase-expressing melanoma B16 cell line, B16-Luc, into the brain and under the skin of syngeneic C57BL/6 mice. IF7C(RR)-SN38 was injected intravenously daily at 7.0 μmoles/kg and growth of tumours was assessed by chemiluminescence using an IVIS imager. A similar dual-tumour model was generated with the C6-Luc line in immunocompromised SCID mice. (2) IF7C(RR)-SN38 formulated with 10% Solutol HS15 was injected intravenously daily at 2.5 μmoles/kg into two brain tumour mouse models: B16-Luc cells in C57BL/6 mice, and C6-Luc cells in nude mice.
    Results: (1) Daily IF7C(RR)-SN38 injection suppressed tumour growth regardless of cell lines or mouse strains. (2) Daily injection of Solutol-formulated IF7C(RR)-SN38 led into complete disappearance of B16-Luc brain tumour in C57BL/6 mice, whereas this did not occur in C6-Luc in nude mice.
    Conclusions: IF7C(RR)-SN38 crosses the blood-brain barrier and suppresses growth of brain tumours in mouse models. Solutol HS15-formulated IF7C(RR)-SN38 may have promoted an antitumour immune response.
    MeSH term(s) Animals ; Annexin A1/metabolism ; Antineoplastic Agents/pharmacology ; Blood-Brain Barrier/metabolism ; Brain Neoplasms ; Drug Carriers/pharmacology ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, SCID ; Peptides ; Rats
    Chemical Substances Annexin A1 ; Antineoplastic Agents ; Drug Carriers ; Peptides
    Language English
    Publishing date 2020-09-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80075-2
    ISSN 1532-1827 ; 0007-0920
    ISSN (online) 1532-1827
    ISSN 0007-0920
    DOI 10.1038/s41416-020-01066-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  4. Article: Enzymatic assembly of the bis-indole core of rebeccamycin.

    Nishizawa, Tomoyasu / Grüschow, Sabine / Jayamaha, Don-Hema E / Nishizawa-Harada, Chizuko / Sherman, David H

    Journal of the American Chemical Society

    2006  Volume 128, Issue 3, Page(s) 724–725

    Abstract: Rebeccamycin is a member of the family of indolocarbazole antibiotics with broad spectrum antitumor activity. The indolocarbazole framework is derived from two molecules of tryptophan, but very little is known about the enzymes involved in rebeccamycin ... ...

    Abstract Rebeccamycin is a member of the family of indolocarbazole antibiotics with broad spectrum antitumor activity. The indolocarbazole framework is derived from two molecules of tryptophan, but very little is known about the enzymes involved in rebeccamycin biosynthesis. Here, we show that RebD is responsible for all catalytic steps forming the central pyrrole ring of chlorochromopyrrolic acid from two molecules of chloroindolepyruvic acid. This transformation does not require any additional cofactors and constitutes the first step of bis-indole formation in the biosynthesis of rebeccamycin.
    MeSH term(s) Actinomycetales/enzymology ; Actinomycetales/genetics ; Actinomycetales/metabolism ; Bacterial Proteins/metabolism ; Carbazoles/metabolism ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Hemeproteins/metabolism ; Indoles/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
    Chemical Substances Bacterial Proteins ; Carbazoles ; Hemeproteins ; Indoles ; Recombinant Proteins ; heme protein, bacteria ; rebeccamycin (93908-02-2)
    Language English
    Publishing date 2006-01-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/ja056749x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

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