Inhibition of matrix metalloproteinase-9 (MMP-9) activity by cleistanthin A, a diphyllin glycoside from Cleistanthus collinus

Chung Ren Jan; Jue Lone Wang; Muh Chiou Lin; Kam Chung Lee; Kang Ju Chou; Hung Ting Chiang

doi:10.1002/1098-2299(200006)50:2<193::AID-DDR9>3.0.CO;2-F

Inhibition of matrix metalloproteinase-9 (MMP-9) activity by cleistanthin A, a diphyllin glycoside from Cleistanthus collinus

Chung Ren Jan, Jue Lone Wang, Muh Chiou Lin, Kam Chung Lee, Kang Ju Chou, Hung Ting Chiang

Research output: Contribution to journal › Journal Article › peer-review

7 Scopus citations

Abstract

Matrix metalloproteinases (MMPs) are responsible for the remodeling of the extracellular matrix throughout the body. Inhibitors of these enzymes have been suggested as potential therapeutic agents for use in treatment of cancer. Our observations showed that cleistanthin A, a diphyllin glycoside from the leaves of the plant Cleistanthus collinus inhibited MMP-9, a 92 kDa matrix metalloproteinase. Further evaluation of this compound might reveal many such novel properties that might help in the evolution of this compound as an anticancer drug. (C) 2000 Wiley-Liss, Inc.

Original language	English
Pages (from-to)	193-194
Number of pages	2
Journal	Drug Development Research
Volume	50
Issue number	2
DOIs	https://doi.org/10.1002/1098-2299(200006)50:2<193::AID-DDR9>3.0.CO;2-F
State	Published - 2000
Externally published	Yes

Keywords

MMP-9
S-180 cell lines
Zymography

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/1098-2299(200006)50:2<193::AID-DDR9>3.0.CO;2-F

Cite this

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title = "Inhibition of matrix metalloproteinase-9 (MMP-9) activity by cleistanthin A, a diphyllin glycoside from Cleistanthus collinus",

abstract = "Matrix metalloproteinases (MMPs) are responsible for the remodeling of the extracellular matrix throughout the body. Inhibitors of these enzymes have been suggested as potential therapeutic agents for use in treatment of cancer. Our observations showed that cleistanthin A, a diphyllin glycoside from the leaves of the plant Cleistanthus collinus inhibited MMP-9, a 92 kDa matrix metalloproteinase. Further evaluation of this compound might reveal many such novel properties that might help in the evolution of this compound as an anticancer drug. (C) 2000 Wiley-Liss, Inc.",

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author = "Jan, {Chung Ren} and Wang, {Jue Lone} and Lin, {Muh Chiou} and Lee, {Kam Chung} and Chou, {Kang Ju} and Chiang, {Hung Ting}",

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doi = "10.1002/1098-2299(200006)50:2<193::AID-DDR9>3.0.CO;2-F",

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AU - Lin, Muh Chiou

AU - Lee, Kam Chung

AU - Chou, Kang Ju

AU - Chiang, Hung Ting

PY - 2000

Y1 - 2000

N2 - Matrix metalloproteinases (MMPs) are responsible for the remodeling of the extracellular matrix throughout the body. Inhibitors of these enzymes have been suggested as potential therapeutic agents for use in treatment of cancer. Our observations showed that cleistanthin A, a diphyllin glycoside from the leaves of the plant Cleistanthus collinus inhibited MMP-9, a 92 kDa matrix metalloproteinase. Further evaluation of this compound might reveal many such novel properties that might help in the evolution of this compound as an anticancer drug. (C) 2000 Wiley-Liss, Inc.

AB - Matrix metalloproteinases (MMPs) are responsible for the remodeling of the extracellular matrix throughout the body. Inhibitors of these enzymes have been suggested as potential therapeutic agents for use in treatment of cancer. Our observations showed that cleistanthin A, a diphyllin glycoside from the leaves of the plant Cleistanthus collinus inhibited MMP-9, a 92 kDa matrix metalloproteinase. Further evaluation of this compound might reveal many such novel properties that might help in the evolution of this compound as an anticancer drug. (C) 2000 Wiley-Liss, Inc.

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KW - S-180 cell lines

KW - Zymography

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M3 - 文章

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Inhibition of matrix metalloproteinase-9 (MMP-9) activity by cleistanthin A, a diphyllin glycoside from Cleistanthus collinus

Abstract

Keywords

UN SDGs

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