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Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells

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Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells. / Gorzelanny, Christian; Pöppelmann, Birgit; Strozyk, Elwira; Moerschbacher, Bruno M; Schneider, Stefan W.

in: BIOMACROMOLECULES, Jahrgang 8, Nr. 10, 10.2007, S. 3035-40.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Gorzelanny, C, Pöppelmann, B, Strozyk, E, Moerschbacher, BM & Schneider, SW 2007, 'Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells', BIOMACROMOLECULES, Jg. 8, Nr. 10, S. 3035-40. https://doi.org/10.1021/bm0703214

APA

Gorzelanny, C., Pöppelmann, B., Strozyk, E., Moerschbacher, B. M., & Schneider, S. W. (2007). Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells. BIOMACROMOLECULES, 8(10), 3035-40. https://doi.org/10.1021/bm0703214

Vancouver

Gorzelanny C, Pöppelmann B, Strozyk E, Moerschbacher BM, Schneider SW. Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells. BIOMACROMOLECULES. 2007 Okt;8(10):3035-40. https://doi.org/10.1021/bm0703214

Bibtex

@article{d6e36bba5c1c448181eef9c824a48929,
title = "Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells",
abstract = "The crucial event in metastasis is tumor invasion which in the case of melanoma cells is dependent on matrix metalloprotease 2 (MMP2). Chitosan (MW ca. 5 x 10(5) g mol(-1), degree of acetylation ca. 30%) attenuated the invasive activity of melanoma cells in a cell-based invasion assay and reduced MMP2 activity in the supernatant of melanoma cells. While the expression level of MMP2 was not affected, the amount of MMP2 in the cell supernatant was reduced, indicating a posttranscriptional effect of chitosan on MMP2. Atomic force microscopy revealed a direct molecular interaction between MMP2 and chitosan forming a complex with a diameter of 349.0 +/- 69.06 nm and a height of 26.5 +/- 11.50 nm. Affinity chromatography revealed a high binding-specificity of MMP2 to chitosan, and a colorimetric MMP2 activity assay suggests a noncompetitive inhibition of MMP2 by chitosan. The possible use of chitosan as a new type of MMP2 inhibitor is discussed.",
keywords = "Animals, Cell Line, Tumor, Cell Movement, Cell Proliferation, Chitosan, Chromatography, Affinity, Dogs, Gelatin, Humans, Matrix Metalloproteinase 2, Melanoma, Microscopy, Atomic Force, Models, Biological, Neoplasm Invasiveness, Skin Neoplasms, Journal Article, Research Support, Non-U.S. Gov't",
author = "Christian Gorzelanny and Birgit P{\"o}ppelmann and Elwira Strozyk and Moerschbacher, {Bruno M} and Schneider, {Stefan W}",
year = "2007",
month = oct,
doi = "10.1021/bm0703214",
language = "English",
volume = "8",
pages = "3035--40",
journal = "BIOMACROMOLECULES",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "10",

}

RIS

TY - JOUR

T1 - Specific interaction between chitosan and matrix metalloprotease 2 decreases the invasive activity of human melanoma cells

AU - Gorzelanny, Christian

AU - Pöppelmann, Birgit

AU - Strozyk, Elwira

AU - Moerschbacher, Bruno M

AU - Schneider, Stefan W

PY - 2007/10

Y1 - 2007/10

N2 - The crucial event in metastasis is tumor invasion which in the case of melanoma cells is dependent on matrix metalloprotease 2 (MMP2). Chitosan (MW ca. 5 x 10(5) g mol(-1), degree of acetylation ca. 30%) attenuated the invasive activity of melanoma cells in a cell-based invasion assay and reduced MMP2 activity in the supernatant of melanoma cells. While the expression level of MMP2 was not affected, the amount of MMP2 in the cell supernatant was reduced, indicating a posttranscriptional effect of chitosan on MMP2. Atomic force microscopy revealed a direct molecular interaction between MMP2 and chitosan forming a complex with a diameter of 349.0 +/- 69.06 nm and a height of 26.5 +/- 11.50 nm. Affinity chromatography revealed a high binding-specificity of MMP2 to chitosan, and a colorimetric MMP2 activity assay suggests a noncompetitive inhibition of MMP2 by chitosan. The possible use of chitosan as a new type of MMP2 inhibitor is discussed.

AB - The crucial event in metastasis is tumor invasion which in the case of melanoma cells is dependent on matrix metalloprotease 2 (MMP2). Chitosan (MW ca. 5 x 10(5) g mol(-1), degree of acetylation ca. 30%) attenuated the invasive activity of melanoma cells in a cell-based invasion assay and reduced MMP2 activity in the supernatant of melanoma cells. While the expression level of MMP2 was not affected, the amount of MMP2 in the cell supernatant was reduced, indicating a posttranscriptional effect of chitosan on MMP2. Atomic force microscopy revealed a direct molecular interaction between MMP2 and chitosan forming a complex with a diameter of 349.0 +/- 69.06 nm and a height of 26.5 +/- 11.50 nm. Affinity chromatography revealed a high binding-specificity of MMP2 to chitosan, and a colorimetric MMP2 activity assay suggests a noncompetitive inhibition of MMP2 by chitosan. The possible use of chitosan as a new type of MMP2 inhibitor is discussed.

KW - Animals

KW - Cell Line, Tumor

KW - Cell Movement

KW - Cell Proliferation

KW - Chitosan

KW - Chromatography, Affinity

KW - Dogs

KW - Gelatin

KW - Humans

KW - Matrix Metalloproteinase 2

KW - Melanoma

KW - Microscopy, Atomic Force

KW - Models, Biological

KW - Neoplasm Invasiveness

KW - Skin Neoplasms

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1021/bm0703214

DO - 10.1021/bm0703214

M3 - SCORING: Journal article

C2 - 17845054

VL - 8

SP - 3035

EP - 3040

JO - BIOMACROMOLECULES

JF - BIOMACROMOLECULES

SN - 1525-7797

IS - 10

ER -