- The Functional Role of Extracellular Matrix

2014 ◽  
pp. 40-75
Keyword(s):  
Extracellular Matrix ◽  
Functional Role

Review article: the signalling and functional role of the extracellular matrix in the development of liver fibrosis

2020 ◽  
Vol 52 (1) ◽  
pp. 85-97 ◽  
Author(s):  
Ida Falk Villesen ◽  
Samuel Joseph Daniels ◽  
Diana Julie Leeming ◽  
Morten Asser Karsdal ◽  
Mette Juul Nielsen
Keyword(s):  
Extracellular Matrix ◽  
Liver Fibrosis ◽  
Functional Role ◽  
Review Article

Extracellular matrix modulates insulin production during differentiation of AR42J cells: Functional role of Pax6 transcription factor

2011 ◽  
Vol 112 (1) ◽  
pp. 318-329 ◽  
Author(s):  
Kohei Hamamoto ◽  
Satoko Yamada ◽  
Akemi Hara ◽  
Tsutomu Kodera ◽  
Masaharu Seno ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Transcription Factor ◽  
Functional Role ◽  
Insulin Production ◽  
Ar42j Cells

scholarly journals Functional role of glycosaminoglycans in decellularized lung extracellular matrix

2020 ◽  
Vol 102 ◽  
pp. 231-246 ◽  
Author(s):  
Franziska E. Uhl ◽  
Fuming Zhang ◽  
Robert A. Pouliot ◽  
Juan J. Uriarte ◽  
Sara Rolandsson Enes ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Functional Role

scholarly journals Functional role of laminin carbohydrate.

1984 ◽  
Vol 4 (1) ◽  
pp. 1-7 ◽  
Author(s):  
C C Howe
Keyword(s):  
Extracellular Matrix ◽  
Functional Role ◽  
Culture Medium ◽  
Proteolytic Degradation ◽  
Extracellular Matrix Component ◽  
Matrix Component ◽  
Disulfide Bonding ◽  
Cell Lysate ◽  
The Stability

Previous work showed that tunicamycin suppresses glycosylation of laminin. In the present work, the role of glycosylation in the secretion of laminin and in the disulfide bonding of laminin subunits was studied, using tunicamycin to inhibit glycosylation. Tunicamycin inhibited extensively the secretion of laminin into culture medium and extracellular matrix even though the treated cells contained higher concentrations of laminin than the control cells. The laminin subunits synthesized in the presence of tunicamycin were disulfide bonded. Thus, suppression of glycosylation did not adversely affect disulfide bonding of the subunits, but did decrease the secretion of laminin. Glycosidases were also used to remove the carbohydrate of laminin to study the role of carbohydrate in the stability of laminin and in its interaction with another extracellular matrix component, heparin. The glycosidases removed about 73% of [3H]glucosamine. Both glycosidase-treated and untreated laminin were stable when incubated with cell lysate or culture medium. The glycosidase-treated laminin bound as efficiently as the untreated laminin to heparin. These results suggest that the presence of a carbohydrate moiety, at least at the level found in untreated laminin, is not essential in binding to heparin or in protecting laminin from proteolytic degradation in the cell or culture medium.

scholarly journals The Functional Role of Extracellular Matrix Proteins in Cancer

Cancers ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 238
Author(s):  
Nadezhda V. Popova ◽  
Manfred Jücker
Keyword(s):  
Extracellular Matrix ◽  
Tumor Microenvironment ◽  
Cancer Progression ◽  
Functional Role ◽  
Signaling Cascades ◽  
Surface Receptors ◽  
Current State ◽  
Composition And Structure ◽  
Major Structural Component

The extracellular matrix (ECM) is highly dynamic as it is constantly deposited, remodeled and degraded to maintain tissue homeostasis. ECM is a major structural component of the tumor microenvironment, and cancer development and progression require its extensive reorganization. Cancerized ECM is biochemically different in its composition and is stiffer compared to normal ECM. The abnormal ECM affects cancer progression by directly promoting cell proliferation, survival, migration and differentiation. The restructured extracellular matrix and its degradation fragments (matrikines) also modulate the signaling cascades mediated by the interaction with cell-surface receptors, deregulate the stromal cell behavior and lead to emergence of an oncogenic microenvironment. Here, we summarize the current state of understanding how the composition and structure of ECM changes during cancer progression. We also describe the functional role of key proteins, especially tenascin C and fibronectin, and signaling molecules involved in the formation of the tumor microenvironment, as well as the signaling pathways that they activate in cancer cells.

Functional role of laminin carbohydrate

1984 ◽  
Vol 4 (1) ◽  
pp. 1-7
Author(s):  
C C Howe
Keyword(s):  
Extracellular Matrix ◽  
Functional Role ◽  
Culture Medium ◽  
Proteolytic Degradation ◽  
Extracellular Matrix Component ◽  
Matrix Component ◽  
Disulfide Bonding ◽  
Cell Lysate ◽  
The Stability

Previous work showed that tunicamycin suppresses glycosylation of laminin. In the present work, the role of glycosylation in the secretion of laminin and in the disulfide bonding of laminin subunits was studied, using tunicamycin to inhibit glycosylation. Tunicamycin inhibited extensively the secretion of laminin into culture medium and extracellular matrix even though the treated cells contained higher concentrations of laminin than the control cells. The laminin subunits synthesized in the presence of tunicamycin were disulfide bonded. Thus, suppression of glycosylation did not adversely affect disulfide bonding of the subunits, but did decrease the secretion of laminin. Glycosidases were also used to remove the carbohydrate of laminin to study the role of carbohydrate in the stability of laminin and in its interaction with another extracellular matrix component, heparin. The glycosidases removed about 73% of [3H]glucosamine. Both glycosidase-treated and untreated laminin were stable when incubated with cell lysate or culture medium. The glycosidase-treated laminin bound as efficiently as the untreated laminin to heparin. These results suggest that the presence of a carbohydrate moiety, at least at the level found in untreated laminin, is not essential in binding to heparin or in protecting laminin from proteolytic degradation in the cell or culture medium.

Extracellular matrix: the gatekeeper of tumor angiogenesis

2019 ◽  
Vol 47 (5) ◽  
pp. 1543-1555 ◽  
Author(s):  
Maurizio Mongiat ◽  
Simone Buraschi ◽  
Eva Andreuzzi ◽  
Thomas Neill ◽  
Renato V. Iozzo
Keyword(s):  
Extracellular Matrix ◽  
Tumor Angiogenesis ◽  
Signaling Cascades ◽  
Cancer Growth ◽  
Cell Behavior ◽  
Metastatic Progression ◽  
Surface Receptors ◽  
The Matrix ◽  
Multiple Signaling

Abstract The extracellular matrix is a network of secreted macromolecules that provides a harmonious meshwork for the growth and homeostatic development of organisms. It conveys multiple signaling cascades affecting specific surface receptors that impact cell behavior. During cancer growth, this bioactive meshwork is remodeled and enriched in newly formed blood vessels, which provide nutrients and oxygen to the growing tumor cells. Remodeling of the tumor microenvironment leads to the formation of bioactive fragments that may have a distinct function from their parent molecules, and the balance among these factors directly influence cell viability and metastatic progression. Indeed, the matrix acts as a gatekeeper by regulating the access of cancer cells to nutrients. Here, we will critically evaluate the role of selected matrix constituents in regulating tumor angiogenesis and provide up-to-date information concerning their primary mechanisms of action.

Expression and functional role of c-Kit and erbB2 in human hepatoblastoma.

2009 ◽  
Vol 221 (03) ◽  
Author(s):  
B Steiger ◽  
I Leuschner ◽  
D Denkhaus ◽  
D von Schweinitz ◽  
T Pietsch
Keyword(s):  
Functional Role
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