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 ◽  
...  
2020 ◽  
Vol 52 (1) ◽  
pp. 85-97 ◽  
Author(s):  
Ida Falk Villesen ◽  
Samuel Joseph Daniels ◽  
Diana Julie Leeming ◽  
Morten Asser Karsdal ◽  
Mette Juul Nielsen

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

2012 ◽  
Vol 227 (6) ◽  
pp. 2470-2479 ◽  
Author(s):  
Tao Zhang ◽  
Nicolle A. Saunee ◽  
Mary B. Breslin ◽  
Kejing Song ◽  
Michael S. Lan

1984 ◽  
Vol 4 (1) ◽  
pp. 1-7 ◽  
Author(s):  
C C Howe

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.


2007 ◽  
Vol 97 (8) ◽  
pp. 1106-1115 ◽  
Author(s):  
H Kayed ◽  
X Jiang ◽  
S Keleg ◽  
R Jesnowski ◽  
T Giese ◽  
...  

2004 ◽  
Vol 34 (12) ◽  
pp. 3401-3412 ◽  
Author(s):  
Michael Hausding ◽  
I-Cheng Ho ◽  
Hans?A. Lehr ◽  
B. Weigmann ◽  
Christine Lux ◽  
...  

Cancers ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 238
Author(s):  
Nadezhda V. Popova ◽  
Manfred Jücker

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.


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