scholarly journals The C-terminal region of NELL1 mediates osteoblastic cell adhesion through integrin α3β1

FEBS Letters ◽  
2012 ◽  
Vol 586 (16) ◽  
pp. 2500-2506 ◽  
Author(s):  
Ai Hasebe ◽  
Yoko Nakamura ◽  
Hiroki Tashima ◽  
Kaneyoshi Takahashi ◽  
Masumi Iijima ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Terminal Region ◽  
Osteoblastic Cell ◽  
Integrin Α3β1

Role of vasostatin-1 C-terminal region in fibroblast cell adhesion

2010 ◽  
Vol 67 (12) ◽  
pp. 2107-2118 ◽  
Author(s):  
Eleonora Dondossola ◽  
Anna Gasparri ◽  
Angela Bachi ◽  
Renato Longhi ◽  
Marie-Hélène Metz-Boutigue ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Fibroblast Cell ◽  
Terminal Region

Wettability and osteoblastic cell adhesion on ultrapolished commercially pure titanium surfaces: the role of the oxidation and pollution states

2014 ◽  
Vol 28 (12) ◽  
pp. 1207-1218 ◽  
Author(s):  
Miguel A. Fernández-Rodríguez ◽  
Alda Y. Sánchez-Treviño ◽  
Elvira De Luna-Bertos ◽  
Javier Ramos-Torrecillas ◽  
Olga García-Martínez ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Pure Titanium ◽  
Osteoblastic Cell ◽  
Commercially Pure Titanium ◽  
Commercially Pure ◽  
Titanium Surfaces

scholarly journals The Effects of Syndecan on Osteoblastic Cell Adhesion Onto Nano-Zirconia Surface

2020 ◽  
Vol Volume 15 ◽  
pp. 5061-5072
Author(s):  
Lu Sun ◽  
Guang Hong ◽  
Hiroyuki Matsui ◽  
Yun-Jia Song ◽  
Keiichi Sasaki
Keyword(s):  
Cell Adhesion ◽  
Osteoblastic Cell

Controlling pre-osteoblastic cell adhesion and spreading on glycopolymer brushes of variable film thickness

2018 ◽  
Vol 29 (7) ◽  
Author(s):  
Chrystalleni Hadjicharalambous ◽  
Chara Flouraki ◽  
Ravin Narain ◽  
Maria Chatzinikolaidou ◽  
Maria Vamvakaki
Keyword(s):  
Cell Adhesion ◽  
Film Thickness ◽  
Osteoblastic Cell

scholarly journals A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin

1999 ◽  
Vol 341 (1) ◽  
pp. 11-14 ◽  
Author(s):  
Valentina DUBLJEVIC ◽  
Adnan SALI ◽  
James W. GODING
Keyword(s):  
Cell Adhesion ◽  
Transferrin Receptor ◽  
Iron Uptake ◽  
Terminal Region ◽  
Rgd Sequence

The transferrin receptor contains a highly conserved Arg-Gly-Asp (RGD) sequence in the C-terminal region where transferrin is thought to bind. RGD sequences are commonly involved in cell adhesion. This sequence is crucial for transferrin binding, suggesting possible evolutionary links between molecules mediating iron uptake and cell adhesion.

scholarly journals The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion.

1993 ◽  
Vol 12 (8) ◽  
pp. 3073-3081 ◽  
Author(s):  
J. McGlade ◽  
B. Brunkhorst ◽  
D. Anderson ◽  
G. Mbamalu ◽  
J. Settleman ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Terminal Region ◽  
Cytoskeletal Structure

scholarly journals Mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin α5 in the glomerular basement membrane

2003 ◽  
Vol 161 (1) ◽  
pp. 187-196 ◽  
Author(s):  
Yamato Kikkawa ◽  
Ismo Virtanen ◽  
Jeffrey H. Miner
Keyword(s):  
Cell Adhesion ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Mesangial Cell ◽  
Mesangial Cells ◽  
Basement Membranes ◽  
Domain Specific ◽  
Integrin Α3β1 ◽  
Glomerular Capillaries

In developing glomeruli, laminin α5 replaces laminin α1 in the glomerular basement membrane (GBM) at the capillary loop stage, a transition required for glomerulogenesis. To investigate domain-specific functions of laminin α5 during glomerulogenesis, we produced transgenic mice that express a chimeric laminin composed of laminin α5 domains VI through I fused to the human laminin α1 globular (G) domain, designated Mr51. Transgene-derived protein accumulated in many basement membranes, including the developing GBM. When bred onto the Lama5 −/− background, Mr51 supported GBM formation, preventing the breakdown that normally occurs in Lama5 −/− glomeruli. In addition, podocytes exhibited their typical arrangement in a single cell layer epithelium adjacent to the GBM, but convolution of glomerular capillaries did not occur. Instead, capillaries were distended and exhibited a ballooned appearance, a phenotype similar to that observed in the total absence of mesangial cells. However, here the phenotype could be attributed to the lack of mesangial cell adhesion to the GBM, suggesting that the G domain of laminin α5 is essential for this adhesion. Analysis of an additional chimeric transgene allowed us to narrow the region of the α5 G domain essential for mesangial cell adhesion to α5LG3-5. Finally, in vitro studies showed that integrin α3β1 and the Lutheran glycoprotein mediate adhesion of mesangial cells to laminin α5. Our results elucidate a mechanism whereby mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin α5 in the GBM.

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