scholarly journals Novel cell surface adhesion receptors involved in interactions between stromal macrophages and haematopoietic cells

1988 ◽  
Vol 1988 (Supplement 9) ◽  
pp. 185-206 ◽  
Author(s):  
P. R. CROCKER ◽  
L. MORRIS ◽  
S. GORDON
Keyword(s):  
Cell Surface ◽  
Surface Adhesion ◽  
Adhesion Receptors ◽  
Haematopoietic Cells

Cell surface adhesion receptors

1994 ◽  
Vol 4 (6) ◽  
pp. 841-851 ◽  
Author(s):  
Gerhard Wagner ◽  
Daniel F. Wyss
Keyword(s):  
Cell Surface ◽  
Surface Adhesion ◽  
Adhesion Receptors

Mechanistic Features of Cell-Surface Adhesion Receptors

2003 ◽  
pp. 71-77
Author(s):  
Steven C. Almo ◽  
Anne R. Bresnick ◽  
Xuewu Zhang
Keyword(s):  
Cell Surface ◽  
Surface Adhesion ◽  
Adhesion Receptors

scholarly journals Integrin activation takes shape

2002 ◽  
Vol 158 (5) ◽  
pp. 833-839 ◽  
Author(s):  
R.C. Liddington ◽  
M.H. Ginsberg
Keyword(s):  
Cell Surface ◽  
Ligand Binding ◽  
Cytoplasmic Domain ◽  
Structural Basis ◽  
Surface Adhesion ◽  
Integrin Activation ◽  
Adhesion Receptors ◽  
Ligand Activation ◽  
And Function

Integrins are cell surface adhesion receptors that are essential for the development and function of multicellular animals. Here we summarize recent findings on the regulation of integrin affinity for ligand (activation), one mechanism by which cells modulate integrin function. The focus is on the structural basis of integrin activation, the role of the cytoplasmic domain in integrin affinity regulation, and potential mechanisms by which activation signals are propagated from integrin cytoplasmic domains to the extracellular ligand-binding domain.

Mechanistic Features of Cell-Surface Adhesion Receptors

2010 ◽  
pp. 63-69
Author(s):  
Steven C. Almo ◽  
Anne R. Bresnick ◽  
Xuewu Zhang
Keyword(s):  
Cell Surface ◽  
Surface Adhesion ◽  
Adhesion Receptors

Plasma and endothelial cell-surface adhesion molecules and cardiopulmonary bypass

2000 ◽  
Vol 9 (3) ◽  
pp. A185
Author(s):  
Michael P. Vallely ◽  
Paul G. Bannon ◽  
Clifford F. Hughes ◽  
Leonard Kritharides
Keyword(s):  
Cardiopulmonary Bypass ◽  
Endothelial Cell ◽  
Cell Surface ◽  
Adhesion Molecules ◽  
Surface Adhesion ◽  
Endothelial Cell Surface

scholarly journals Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction

1997 ◽  
Vol 322 (3) ◽  
pp. 859-865 ◽  
Author(s):  
Takami TOMIYAMA ◽  
Hideshi KANEKO ◽  
Ken-ichiro KATAOKA ◽  
Satoshi ASANO ◽  
Noriaki ENDO
Keyword(s):  
Cell Surface ◽  
Immunofluorescence Microscopy ◽  
Therapeutic Potential ◽  
Cell Interaction ◽  
Human Islet ◽  
Surface Adhesion ◽  
Islet Amyloid ◽  
Amyloid Peptides ◽  
Pheochromocytoma Pc12 ◽  
Peptide Fibrils

Rifampicin and its analogues,p-benzoquinone and hydroquinone, inhibited the toxicity of preformed aggregates of human islet amyloid polypeptide, amylin, to rat pheochromocytoma PC12 cells, when preincubated with the aggregated peptide before addition to cell cultures. Immunofluorescence microscopy showed that they prevented the adhesion of amylin aggregates to the cell surface, and this effect was induced probably by their binding to peptide fibrils during preincubation. Other quinone derivatives, i.e., p-methoxyphenol, AA-861 and idebenone, failed to inhibit the toxicity and cell-surface adhesion of amylin aggregates. Rifampicin analogues also inhibited the toxicity of pre-aggregated amyloid β1–42 peptides, suggesting a common toxic mechanism of different amyloid peptides and their therapeutic potential for several amyloidoses.

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