Expression of Collagen-Binding Integrin Receptors in the Mammalian Sclera and Their Regulation during the Development of Myopia

2006 ◽  
Vol 47 (11) ◽  
pp. 4674 ◽  
Author(s):  
Neville A. McBrien ◽  
Ravikanth Metlapally ◽  
Andrew I. Jobling ◽  
Alex Gentle
Keyword(s):  
Integrin Receptors ◽  
Collagen Binding

scholarly journals Endocytosis of Integrin-Binding Human Picornaviruses

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Pirjo Merilahti ◽  
Satu Koskinen ◽  
Outi Heikkilä ◽  
Eveliina Karelehto ◽  
Petri Susi
Keyword(s):  
Economic Importance ◽  
Integrin Receptors ◽  
Human Parechovirus ◽  
Collagen Binding ◽  
Cellular Receptors ◽  
Disease Symptoms ◽  
Receptor Endocytosis ◽  
Wide Range ◽  
Coxsackievirus A9 ◽  
Picornavirus Infection

Picornaviruses that infect humans form one of the largest virus groups with almost three hundred virus types. They include significant enteroviral pathogens such as rhino-, polio-, echo-, and coxsackieviruses and human parechoviruses that cause wide range of disease symptoms. Despite the economic importance of picornaviruses, there are no antivirals. More than ten cellular receptors are known to participate in picornavirus infection, but experimental evidence of their role in cellular infection has been shown for only about twenty picornavirus types. Three enterovirus types and one parechovirus have experimentally been shown to bind and use integrin receptors in cellular infection. These include coxsackievirus A9 (CV-A9), echovirus 9, and human parechovirus 1 that are among the most common and epidemic human picornaviruses and bind toαV-integrins via RGD motif that resides on virus capsid. In contrast, echovirus 1 (E-1) has no RGD and uses integrinα2β1 as cellular receptor. Endocytosis of CV-A9 has recently been shown to occur via a novel Arf6- and dynamin-dependent pathways, while, contrary to collagen binding, E-1 binds inactiveβ1 integrin and enters via macropinocytosis. In this paper, we review what is known about receptors and endocytosis of integrin-binding human picornaviruses.

Processing of human melanoma cells for correlative TEM, LVSEM, and LM

1991 ◽  
Vol 49 ◽  
pp. 106-107
Author(s):  
Marek Malecki ◽  
J. Victor Small ◽  
James Pawley
Keyword(s):  
Electron Microscopy ◽  
Low Voltage ◽  
Fluorescent Microscopy ◽  
Blood Stream ◽  
Surface Topology ◽  
Integrin Receptors ◽  
Transmission Electron ◽  
Develop Technology ◽  
Voltage Scanning ◽  
Mechanisms Of Adhesion

The relative roles of adhesion and locomotion in malignancy have yet to be clearly established. In a tumor, subpopulations of cells may be recognized according to their capacity to invade neighbouring tissue,or to enter the blood stream and metastasize. The mechanisms of adhesion and locomotion are themselves tightly linked to the cytoskeletal apparatus and cell surface topology, including expression of integrin receptors. In our studies on melanomas with Fluorescent Microscopy (FM) and Cell Sorter(FACS), we noticed that cells in cultures derived from metastases had more numerous actin bundles, then cells from primary foci. Following this track, we attempted to develop technology allowing to compare ultrastructure of these cells using correlative Transmission Electron Microscopy(TEM) and Low Voltage Scanning Electron Microscopy(LVSEM).

Distribution of VLA-5 and VLA-4 fibronectin receptors in human monocytes demonstrated by immunofluorescence, immunocytochemistry, and autoradiography

1993 ◽  
Vol 51 ◽  
pp. 306-307
Author(s):  
Robert Williams ◽  
Che-Hung Lee ◽  
Sara E. Quella ◽  
David M. Harlan ◽  
Yuan-Hsu Kang
Keyword(s):  
Present Report ◽  
Matrix Proteins ◽  
Extracellular Matrices ◽  
Human Monocytes ◽  
Integrin Receptors ◽  
Morphological Evaluation ◽  
The Matrix ◽  
Specific Receptors ◽  
Cytokine Stimulation ◽  
Monocyte Adherence

Monocyte adherence to endothelial or extracellular matrices plays an important role in triggering monocyte activation in extravascular sites of infection, chronic inflammatory disorders, and tissue damage. Migration of monocytes in the tissues involves the response to a chemoattractant and movement by a series of attachments and detachments to the extracellular matrices which are regulated by expression and distribution of specific receptors for the matrix proteins such as fibronectin (FN). The VSAs (very late antigens or beta integrins), a subfamily of the transmembrane heterodimeric integrin receptors, have been thought to play a major role in monocyte adherence to the extracellular matrices and cells. In this subfamily, VLA-5 and VLA-4 are believed to be the most essential integrins mediating monocyte adherence to FN. In the present report, we have established and compared different procedures for morphological evaluation of the expression and distribution of the FN receptors on human monocytes in order to investigate their response to endotoxin or cytokine stimulation.

Keratinocyte growth factor binds to collagens of the gastrointestinal tract: Identification of the collagen binding structure

2001 ◽  
Vol 120 (5) ◽  
pp. A695-A695
Author(s):  
M RUEHL ◽  
I SCHOENFELDER ◽  
R FARNDALE ◽  
G KNIGHT ◽  
R SOMASUNDARAM ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Growth Factor ◽  
Keratinocyte Growth Factor ◽  
Collagen Binding ◽  
Binding Structure

Plasma Derived von Willebrand Factor Preparations: Collagen Binding and Ristocetin Cofactor Activities

1997 ◽  
Vol 78 (02) ◽  
pp. 930-933 ◽  
Author(s):  
Ping Chang ◽  
D L Aronson
Keyword(s):  
Von Willebrand Factor ◽  
Functional Activity ◽  
Binding Activity ◽  
Collagen Binding ◽  
Binding Function ◽  
Cofactor Activity ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Ristocetin Cofactor ◽  
Ristocetin Cofactor Activity

SummaryFive plasma preparations (11 lots) used in the treatment of von Willebrand’s disease (vWD) were evaluated. The collagen binding function of von Willebrand factor (vWF) containing preparations was compared with the ristocetin cofactor activity and the vWF antigen. Some preparations have higher ratio of functional activity (ristocetin cofactor and collagen binding) relative to the antigen than is found in normal plasma. The ristocetin cofactor activity and the collagen binding activity are tightly correlated (r = .95). Ultracentrifugal (UCF) analysis was used to compare the size distribution of vWf antigen, ristocetin cofactor and collagen binding activity. The sedimentation of all of the vWF parameters in the plasma products was slower than in plasma. In plasma products the ristocetin cofactor activity sediments the most rapidly, the collagen binding activity is slower and the antigen the slowest. The collagen/antigen ratio decreases with decreasing vWF size. Assignment of potency to vWF containing preparations utilizing the collagen binding activity may be more precise and as accurate as with the traditional ristocetin cofactor assay.

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