Inhibition of adherence of Actinomyces naeslundii (Actinomyces viscosus) T14V-J1 to saliva-treated hydroxyapatite by a monoclonal antibody to type 1 fimbriae

1996 ◽  
Vol 11 (1) ◽  
pp. 51-58 ◽  
Author(s):  
W. E. Nesbitt ◽  
J. E. Beem ◽  
K-P. Leung ◽  
S. Stroup ◽  
R. Swift ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Type 1 Fimbriae ◽  
Actinomyces Naeslundii

scholarly journals Amended Description of the Genes for Synthesis of Actinomyces naeslundii T14V Type 1 Fimbriae and Associated Adhesin

2007 ◽  
Vol 75 (8) ◽  
pp. 4181-4185 ◽  
Author(s):  
Ping Chen ◽  
John O. Cisar ◽  
Sonja Hess ◽  
Jenny T. C. Ho ◽  
Kai P. Leung
Keyword(s):  
Tooth Surface ◽  
Gram Positive ◽  
Type 1 Fimbriae ◽  
Actinomyces Naeslundii ◽  
Fimbrial Subunit ◽  
Structural Subunit ◽  
A Minor

ABSTRACT The type 1 fimbriae of Actinomyces naeslundii T14V mediate adhesion of this gram-positive species to the tooth surface. The present findings show that the locus for type 1 fimbria production in this strain includes three genes, fimQ for a minor fimbrial subunit that appears to be an adhesin, fimP for the major structural subunit, and srtC1 for a type 1 fimbria-specific sortase involved in the assembly of these structures.

Insulin-like growth factor type 1 receptor (IGF-1R) exclusive nuclear staining: A predictive biomarker for IGF-1R monoclonal antibody (Ab) therapy in sarcomas

2012 ◽  
Vol 48 (16) ◽  
pp. 3027-3035 ◽  
Author(s):  
Irène Asmane ◽  
Emmanuel Watkin ◽  
Laurent Alberti ◽  
Adeline Duc ◽  
Perrine Marec-Berard ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Predictive Biomarker ◽  
Nuclear Staining ◽  
Insulin Like Growth Factor ◽  
Factor Type

Characteristics of ruminant mammary epithelial cells grown in primary culture in serum-free medium

1992 ◽  
Vol 59 (4) ◽  
pp. 491-498 ◽  
Author(s):  
Steven J. Winder ◽  
Alan Turvey ◽  
Isabel A. Forsyth
Keyword(s):  
Monoclonal Antibody ◽  
Mammary Epithelial Cells ◽  
Myoepithelial Cells ◽  
Mammary Epithelial ◽  
Serum Free ◽  
Commercial Medium ◽  
Attachment Factor ◽  
Rat Tail

SummaryCells were obtained from the mammary glands of sheep and cows by collagenase–hyaluronidase digestion. Characterization of cells as epithelial was by reaction with a monoclonal antibody to cytokeratin. A subpopulation of spindle-shaped or stellate cells reacted with a monoclonal antibody to desmin and may be related to myoepithelial cells. The development is described of a simple serum-free culture system for these cells on gels of rat tail (type 1) collagen. A commercial medium (M199) was used, buffered with Hepes and with bovine serum albumin as the sole protein supplement, plus fibronectin for the first 18 h only as an attachment factor. The cell cultures showed stimulated DNA synthesis in response to mitogens on attached gels and also responded as floating cultures to lactogenic hormones with production of α-lactalbumin.

scholarly journals Role of the ceramide-signaling pathway in cytokine responses to P-fimbriated Escherichia coli.

1996 ◽  
Vol 183 (3) ◽  
pp. 1037-1044 ◽  
Author(s):  
M Hedlund ◽  
M Svensson ◽  
A Nilsson ◽  
R D Duan ◽  
C Svanborg
Keyword(s):  
Escherichia Coli ◽  
Signaling Pathway ◽  
Kinase Inhibitors ◽  
Human Kidney ◽  
Cytokine Response ◽  
Protein Kinase Inhibitors ◽  
E Coli ◽  
Type 1 Fimbriae ◽  
Outer Leaflet

Escherichia coli express fimbriae-associated adhesins through which they attach to mucosal cells and activate a cytokine response. The receptors for E. coli P fimbriae are the globoseries of glycosphingolipids; Gal alpha 1-->4Gal beta-containing oligosaccharides bound to ceramide in the outer leaflet of the lipid bilayer. The receptors for type 1 fimbriae are mannosylated glycoproteins rather than glycolipids. This study tested the hypothesis that P-fimbriated E. coli elicit a cytokine response through the release of ceramide in the receptor-bearing cell. We used the A498 human kidney cell line, which expressed functional receptors for P and type 1 fimbriae and secreted higher levels of interleukin (IL)-6 when exposed to the fimbriated strains than to isogenic nonfimbriated controls. P-fimbriated E. coli caused the release of ceramide and increased the phosphorylation of ceramide to ceramide 1-phosphate. The IL-6 response to P-fimbriated E. coli was reduced by inhibitors of serine/threonine kinases but not by other protein kinase inhibitors. In contrast, ceramide levels were not influenced by type 1-fimbriated E. coli, and the IL-6 response was insensitive to the serine/threonine kinase inhibitors. These results demonstrate that the ceramide-signaling pathway is activated by P-fimbriated E. coli, and that the receptor specificity of the P fimbriae influences this process. We propose that this activation pathway contributes to the cytokine induction by P-fimbriated E. coli in epithelial cells.

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