The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae

1990 ◽  
Vol 220 (2) ◽  
pp. 334-338 ◽  
Author(s):  
Per Klemm ◽  
Gunna Christiansen
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Type 1 Fimbriae ◽  
Surface Localization ◽  
Cell Surface Localization

Cdc42 and RhoA have opposing roles in regulating membrane type 1-matrix metalloproteinase localization and matrix metalloproteinase-2 activation

2008 ◽  
Vol 295 (3) ◽  
pp. C600-C610 ◽  
Author(s):  
Eric Ispanovic ◽  
Damiano Serio ◽  
Tara L. Haas
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Actin Cytoskeleton ◽  
Cortical Actin ◽  
Rhoa Activity ◽  
Surface Localization ◽  
Cell Surface Localization ◽  
Membrane Type

Proteolysis of the basement membrane and interstitial matrix occurs early in the angiogenic process and requires matrix metalloproteinase (MMP) activity. Skeletal muscle microvascular endothelial cells exhibit robust actin stress fibers, low levels of membrane type 1 (MT1)-MMP expression, and minimal MMP-2 activation. Depolymerization of the actin cytoskeleton increases MT1-MMP expression and MMP-2 activation. Rho family GTPases are regulators of actin cytoskeleton dynamics, and their activity can be modulated in response to angiogenic stimuli such as vascular endothelial growth factor (VEGF). Therefore, we investigated their roles in MMP-2 and MT1-MMP production. Endothelial cells treated with H1152 [an inhibitor of Rho kinase (ROCK)] induced stress fiber depolymerization and an increase in cortical actin. Both MMP-2 and MT1-MMP mRNA increased, which translated into greater MMP-2 protein production and activation. ROCK inhibition rapidly increased cell surface localization of MT1-MMP and increased PI3K activity, which was required for MMP-2 activation. Constitutively active Cdc42 increased cortical actin polymerization, phosphatidylinositol 3-kinase activity, MT1-MMP cell surface localization, and MMP-2 activation similarly to inhibition of ROCK. Activation of Cdc42 was sufficient to decrease RhoA activity. Capillary sprout formation in a three-dimensional collagen matrix was increased in cultures treated with RhoAN19 or Cdc42QL and, conversely, decreased in cultures treated with dominant negative Cdc42N17. VEGF stimulation also induced activation of Cdc42 while inhibiting RhoA activity. Furthermore, VEGF-dependent activation of MMP-2 was reduced by inhibition of Cdc42. These results suggest that Cdc42 and RhoA have opposing roles in regulating cell surface localization of MT1-MMP and MMP-2 activation.

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.

Type 1 Fimbriae of Escherichia coli

Fimbriae ◽  
2020 ◽  
pp. 9-26
Author(s):  
Per Klemm ◽  
Karen Angeliki Krogfelt
Keyword(s):  
Escherichia Coli ◽  
Type 1 Fimbriae

scholarly journals Pseudocatabolite repression of type 1 fimbriae of Escherichia coli.

1982 ◽  
Vol 151 (3) ◽  
pp. 1560-1567 ◽  
Author(s):  
B I Eisenstein ◽  
D C Dodd
Keyword(s):  
Escherichia Coli ◽  
Type 1 Fimbriae

scholarly journals Expression of Escherichia coli F-18 type 1 fimbriae in the streptomycin-treated mouse large intestine.

1991 ◽  
Vol 59 (4) ◽  
pp. 1567-1568 ◽  
Author(s):  
K A Krogfelt ◽  
B A McCormick ◽  
R L Burghoff ◽  
D C Laux ◽  
P S Cohen
Keyword(s):  
Escherichia Coli ◽  
Large Intestine ◽  
Treated Mouse ◽  
Type 1 Fimbriae

FimH adhesin of Escherichia coli K1 type 1 fimbriae activates BV-2 microglia

2005 ◽  
Vol 334 (3) ◽  
pp. 917-923 ◽  
Author(s):  
Jongseok Lee ◽  
Sooan Shin ◽  
Ching-Hao Teng ◽  
Suk Jin Hong ◽  
Kwang Sik Kim
Keyword(s):  
Escherichia Coli ◽  
Type 1 Fimbriae ◽  
Escherichia Coli K1
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