scholarly journals Effect of Chemoreceptor Modification on Assembly and Activity of the Receptor-Kinase Complex in Escherichia coli

2004 ◽  
Vol 186 (19) ◽  
pp. 6643-6646 ◽  
Author(s):  
Louisa Liberman ◽  
Howard C. Berg ◽  
Victor Sourjik
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Kinase Activity ◽  
Receptor Activity ◽  
Receptor Kinase ◽  
Cluster Morphology ◽  
Bacterial Chemoreceptors

ABSTRACT Bacterial chemoreceptors are embedded in the inner cell membrane in tight clusters. We show that changes in receptor methylation that generate large changes in kinase activity have relatively little effect on cluster morphology. Thus, changes in receptor activity do not appear to be mediated by changes in receptor-kinase assembly.

Über die Zellmembran von Escherichia Coli B

1954 ◽  
Vol 9 (6) ◽  
pp. 398-406 ◽  
Author(s):  
Wolfhard Weidel ◽  
Gebhard Koch ◽  
Friedrich Lohss
Keyword(s):  
Escherichia Coli ◽  
Chemical Analysis ◽  
Cell Membrane ◽  
B Cell ◽  
Dry Weight ◽  
Shigella Sonnei ◽  
Receptor Activity ◽  
Escherichia Coli B

Dissociation in 90% phenol uncovers a layer of the Coli B-cell membrane showing the typical antiviral specificity of the receptor for phages T3, T4 and T7. Chemical analysis proved glucose, glucosamine and a yet unknown carbohydrate, probably a heptose, to be components of the receptor material, which amounts to about 13% of the dry weight of the whole membrane.Analogous material obtained from the membrane of B/3,4,7, a B-mutant resistant against phages T3, T4 and T7, has no activity against these phages and contains glucosamine and small amounts of glucose, but no heptose.In view of similar findings of Jesaitis and Goebel with T3,4,7 - receptor material from Shigella Sonnei, the rôle of the heptose as a characteristic and functionally indispensable component of lipocarbohydrates with receptor activity against T3, T4 and T7 is discussed.

Insulin-receptor kinase activity of adipose tissue from morbidly obese humans with and without NIDDM

Diabetes ◽  
1987 ◽  
Vol 36 (5) ◽  
pp. 620-625 ◽  
Author(s):  
M. K. Sinha ◽  
W. J. Pories ◽  
E. G. Flickinger ◽  
D. Meelheim ◽  
J. F. Caro
Keyword(s):  
Adipose Tissue ◽  
Insulin Receptor ◽  
Kinase Activity ◽  
Morbidly Obese ◽  
Receptor Kinase ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity

Alteration of insulin-receptor kinase activity by high-fat feeding

Diabetes ◽  
1988 ◽  
Vol 37 (10) ◽  
pp. 1397-1404 ◽  
Author(s):  
T. Watarai ◽  
M. Kobayashi ◽  
Y. Takata ◽  
T. Sasaoka ◽  
M. Iwasaki ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Kinase Activity ◽  
Receptor Kinase ◽  
High Fat ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity ◽  
Fat Feeding

scholarly journals Two Atypical Enteropathogenic Escherichia coli Strains Induce the Production of Secreted and Membrane-Bound Mucins To Benefit Their Own Growth at the Apical Surface of Human Mucin-Secreting Intestinal HT29-MTX Cells

2010 ◽  
Vol 78 (3) ◽  
pp. 927-938 ◽  
Author(s):  
Mônica A. M. Vieira ◽  
Tânia A. T. Gomes ◽  
Antonio J. P. Ferreira ◽  
Terezinha Knöbl ◽  
Alain L. Servin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Brush Border ◽  
Apical Surface ◽  
Enteropathogenic Escherichia Coli ◽  
Typical Epec ◽  
Membrane Bound

ABSTRACT In rabbit ligated ileal loops, two atypical enteropathogenic Escherichia coli (aEPEC) strains, 3991-1 and 0421-1, intimately associated with the cell membrane, forming the characteristic EPEC attachment and effacement lesion of the brush border, induced a mucous hypersecretion, whereas typical EPEC (tEPEC) strain E2348/69 did not. Using cultured human mucin-secreting intestinal HT29-MTX cells, we demonstrate that apically aEPEC infection is followed by increased production of secreted MUC2 and MUC5AC mucins and membrane-bound MUC3 and MUC4 mucins. The transcription of the MUC5AC and MUC4 genes was transiently upregulated after aEPEC infection. We provide evidence that the apically adhering aEPEC cells exploit the mucins' increased production since they grew in the presence of membrane-bound mucins, whereas tEPEC did not. The data described herein report a putative new virulence phenomenon in aEPEC.

Sign in / Sign up

Export Citation Format

Share Document