Linked Life Data

19625374

Source:http://linkedlifedata.com/resource/pubmed/id/19625374

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-9-29
pubmed:abstractText
Bacterial infection of the kidney is associated with renal tubule dysfunction and dysregulation of systemic electrolyte balance. Whether bacterial molecules directly affect renal tubule transport is unknown. We examined the effects of LPS on HCO3(-) absorption in the isolated rat and mouse medullary thick ascending limb (MTAL). LPS decreased HCO3(-) absorption when added to bath or lumen. The MEK/ERK inhibitor U0126 eliminated inhibition by bath LPS but had no effect on inhibition by lumen LPS. Conversely, the mammalian target of rapamycin (mTOR) inhibitor rapamycin eliminated inhibition by lumen LPS but had no effect on inhibition by bath LPS. Inhibiting basolateral Na(+)/H(+) exchange with amiloride eliminated inhibition of HCO3(-) absorption by lumen but not bath LPS. Confocal immunofluorescence showed expression of TLR4 in basolateral and apical membrane domains. Inhibition of HCO3(-) absorption by bath and lumen LPS was eliminated in MTALs from TLR4(-/-) mice. Thus LPS inhibits HCO3(-) absorption through distinct TLR4-dependent pathways in basolateral and apical membranes. These results establish that bacterial molecules can directly impair the transport function of renal tubules, identifying a new mechanism contributing to tubule dysfunction during bacterial infection. The LPS-induced reduction in luminal acidification may contribute to Gram-negative pathogenicity by promoting bacterial adherence and growth and impairing correction of infection-induced systemic acid-base disorders.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1522-1466
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
297
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
F866-74
pubmed:dateRevised
2011-4-28
pubmed:meshHeading
pubmed-meshheading:19625374-Amiloride, pubmed-meshheading:19625374-Animals, pubmed-meshheading:19625374-Bicarbonates, pubmed-meshheading:19625374-Butadienes, pubmed-meshheading:19625374-Disease Progression, pubmed-meshheading:19625374-Endotoxemia, pubmed-meshheading:19625374-Escherichia coli Infections, pubmed-meshheading:19625374-Escherichia coli K12, pubmed-meshheading:19625374-Immunity, Innate, pubmed-meshheading:19625374-Kidney Tubules, pubmed-meshheading:19625374-Lipid A, pubmed-meshheading:19625374-Lipopolysaccharides, pubmed-meshheading:19625374-Male, pubmed-meshheading:19625374-Mice, pubmed-meshheading:19625374-Mice, Inbred C57BL, pubmed-meshheading:19625374-Mice, Knockout, pubmed-meshheading:19625374-Nitriles, pubmed-meshheading:19625374-Rats, pubmed-meshheading:19625374-Rats, Sprague-Dawley, pubmed-meshheading:19625374-Serum, pubmed-meshheading:19625374-Signal Transduction, pubmed-meshheading:19625374-Sirolimus, pubmed-meshheading:19625374-Toll-Like Receptor 4, pubmed-meshheading:19625374-Urinary Tract Infections
pubmed:year
2009
pubmed:articleTitle
Lipopolysaccharide directly alters renal tubule transport through distinct TLR4-dependent pathways in basolateral and apical membranes.
pubmed:affiliation
Div. of Nephrology, 4.200 John Sealy Annex, The Univ. of Texas Medical Branch, 301 Univ. Blvd., Galveston, TX 77555-0562, USA. dgood@utmb.edu
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural