Linked Life Data

20538895

Source:http://linkedlifedata.com/resource/pubmed/id/20538895

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-8-3
pubmed:abstractText
In the past, we have used the kinins of the cockroach Leucophaea (the leucokinins) to evaluate the mechanism of diuretic action of kinin peptides in Malpighian tubules of the yellow fever mosquito Aedes aegypti. Now using the kinins of Aedes (the aedeskinins), we have found that in isolated Aedes Malpighian tubules all three aedeskinins (1 microM) significantly 1) increased the rate of fluid secretion (V(S)), 2) hyperpolarized the basolateral membrane voltage (V(bl)), and 3) decreased the input resistance (R(in)) of principal cells, consistent with the known increase in the Cl(-) conductance of the paracellular pathway in Aedes Malpighian tubules. Aedeskinin-III, studied in further detail, significantly increased V(S) with an EC(50) of 1.5 x 10(-8) M. In parallel, the Na(+) concentration in secreted fluid significantly decreased, and the K(+) concentration significantly increased. The concentration of Cl(-) remained unchanged. While the three aedeskinins triggered effects on V(bl), R(in), and V(S), synthetic kinin analogs, which contain modifications of the COOH-terminal amide pentapeptide core sequence critical for biological activity, displayed variable effects. For example, kinin analog 1578 significantly stimulated V(S) but had no effect on V(bl) and R(in), whereas kinin analog 1708 had no effect on V(S) but significantly affected V(bl) and R(in). These observations suggest separate signaling pathways activated by kinins. One triggers the electrophysiological response, and the other triggers fluid secretion. It remains to be determined whether the two signaling pathways emanate from a single kinin receptor via agonist-directed signaling or from a differentially glycosylated receptor. Occasionally, Malpighian tubules did not exhibit a detectable response to natural and synthetic kinins. Hypothetically, the expression of the kinin receptor may depend on developmental, nutritional, and/or reproductive signals.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1522-1490
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
299
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
R612-22
pubmed:dateRevised
2010-12-17
pubmed:meshHeading
pubmed-meshheading:20538895-Aedes, pubmed-meshheading:20538895-Animals, pubmed-meshheading:20538895-Body Fluids, pubmed-meshheading:20538895-Chlorides, pubmed-meshheading:20538895-Electric Impedance, pubmed-meshheading:20538895-Epithelial Cells, pubmed-meshheading:20538895-Insect Proteins, pubmed-meshheading:20538895-Kinetics, pubmed-meshheading:20538895-Kinins, pubmed-meshheading:20538895-Malpighian Tubules, pubmed-meshheading:20538895-Membrane Potentials, pubmed-meshheading:20538895-Potassium, pubmed-meshheading:20538895-Protein Conformation, pubmed-meshheading:20538895-Receptors, G-Protein-Coupled, pubmed-meshheading:20538895-Signal Transduction, pubmed-meshheading:20538895-Sodium, pubmed-meshheading:20538895-Structure-Activity Relationship, pubmed-meshheading:20538895-Yellow fever virus
pubmed:year
2010
pubmed:articleTitle
The single kinin receptor signals to separate and independent physiological pathways in Malpighian tubules of the yellow fever mosquito.
pubmed:affiliation
Dept. of Biomedical Sciences, VRT 8004, Cornell Univ., Ithaca, NY 14853, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.