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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-1-9
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pubmed:abstractText |
The hormone-induced depletion of cellular Ca stores provides a signal for the Ca2+ influx into electrically non-excitable cells; however, the underlying molecular mechanisms remain elusive. Therefore, we analyzed bradykinin-activated Ca2+ influx into human foreskin fibroblast cells, HF-15, by fura-2 and 45Ca labeling to discriminate between Ca2+ influx into the fura-sensitive compartment and Ca uptake into fura-insensitive Ca stores. Bradykinin-activated Ca2+ influx into the fura-sensitive compartment was blocked by inhibitors of NO synthases. These inhibitors also suppressed bradykinin-activated increases in cGMP, indicating that the NO-dependent increase in cGMP is involved in the activation of the Ca2+ influx into the fura-sensitive compartment. The cGMP-dependent kinase inhibitors KT5823 and Rp-8-(parachlorophenylthio)-cGMP (Rp-8-pCPT-cGMPS) blocked bradykinin-activated Ca2+ influx into the fura-sensitive compartment, suggesting that a cGMP-dependent kinase step participates in the activation of this Ca2+ influx pathway. In addition to the NO/cGMP-mediated Ca2+ influx into the fura-sensitive compartment, bradykinin enhanced 45Ca uptake into Ca stores that were not accessible to fura-2. This enhanced 45Ca uptake was insensitive to blockers of the NO/cGMP pathway, indicating that the 45Ca uptake pathway is distinct from the NO-dependent Ca2+ influx into the fura-sensitive compartment. Furthermore, bradykinin enhanced 45Ca uptake into proliferating but not into quiescent HF-15 fibroblasts. Hence, bradykinin stimulates two distinct Ca2+ influx pathways in HF-15 cells, (a) Ca2+ influx into the fura-sensitive compartment which is NO/cGMP-dependent and (b) Ca uptake into Ca stores which bypasses the cytoplasm, which is NO insensitive and which is linked to cell proliferation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Fura-2,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Bradykinin B2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bradykinin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
241
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
498-506
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8917448-Bradykinin,
pubmed-meshheading:8917448-Calcium,
pubmed-meshheading:8917448-Calcium Channel Blockers,
pubmed-meshheading:8917448-Cell Division,
pubmed-meshheading:8917448-Cell Line,
pubmed-meshheading:8917448-Cyclic GMP,
pubmed-meshheading:8917448-Cyclic GMP-Dependent Protein Kinases,
pubmed-meshheading:8917448-Fluorescent Dyes,
pubmed-meshheading:8917448-Fura-2,
pubmed-meshheading:8917448-Humans,
pubmed-meshheading:8917448-Interphase,
pubmed-meshheading:8917448-Ion Transport,
pubmed-meshheading:8917448-Nitric Oxide,
pubmed-meshheading:8917448-Receptor, Bradykinin B2,
pubmed-meshheading:8917448-Receptors, Bradykinin
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pubmed:year |
1996
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pubmed:articleTitle |
Two distinct Ca2+ influx pathways activated by the bradykinin B2 receptor.
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pubmed:affiliation |
Institute of Physiological Chemistry and Pathobiochemistry, University of Mainz, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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