| pubmed-article:1309744 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1309744 | lifeskim:mentions | umls-concept:C0376604 | lld:lifeskim |
| pubmed-article:1309744 | lifeskim:mentions | umls-concept:C0521428 | lld:lifeskim |
| pubmed-article:1309744 | lifeskim:mentions | umls-concept:C1153433 | lld:lifeskim |
| pubmed-article:1309744 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:1309744 | lifeskim:mentions | umls-concept:C0649006 | lld:lifeskim |
| pubmed-article:1309744 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1309744 | pubmed:dateCreated | 1992-2-18 | lld:pubmed |
| pubmed-article:1309744 | pubmed:abstractText | One of the functions of chromogranin A (CGA), the major soluble component of secretory granules in both adrenal medullary chromaffin cells and many other endocrine cell types appears to be that of a prohormone. CGA is the precursor of several peptides including pancreastatin, a 49-residue peptide, and a 20-residue peptide, chromostatin, which have been identified as biologically active peptides. Chromostatin produces a dose-dependent inhibition (ID50 of 5 nM) of the secretagogue-evoked catecholamine secretion from chromaffin cells. Here we report that chromostatin potently inhibits L-type calcium currents recorded with the nystatin-perforated patch technique in cultured chromaffin cells. This inhibitory effect of chromostatin on calcium currents was not observed in experiments using the classical patch-clamp whole-cell approach which induces the leakage of cytoplasmic components. Using 125I-chromostatin, we show that chromostatin exhibits a fully reversible and saturable binding to the plasma membrane of cultured chromaffin cells. Analysis of binding experiments at equilibrium indicates the existence of one class of binding sites with a Bmax of 2.7 pmol/mg of chromaffin cell proteins and an apparent Kd of 6.5 nM. This high affinity is in good correlation with the half-maximal concentration (ID50 5 nM) of chromostatin inhibiting catecholamine secretion from chromaffin cells. Specificity of the chromostatin binding was further assessed by displacement experiments with unlabeled CGA-related or -unrelated peptides. We found an excellent quantitative correlation between the affinities of the various peptides determined by binding assays and their functional potency tested on catecholamine secretion: bovine chromostatin greater than human chromostatin greater than CGA much greater than rat chromostatin, pancreastatin, CAP-14, substance P, and Leu-enkephalin. Cross-linking experiments reveal that chromostatin associates specifically with an 80-kDa plasma membrane protein. These results together with the patch-clamp experiments support the idea that chromaffin cells possess specific chromostatin receptors and that activation of such receptors leads to the inhibition of L-type voltage-sensitive calcium channels through an intracellular second messenger pathway. | lld:pubmed |
| pubmed-article:1309744 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1309744 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1309744 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1309744 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1309744 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1309744 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:AunisDD | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:GalindoEE | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:HubertPP | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:MendezMM | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:BadenM BMB | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:CeñaVV | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:CalvoSS | lld:pubmed |
| pubmed-article:1309744 | pubmed:author | pubmed-author:Gonzalez-Garc... | lld:pubmed |
| pubmed-article:1309744 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1309744 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1309744 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1309744 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1309744 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1309744 | pubmed:pagination | 407-12 | lld:pubmed |
| pubmed-article:1309744 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1309744 | pubmed:meshHeading | pubmed-meshheading:1309744-... | lld:pubmed |
| pubmed-article:1309744 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1309744 | pubmed:articleTitle | Chromostatin receptors control calcium channel activity in adrenal chromaffin cells. | lld:pubmed |
| pubmed-article:1309744 | pubmed:affiliation | Unité Institut National de la Santé et de la Recherche Médicale, U-338 Biologie de la Communication Cellulaire, Strasbourg, France. | lld:pubmed |
| pubmed-article:1309744 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1309744 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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