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Similarly applied, this reagent brings about iodination of cell membranes, although, apparently, at a somewhat lesser rate than in iodinations carried out with lactoperoxidase-glucose oxidase. 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The present experiments were designed to analyse alternative mechanisms, trying to test the hypothesis that cGMP could relax rat mesangial cells by activating myosin light-chain phosphatase (MLC-PP), with the subsequent dephosphorylation of myosin light chain (MLC). The effect of a cGMP analogue, dibutyryl cGMP (dbcGMP), on angiotensin II-(AII) and PMA-induced MLC phosphorylation (MLCP) was tested, in the presence of calyculin A (CA), an inhibitor of MLC-PP. MLCP was measured, after cell labelling with (32)P, by immunoprecipitation. dbcGMP prevented the increased MLCP induced by AII or PMA, and this inhibition was blocked by CA. dbcGMP also increased the MLC dephosphorylation observed in cells incubated with AII and in which MLC kinase and protein kinase C activities were blocked. The AII-elicited increased intracellular calcium concentration was only partially inhibited by dbcGMP. These results suggest that the cGMP-induced mesangial-cell relaxation could be due, at least partially, to the stimulation of MLC-PP.", "publicationTitle": "Biochemical Journal", "publisher": "", "place": "", "date": "2000-2-15", "volume": "346", "issue": "Pt 1", "section": "", "partNumber": "", "partTitle": "", "pages": "217-222", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biochem J", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0264-6021", "archive": "", "archiveLocation": "", "shortTitle": "Mechanisms of cGMP-dependent mesangial-cell relaxation", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 10657260\nPMCID: PMC1220843", "tags": [], "collections": [], "relations": {}, "dateAdded": "2012-04-29T04:02:20Z", "dateModified": "2012-04-29T04:02:20Z" } }, { "key": "HUT6X8W2", "version": 1, "library": { "type": "group", "id": 69449, "name": "BME2104 - CCC", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_-_ccc", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/69449/items/HUT6X8W2", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_-_ccc/items/HUT6X8W2", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/69449/items/4V3ZX3SR", "type": "application/json" } }, "meta": { "createdByUser": { "id": 899870, "username": "cnc8ad", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/cnc8ad", "type": "text/html" } } } }, "data": { "key": "HUT6X8W2", "version": 1, "parentItem": "4V3ZX3SR", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2012-04-29T04:02:20Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220843/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2012-04-29T04:02:20Z", "dateModified": "2012-04-29T04:02:20Z" } }, { "key": "TBCJUARH", "version": 2, "library": { "type": "group", "id": 69449, "name": "BME2104 - 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The thin filament was selectively removed from bovine cardiac skinned muscle fibres by gelsolin, and the actin filament was reconstituted from purified G-actin. In this reconstitution, yeast wild-type actin (2Ac: two N-terminal negative charges), yeast mutant actins (3Ac and 4Ac), and rabbit skeletal muscle actin (MAc) were used. The effects of phosphate, ATP and ADP on force development were studied at 25°C. With MAc, isometric tension was 77% of the initial tension owing to the lack of a regulatory system. With 2Ac, isometric tension was 10% of the initial tension; with 3Ac, isometric tension was 23%; and with 4Ac, isometric tension was 44%. Stiffness followed a similar pattern (2Ac < 3Ac < 4Ac < MAc). A similar trend was observed during rigor induction and relaxation. Sinusoidal analysis was performed to obtain the kinetic constants of the cross-bridge cycle. The results showed that the variability of the kinetic constants was ≤ 2.5-fold among the 2Ac, 4Ac and MAc muscle models. When the cross-bridge distribution was examined, there was no significant reapportionment among these three models examined. These results indicate that force supported by each cross-bridge is modified by the N-terminal negative charges of actin, presumably via the actomyosin interface. 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