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We used antibodies, microinjection, and transfection to characterize their expression and localization in LLC-PK1 kidney epithelial cells and compared them with other cells. Similar to primary enterocytes, LLC-PK1 cells exhibited predominantly TM-1 and TM-3 of the high-molecular-weight (HMW) isoforms; TM-5 and TM-5b of the low-molecular-weight (LMW) isoforms. Neither TM-4 nor TM-5a was detectable in the LLC-PK1 cells. Immunofluorescence studies revealed that HMW isoforms were localized only on stress fibers, not adhesion belts, whereas the adhesion belts were stained by LMW isoform antibodies. When exogenous proteins are introduced either by transfection or microinjection, the HMW isoforms do not incorporate into the adhesion belt, whereas the LMW isoforms can incorporate into the stress fibers, thus indicating there are different mechanisms at work for the selective localization. Temporal changes in the microfilament system of the LLC-PK1 cells were studied during differentiation in culture as defined by spectrin expression and F-actin architecture. Western blot analysis indicated that TM-5b is only expressed in the LLC-PK1 cells after a certain degree of maturation in culture, which suggests isoform switching after the cell–cell contacts are developed. Collectively these results demonstrate that epithelial cells express a complex pattern of TM isoforms, which exhibit differential localizations within the cells and different patterns of expression depending on their origin and stage of differentiation. The implication of differential localization of TM isoforms on their specific functions is discussed. Cell Motil. Cytoskeleton 40:393–407, 1998. © 1998 Wiley-Liss, Inc.", "publicationTitle": "Cell Motility and the Cytoskeleton", "publisher": "", "place": "", "date": "1998", "volume": "40", "issue": "4", "section": "", "partNumber": "", "partTitle": "", "pages": "393–407", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1002/(SICI)1097-0169(1998)40:4<393::AID-CM7>3.0.CO;2-C", "citationKey": "", "url": "http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0169(1998)40:4<393::AID-CM7>3.0.CO;2-C/abstract", "accessDate": "2013-03-06T23:24:00Z", "PMID": "", "PMCID": "", "ISSN": "1097-0169", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "Wiley Online Library", "callNumber": "", "rights": "Copyright © 1998 Wiley-Liss, Inc.", "extra": "", "tags": [ { "tag": "brush border", "type": 1 }, { "tag": "differentiation", "type": 1 }, { "tag": "epitope tagging", "type": 1 }, { "tag": "kidney", "type": 1 }, { "tag": "temporal expression", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-03-06T23:24:00Z", "dateModified": "2013-03-06T23:24:00Z" } }, { "key": "5AKTGWUG", "version": 43, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/5AKTGWUG", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/5AKTGWUG", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "creatorSummary": "Marston and Redwood", "parsedDate": "1993-06-15", "numChildren": 2 }, "data": { "key": "5AKTGWUG", "version": 43, "itemType": "journalArticle", "title": "The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon.", "creators": [ { "creatorType": "author", "firstName": "S. B.", "lastName": "Marston" }, { "creatorType": "author", "firstName": "C. S.", "lastName": "Redwood" } ], "abstractNote": "We compared the mechanisms by which caldesmon inhibits actin and actin-tropomyosin activation of myosin subfragment 1 (S1) MgATPase activity. Caldesmon always inhibited actin activation by displacing S1.ADP.Pi from actin and inhibition required at least 0.7 caldesmon molecules bond per actin for 90% inhibition. Caldesmon inhibited actin-tropomyosin without any displacement of S1.ADP.Pi; thus it inhibits a rate-limiting step. Inhibition is highly cooperative, requiring no more than one caldesmon bound per 10 actins for 90% inhibition of activation by actin and smooth muscle tropomyosin. The degree of cooperativity is defined by the tropomyosin since inhibition by skeletal tropomyosin requires up to one caldesmon bound per 4 actins for 90% inhibition under identical conditions. Both noncooperative inhibition of actin and cooperative, tropomyosin-dependent, inhibition are manifested by a fragment of caldesmon containing only the C-terminal 99 amino acids (658C), although this fragment does not itself bind to tropomyosin. The functional properties of 658C are very similar to striated muscle troponin I, consequently we propose a similar mechanism for tropomyosin-dependent regulation by caldesmon. Caldesmon binding switches actin-tropomyosin to the \"off\" or \"weak\" state and Ca2+/calmodulin binding to caldesmon blocks this switch and thus reactivates the actin filament.", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "06/15/1993", "volume": "268", "issue": "17", "section": "", "partNumber": "", "partTitle": "", "pages": "12317-12320", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "", "citationKey": "", "url": "http://www.jbc.org/content/268/17/12317", "accessDate": "2013-02-10T21:45:44Z", "PMID": "", "PMCID": "", "ISSN": "0021-9258, 1083-351X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.jbc.org", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-02-24T20:17:53Z", "dateModified": "2013-03-06T23:22:20Z" } }, { "key": "T6FPX4HZ", "version": 38, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/T6FPX4HZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/T6FPX4HZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/150769/items/79G72TKQ", "type": "application/json" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "T6FPX4HZ", "version": 38, "parentItem": "79G72TKQ", "itemType": "attachment", "linkMode": "imported_url", "title": "PubMed Central Full Text PDF", "accessDate": "2013-03-06T23:12:22Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1664955/pdf/tjp0556-0531.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Gaffin et al. - 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2004 - Charged residue changes in the carboxy-terminus of.pdf", "md5": "a6352b7770f4ae409a43f83de5228cbe", "mtime": 1362611519000, "tags": [], "relations": {}, "dateAdded": "2013-03-06T23:11:58Z", "dateModified": "2013-03-06T23:11:59Z" } }, { "key": "7TFEJ8CI", "version": 35, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/7TFEJ8CI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/7TFEJ8CI", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/150769/items/BXNC2PM3", "type": "application/json" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } } }, "data": { "key": "7TFEJ8CI", "version": 35, "parentItem": "BXNC2PM3", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2013-03-06T23:11:58Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1664955/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2013-03-06T23:11:58Z", "dateModified": "2013-03-06T23:11:58Z" } }, { "key": "BXNC2PM3", "version": 35, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/BXNC2PM3", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/BXNC2PM3", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "creatorSummary": "Gaffin et al.", "parsedDate": "2004-04-15", "numChildren": 2 }, "data": { "key": "BXNC2PM3", "version": 35, "itemType": "journalArticle", "title": "Charged residue changes in the carboxy-terminus of ?-tropomyosin alter mouse cardiac muscle contractility", "creators": [ { "creatorType": "author", "firstName": "Robert D", "lastName": "Gaffin" }, { "creatorType": "author", "firstName": "Kuppan", "lastName": "Gokulan" }, { "creatorType": "author", "firstName": "James C", "lastName": "Sacchettini" }, { "creatorType": "author", "firstName": "Timothy", "lastName": "Hewett" }, { "creatorType": "author", "firstName": "Raisa", "lastName": "Klevitsky" }, { "creatorType": "author", "firstName": "Jeffrey", "lastName": "Robbins" }, { "creatorType": "author", "firstName": "Mariappan", "lastName": "Muthuchamy" } ], "abstractNote": "Striated muscle tropomyosin (TM) is an essential thin filament protein that is sterically and allosterically involved in calcium-mediated cardiac contraction. We have previously shown that overexpressing the β-TM isoform in mouse hearts leads to physiological changes in myocardial relaxation and Ca2+ handling of myofilaments. Two important charge differences in β-TM compared to α-TM are the exchange of serine and histidine at positions 229 and 276 with glutamic acid and asparagine, respectively, imparting a more negative charge to β-TM relative to α-TM. Our hypothesis is that the net charge at specific sites on TM might be a major determinant of its role in modulating cardiac muscle performance and in regulating Ca2+ sensitivity of the myofilaments. To address this, we generated transgenic (TG) double mutation mouse lines (α-TM DM) expressing mutated α-TM at the two residues that differ between α- and β-TM (Ser229Glu + His276Asn). Molecular analyses show 60–88% of the native TM is replaced with α-TM DM in the different TG lines. Work-performing heart analyses show that α-TM DM mouse hearts exhibit decreased rates of pressure development and relaxation (+dP/dt and –dP/dt). Skinned myofibre preparations from the TG hearts indicate a decrease in calcium sensitivity of steady state force. Protein modelling studies show that these two charge alterations in α-TM cause a change in the surface charges of the molecule. Our results provide the first evidence that charge changes at the carboxy-terminal of α-TM alter the functional characteristics of the heart at both the whole organ and myofilament levels.", "publicationTitle": "The Journal of Physiology", "publisher": "", "place": "", "date": "2004-4-15", "volume": "556", "issue": "Pt 2", "section": "", "partNumber": "", "partTitle": "", "pages": "531-543", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J Physiol", "DOI": "10.1113/jphysiol.2003.058487", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1664955/", "accessDate": "2013-03-06T23:11:58Z", "PMID": "", "PMCID": "", "ISSN": "0022-3751", "archive": "", "archiveLocation": "", "shortTitle": "Charged residue changes in the carboxy-terminus of ?", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 14766940\nPMCID: PMC1664955", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-03-06T23:11:58Z", "dateModified": "2013-03-06T23:11:58Z" } }, { "key": "9TRCCWQK", "version": 34, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/9TRCCWQK", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/9TRCCWQK", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "creatorSummary": "Graceffa", "parsedDate": "1987-06-22", "numChildren": 2 }, "data": { "key": "9TRCCWQK", "version": 34, "itemType": "journalArticle", "title": "Evidence for interaction between smooth muscle tropomyosin and caldesmon", "creators": [ { "creatorType": "author", "firstName": "Philip", "lastName": "Graceffa" } ], "abstractNote": "The viscosity of chicken gizzard smooth muscle tropomyosin is enhanced 4.7-fold in the absence of salt and 1.43-fold in 0.1 M salt by the presence of stoichiometric amounts of gizzard caldesmon, indicating that the two proteins interact under these conditions. Since the thin filament regulation of smooth muscle contraction by caldesmon requires the presence of tropomyosin, these results suggest that the direct interaction between tropomyosin and caldesmon on the thin filament plays a role in this regulation.", "publicationTitle": "FEBS Letters", "publisher": "", "place": "", "date": "June 22, 1987", "volume": "218", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "139-142", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "FEBS Letters", "DOI": "10.1016/0014-5793(87)81034-7", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/0014579387810347", "accessDate": "2013-02-10T21:41:04Z", "PMID": "", "PMCID": "", "ISSN": "0014-5793", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "(Smooth muscle)", "type": 1 }, { "tag": "Caldesmon", "type": 1 }, { "tag": "Tropomyosin", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-02-24T20:17:53Z", "dateModified": "2013-03-06T23:08:54Z" } }, { "key": "TN935KK3", "version": 33, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/TN935KK3", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/TN935KK3", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/150769/items/RQV2BN4V", "type": "application/json" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "TN935KK3", "version": 33, "parentItem": "RQV2BN4V", "itemType": "attachment", "linkMode": "imported_url", "title": "PubMed Central Full Text PDF", "accessDate": "2013-03-06T23:08:19Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC151575/pdf/mk0303001002.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Bryce et al. - 2003 - Specification of Actin Filament Function and Molec.pdf", "md5": "201a5792a68bfe1653c17683725867f1", "mtime": 1362611303000, "tags": [], "relations": {}, "dateAdded": "2013-03-06T23:08:19Z", "dateModified": "2013-03-06T23:08:23Z" } }, { "key": "8P4FHRJE", "version": 32, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/8P4FHRJE", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/8P4FHRJE", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/150769/items/RQV2BN4V", "type": "application/json" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } } }, "data": { "key": "8P4FHRJE", "version": 32, "parentItem": "RQV2BN4V", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2013-03-06T23:08:19Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC151575/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2013-03-06T23:08:19Z", "dateModified": "2013-03-06T23:08:19Z" } }, { "key": "RQV2BN4V", "version": 32, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/RQV2BN4V", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/RQV2BN4V", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "creatorSummary": "Bryce et al.", "parsedDate": "2003-03", "numChildren": 2 }, "data": { "key": "RQV2BN4V", "version": 32, "itemType": "journalArticle", "title": "Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms", "creators": [ { "creatorType": "author", "firstName": "Nicole S.", "lastName": "Bryce" }, { "creatorType": "author", "firstName": "Galina", "lastName": "Schevzov" }, { "creatorType": "author", "firstName": "Vicki", "lastName": "Ferguson" }, { "creatorType": "author", "firstName": "Justin M.", "lastName": "Percival" }, { "creatorType": "author", "firstName": "Jim J.-C.", "lastName": "Lin" }, { "creatorType": "author", "firstName": "Fumio", "lastName": "Matsumura" }, { "creatorType": "author", "firstName": "James R.", "lastName": "Bamburg" }, { "creatorType": "author", "firstName": "Peter L.", "lastName": "Jeffrey" }, { "creatorType": "author", "firstName": "Edna C.", "lastName": "Hardeman" }, { "creatorType": "author", "firstName": "Peter", "lastName": "Gunning" }, { "creatorType": "author", "firstName": "Ron P.", "lastName": "Weinberger" } ], "abstractNote": "The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability of two Tm isoforms, TmBr3 and the human homologue of Tm5 (hTM5NM1), to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, cell size, and shape. hTm5NM1 was able to recruit myosin II into stress fibers, which resulted in decreased lamellipodia and cellular migration. In contrast, TmBr3 transfection induced lamellipodial formation, increased cellular migration, and reduced stress fibers. Based on coimmunoprecipitation and colocalization studies, TmBr3 appeared to be associated with actin-depolymerizing factor/cofilin (ADF)-bound actin filaments. Additionally, the Tms can specifically regulate the incorporation of other Tms into actin filaments, suggesting that selective dimerization may also be involved in the control of actin filament organization. We conclude that Tm isoforms can be used to specify the functional properties and molecular composition of actin filaments and that spatial segregation of isoforms may lead to localized specialization of actin filament function.", "publicationTitle": "Molecular Biology of the Cell", "publisher": "", "place": "", "date": "2003-3", "volume": "14", "issue": "3", "section": "", "partNumber": "", "partTitle": "", "pages": "1002-1016", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Mol Biol Cell", "DOI": "10.1091/mbc.E02-04-0244", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC151575/", "accessDate": "2013-03-06T23:08:19Z", "PMID": "", "PMCID": "", "ISSN": "1059-1524", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 12631719\nPMCID: PMC151575", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-03-06T23:08:19Z", "dateModified": "2013-03-06T23:08:19Z" } }, { "key": "JZ4XNFHD", "version": 31, "library": { "type": "group", "id": 150769, "name": "dat will guilford", "links": { "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/150769/items/JZ4XNFHD", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/dat_will_guilford/items/JZ4XNFHD", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/150769/items/5HC2T58A", "type": "application/json" } }, "meta": { "createdByUser": { "id": 1284293, "username": "mse3xa", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/mse3xa", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "JZ4XNFHD", "version": 31, "parentItem": "5HC2T58A", "itemType": "attachment", "linkMode": "imported_url", "title": "Full Text PDF", "accessDate": "2013-03-03T14:37:10Z", "url": "http://link.springer.com/content/pdf/10.1007%2F978-0-387-85766-4_5", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Hitchcock-DeGregori - 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