Structural and Functional Properties of Kappa Tropomyosin
In the myocardium, the gene expresses two isoforms of tropomyosin (Tpm), alpha (αTpm; Tpm 1.1) and kappa (κTpm; Tpm 1.2). κTpm is the result of alternative splicing of the gene. We studied the structural features of κTpm and its regulatory function in the atrial and ventricular myocardium using an i...
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| Veröffentlicht in: | International journal of molecular sciences 2023-05, Vol.24 (9), p.8340 |
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| creator | Kopylova, Galina V Kochurova, Anastasia M Yampolskaya, Daria S Nefedova, Victoria V Tsaturyan, Andrey K Koubassova, Natalia A Kleymenov, Sergey Y Levitsky, Dmitrii I Bershitsky, Sergey Y Matyushenko, Alexander M Shchepkin, Daniil V |
| description | In the myocardium, the
gene expresses two isoforms of tropomyosin (Tpm), alpha (αTpm; Tpm 1.1) and kappa (κTpm; Tpm 1.2). κTpm is the result of alternative splicing of the
gene. We studied the structural features of κTpm and its regulatory function in the atrial and ventricular myocardium using an in vitro motility assay. We tested the possibility of Tpm heterodimer formation from α- and κ-chains. Our result shows that the formation of ακTpm heterodimer is thermodynamically favorable, and in the myocardium, κTpm most likely exists as ακTpm heterodimer. Using circular dichroism, we compared the thermal unfolding of ααTpm, ακTpm, and κκTpm. κκTpm had the lowest stability, while the ακTpm was more stable than ααTpm. The differential scanning calorimetry results indicated that the thermal stability of the N-terminal part of κκTpm is much lower than that of ααTpm. The affinity of ααTpm and κκTpm to F-actin did not differ, and ακTpm interacted with F-actin significantly worse. The troponin T1 fragment enhanced the κκTpm and ακTpm affinity to F-actin. κκTpm differently affected the calcium regulation of the interaction of pig and rat ventricular myosin with the thin filament. With rat myosin, calcium sensitivity of thin filaments containing κκTpm was significantly lower than that with ααTpm and with pig myosin, and the sensitivity did not differ. Thin filaments containing κκTpm and ακTpm were better activated by pig atrial myosin than those containing ααTpm. |
| doi_str_mv | 10.3390/ijms24098340 |
| format | Article |
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gene expresses two isoforms of tropomyosin (Tpm), alpha (αTpm; Tpm 1.1) and kappa (κTpm; Tpm 1.2). κTpm is the result of alternative splicing of the
gene. We studied the structural features of κTpm and its regulatory function in the atrial and ventricular myocardium using an in vitro motility assay. We tested the possibility of Tpm heterodimer formation from α- and κ-chains. Our result shows that the formation of ακTpm heterodimer is thermodynamically favorable, and in the myocardium, κTpm most likely exists as ακTpm heterodimer. Using circular dichroism, we compared the thermal unfolding of ααTpm, ακTpm, and κκTpm. κκTpm had the lowest stability, while the ακTpm was more stable than ααTpm. The differential scanning calorimetry results indicated that the thermal stability of the N-terminal part of κκTpm is much lower than that of ααTpm. The affinity of ααTpm and κκTpm to F-actin did not differ, and ακTpm interacted with F-actin significantly worse. The troponin T1 fragment enhanced the κκTpm and ακTpm affinity to F-actin. κκTpm differently affected the calcium regulation of the interaction of pig and rat ventricular myosin with the thin filament. With rat myosin, calcium sensitivity of thin filaments containing κκTpm was significantly lower than that with ααTpm and with pig myosin, and the sensitivity did not differ. Thin filaments containing κκTpm and ακTpm were better activated by pig atrial myosin than those containing ααTpm.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms24098340</identifier><identifier>PMID: 37176047</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Actin ; Actin Cytoskeleton - chemistry ; Actins - chemistry ; Affinity ; Alternative splicing ; Animals ; Calcium ; Calcium - analysis ; Cardiomyopathy ; Circular dichroism ; Comparative analysis ; Dichroism ; Differential scanning calorimetry ; Filaments ; Isoforms ; Muscle proteins ; Myocardium ; Myosin ; Myosins - analysis ; Rats ; Sensitivity ; Splicing ; Structure-function relationships ; Swine ; Thermal stability ; Transgenic animals ; Tropomyosin ; Tropomyosin - chemistry ; Tropomyosin - genetics ; Troponin ; Ventricle</subject><ispartof>International journal of molecular sciences, 2023-05, Vol.24 (9), p.8340</ispartof><rights>COPYRIGHT 2023 MDPI AG</rights><rights>2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2023 by the authors. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c480t-62eec618d842be2d9310da456e0135dd9e2ceb1f8013b3c3ca84b3fbea5866e73</citedby><cites>FETCH-LOGICAL-c480t-62eec618d842be2d9310da456e0135dd9e2ceb1f8013b3c3ca84b3fbea5866e73</cites><orcidid>0000-0003-4265-1525 ; 0000-0001-5342-1739 ; 0000-0003-2976-2108 ; 0000-0002-5583-5342 ; 0000-0002-7755-9895 ; 0000-0001-5085-0327 ; 0000-0002-0238-4920</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10179609/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10179609/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37176047$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kopylova, Galina V</creatorcontrib><creatorcontrib>Kochurova, Anastasia M</creatorcontrib><creatorcontrib>Yampolskaya, Daria S</creatorcontrib><creatorcontrib>Nefedova, Victoria V</creatorcontrib><creatorcontrib>Tsaturyan, Andrey K</creatorcontrib><creatorcontrib>Koubassova, Natalia A</creatorcontrib><creatorcontrib>Kleymenov, Sergey Y</creatorcontrib><creatorcontrib>Levitsky, Dmitrii I</creatorcontrib><creatorcontrib>Bershitsky, Sergey Y</creatorcontrib><creatorcontrib>Matyushenko, Alexander M</creatorcontrib><creatorcontrib>Shchepkin, Daniil V</creatorcontrib><title>Structural and Functional Properties of Kappa Tropomyosin</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>In the myocardium, the
gene expresses two isoforms of tropomyosin (Tpm), alpha (αTpm; Tpm 1.1) and kappa (κTpm; Tpm 1.2). κTpm is the result of alternative splicing of the
gene. We studied the structural features of κTpm and its regulatory function in the atrial and ventricular myocardium using an in vitro motility assay. We tested the possibility of Tpm heterodimer formation from α- and κ-chains. Our result shows that the formation of ακTpm heterodimer is thermodynamically favorable, and in the myocardium, κTpm most likely exists as ακTpm heterodimer. Using circular dichroism, we compared the thermal unfolding of ααTpm, ακTpm, and κκTpm. κκTpm had the lowest stability, while the ακTpm was more stable than ααTpm. The differential scanning calorimetry results indicated that the thermal stability of the N-terminal part of κκTpm is much lower than that of ααTpm. The affinity of ααTpm and κκTpm to F-actin did not differ, and ακTpm interacted with F-actin significantly worse. The troponin T1 fragment enhanced the κκTpm and ακTpm affinity to F-actin. κκTpm differently affected the calcium regulation of the interaction of pig and rat ventricular myosin with the thin filament. With rat myosin, calcium sensitivity of thin filaments containing κκTpm was significantly lower than that with ααTpm and with pig myosin, and the sensitivity did not differ. Thin filaments containing κκTpm and ακTpm were better activated by pig atrial myosin than those containing ααTpm.</description><subject>Actin</subject><subject>Actin Cytoskeleton - chemistry</subject><subject>Actins - chemistry</subject><subject>Affinity</subject><subject>Alternative splicing</subject><subject>Animals</subject><subject>Calcium</subject><subject>Calcium - analysis</subject><subject>Cardiomyopathy</subject><subject>Circular dichroism</subject><subject>Comparative analysis</subject><subject>Dichroism</subject><subject>Differential scanning calorimetry</subject><subject>Filaments</subject><subject>Isoforms</subject><subject>Muscle proteins</subject><subject>Myocardium</subject><subject>Myosin</subject><subject>Myosins - analysis</subject><subject>Rats</subject><subject>Sensitivity</subject><subject>Splicing</subject><subject>Structure-function relationships</subject><subject>Swine</subject><subject>Thermal stability</subject><subject>Transgenic animals</subject><subject>Tropomyosin</subject><subject>Tropomyosin - chemistry</subject><subject>Tropomyosin - genetics</subject><subject>Troponin</subject><subject>Ventricle</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNptkU1P3DAQhi1UVCjtjXMVqRcOXfBXHPuEEGIpAgkktmfLcSbUq8QOdoK0_75ePlYLQj7YM37m9XhehA4JPmZM4RO37BPlWEnG8Q7aJ5zSGcai-rJ13kPfUlpiTBkt1Ve0xypSCcyrfaTuxzjZcYqmK4xvivnk7eiCz-FdDAPE0UEqQltcm2EwxSLnQr8KyfnvaLc1XYIfr_sB-ju_WJz_md3cXl6dn93MLJd4nAkKYAWRjeS0BtooRnBjeCkAE1Y2jQJqoSatzGHNLLNG8pq1NZhSCgEVO0CnL7rDVPfQWPBjblYP0fUmrnQwTr-_8e6ffghPmmBSKYFVVjh6VYjhcYI06t4lC11nPIQpaSpzJ6Us1Rr99QFdhinmaTxTVBAiyBb1YDrQzrchP2zXovqsKimnTDCaqeNPqLwa6J0NHlqX8-8Kfr8U2BhSitBuPkmwXnutt73O-M_twWzgN3PZf7YZo8g</recordid><startdate>20230506</startdate><enddate>20230506</enddate><creator>Kopylova, Galina V</creator><creator>Kochurova, Anastasia M</creator><creator>Yampolskaya, Daria S</creator><creator>Nefedova, Victoria V</creator><creator>Tsaturyan, Andrey K</creator><creator>Koubassova, Natalia A</creator><creator>Kleymenov, Sergey Y</creator><creator>Levitsky, Dmitrii I</creator><creator>Bershitsky, Sergey Y</creator><creator>Matyushenko, Alexander M</creator><creator>Shchepkin, Daniil V</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4265-1525</orcidid><orcidid>https://orcid.org/0000-0001-5342-1739</orcidid><orcidid>https://orcid.org/0000-0003-2976-2108</orcidid><orcidid>https://orcid.org/0000-0002-5583-5342</orcidid><orcidid>https://orcid.org/0000-0002-7755-9895</orcidid><orcidid>https://orcid.org/0000-0001-5085-0327</orcidid><orcidid>https://orcid.org/0000-0002-0238-4920</orcidid></search><sort><creationdate>20230506</creationdate><title>Structural and Functional Properties of Kappa Tropomyosin</title><author>Kopylova, Galina V ; 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gene expresses two isoforms of tropomyosin (Tpm), alpha (αTpm; Tpm 1.1) and kappa (κTpm; Tpm 1.2). κTpm is the result of alternative splicing of the
gene. We studied the structural features of κTpm and its regulatory function in the atrial and ventricular myocardium using an in vitro motility assay. We tested the possibility of Tpm heterodimer formation from α- and κ-chains. Our result shows that the formation of ακTpm heterodimer is thermodynamically favorable, and in the myocardium, κTpm most likely exists as ακTpm heterodimer. Using circular dichroism, we compared the thermal unfolding of ααTpm, ακTpm, and κκTpm. κκTpm had the lowest stability, while the ακTpm was more stable than ααTpm. The differential scanning calorimetry results indicated that the thermal stability of the N-terminal part of κκTpm is much lower than that of ααTpm. The affinity of ααTpm and κκTpm to F-actin did not differ, and ακTpm interacted with F-actin significantly worse. The troponin T1 fragment enhanced the κκTpm and ακTpm affinity to F-actin. κκTpm differently affected the calcium regulation of the interaction of pig and rat ventricular myosin with the thin filament. With rat myosin, calcium sensitivity of thin filaments containing κκTpm was significantly lower than that with ααTpm and with pig myosin, and the sensitivity did not differ. Thin filaments containing κκTpm and ακTpm were better activated by pig atrial myosin than those containing ααTpm.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>37176047</pmid><doi>10.3390/ijms24098340</doi><orcidid>https://orcid.org/0000-0003-4265-1525</orcidid><orcidid>https://orcid.org/0000-0001-5342-1739</orcidid><orcidid>https://orcid.org/0000-0003-2976-2108</orcidid><orcidid>https://orcid.org/0000-0002-5583-5342</orcidid><orcidid>https://orcid.org/0000-0002-7755-9895</orcidid><orcidid>https://orcid.org/0000-0001-5085-0327</orcidid><orcidid>https://orcid.org/0000-0002-0238-4920</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | International journal of molecular sciences, 2023-05, Vol.24 (9), p.8340 |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Actin Actin Cytoskeleton - chemistry Actins - chemistry Affinity Alternative splicing Animals Calcium Calcium - analysis Cardiomyopathy Circular dichroism Comparative analysis Dichroism Differential scanning calorimetry Filaments Isoforms Muscle proteins Myocardium Myosin Myosins - analysis Rats Sensitivity Splicing Structure-function relationships Swine Thermal stability Transgenic animals Tropomyosin Tropomyosin - chemistry Tropomyosin - genetics Troponin Ventricle |
| title | Structural and Functional Properties of Kappa Tropomyosin |
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