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FRET analysis of Sm2 interaction with actin isoforms in rat aorta smooth muscle cells and tissue
Author(s) -
Black Jason Edward,
Wright Gary L
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1244-b
Subject(s) - gene isoform , actin , myosin , aorta , förster resonance energy transfer , contraction (grammar) , microbiology and biotechnology , biology , vascular smooth muscle , chemistry , medicine , endocrinology , smooth muscle , biochemistry , fluorescence , gene , physics , quantum mechanics
We have examined the differences in association of the myosin II tail isoforms (SM1 and SM2) with the actin isoforms, α‐ and β‐actin, in A7r5 cells and with fluorescence resonance energy transfer (FRET) in rat aorta tissue. Our results with the SM2 isoforms are quite interesting. In the A7r5 cells, no significant changes in the association of the SM2 myosin isoform with each actin isoform were noted when comparing control cells to cells contracted with 10 −7 M phorbol 12,13 dibutyrate (PDBu). Similarly, in tissue the association of SM2 with α‐actin did not change significantly (control, 21 ± 2%, contracted, 12 ± 4%, p<0.1). However, the association of SM2 with β‐actin was decreased when comparing control tissue (22 ± 4%) with contracted tissue (5 ± 5%, p<0.007). This suggests that during contraction these two actin isoforms behave differently during the contraction of aortic smooth muscle. Further studies are in progress to examine the association of SM1 with each of these actin isoforms in rat aorta tissue.