Distribution of myosin isozymes in human atrial and ventricular myocardium: comparison in normal and overloaded heart

Yazaki, Yoshio; Tsuchimochi, Hidetsugu; Kuro‐o, Makoto; Kurabayashi, Masahiko; Isobe, Mitsuaki; Ueda, Seigo; Nagai, Ryouzou; Takaku, Fumimaro

doi:10.1093/eurheartj/5.suppl_f.103

Cited by 44 publications

(18 citation statements)

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“…A rat anti-mouse CD18 mAb (M18/2, IgG2a) was purchased from American Type Culture Collection (Rockville, MD) ( 17). The preparation ofa mouse anti-cardiac myosin mAb (CMA 19) was previously described ( 18). The reactivity of CMAl9 for C3H/He mouse ventricular myosin heavy chain was confirmed by immunoblot analysis (data not shown).…”

Section: Ifn-y * Tnf-amentioning

confidence: 94%

Expression of intercellular adhesion molecule-1 in murine hearts with acute myocarditis caused by coxsackievirus B3.

Seko

Matsuda²,

Kato³

et al. 1993

J. Clin. Invest.

109

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Section: Ifn-y * Tnf-amentioning

confidence: 94%

Expression of intercellular adhesion molecule-1 in murine hearts with acute myocarditis caused by coxsackievirus B3.

Seko

Matsuda²,

Kato³

et al. 1993

J. Clin. Invest.

109

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“…rat IgG2a) [14] were described elsewhere and were used for immunohistochemical study and in vivo mAb treatment study. The preparation of mouse anti-cardiac myosin mAb (CMA19) was as published elsewhere [20]. Another anti-mouse PD-1 mAb (hybridoma PIM-2, rat IgG2a) was recently developed.…”

Section: Monoclonal Antibodies (Mabs)mentioning

confidence: 99%

Roles of programmed death-1 (PD-1)/PD-1 ligands pathway in the development of murine acute myocarditis caused by coxsackievirus B3

Seko¹,

Yagita²,

Okumura³

et al. 2007

Cardiovascular Research

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Objective: This study was designed to investigate the roles of programmed death-1 (PD-1) and PD-1ligands (PD-L) in the development of murine acute myocarditis caused by Coxsackievirus B3. PD-1/PD-L belong to the CD28/B7 superfamily, and the PD-1/PD-L pathway is known to transduce a negative immunoregulatory signal that antagonizes the T-cell receptor-CD28 signal and inhibits T-cell activation. Methods: We first analyzed the expression of PD-L1/PD-L2 on cardiac myocytes in vivo and in vitro. Second, we examined the effects of in vivo treatment with an anti-PD-1, PD-L1, or PD-L2 monoclonal antibodies on the development of myocardial inflammation in C3H/He mice infected with Coxsackievirus B3. Third, to investigate the effects of anti-PD-1 monoclonal antibody treatment on the activation of the infiltrating cells, we examined the expression of interleukin (IL)-2, interferon (IFN)-γ, CD40 ligand (CD40L), Fas ligand (FasL), and perforin as activation markers in mouse hearts by a semiquantitative PCR method. Results: PD-L1 was markedly induced on cardiac myocytes with acute myocarditis. In vivo anti-PD-1 or -PD-L1 blocking monoclonal antibody treatment increased the myocardial inflammation whereas anti-PD-1 stimulating monoclonal antibody treatment decreased the myocardial inflammation, and anti-PD-L2 monoclonal antibody treatment had no effect. Anti-PD-1 monoclonal antibody treatment significantly increased the expression of IFN-γ, FasL, CD40L, perforin, and Coxsackievirus B3 genomes in myocardial tissue. Conclusion: Our findings strongly suggest that the PD-1/PD-L1 pathway played a pivotal role in suppressing myocardial inflammation and raise the possibility of immunotherapy by stimulating the PD-1/PD-L1 pathway to prevent myocardial damage in viral myocarditis.

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“…'3 Using immunofluorescent techniques, Gorza et al 14 and Yazaki et al 15 have suggested that human atrial tissue can respond to hemodynamic loads, as might be seen with mitral valvular disease, by altering the distribution of its specific isomyosins.…”

mentioning

confidence: 99%

Myosin isoenzyme distribution in overloaded human atrial tissue.

Buttrick¹,

Malhotra²,

Brodman³

et al. 1986

Circulation

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Using nondenaturing polyacrylamide gel electrophoresis, we have identified two distinct myosin isoenzymes in human atrial tissue that correspond to the V1 and V3 isomyosins found in rat ventricular tissue. Normal left and right atrial appendages have approximately 50% V3. When the left atrium was exposed to hemodynamic overload secondary to mitral stenosis, the percent V3 increased to 77 + 10% (n = 10); exposure to hemodynamic overload secondary to mitral regurgitation caused an increase to 70 14% (n = 6). Changes in the isoenzyme pattern were seen in the right atria of patients with mitral stenosis and markedly elevated pulmonary arterial pressures compared with control subjects and patients with mitral stenosis without severe pulmonary hypertension. Several clinical variables were examined to determine which factors might influence isoenzyme expression. Age, sex, the presence of atrial fibrillation, and pulmonary capillary wedge pressure did not predict the isoenzyme pattern. However, patients with mitral valvular disease and only slightly enlarged left atria tended to have a higher percent V3 than those with massively enlarged atria. These data confirm that human atrial tissue, like rat ventricular tissue, can alter its isomyosin composition in response to a hemodynamic load. The data further suggest that the isoenzyme shift is an early adaptation to the imposed load. Circulation 74, No. 3, 477-483, 1986. EXPERIMENTAL STUDIES in many mammalian species have demonstrated that the biochemical constituents of the myocardium, especially the heavy chains of myosin, influence the mechanical performance of cardiac muscle1' 2 and that changes in expression of the various isomyosins mediate myocardial adaptations to imposed loads and/or hormonal stimuli.3'4 This is particularly apparent in rodents and other small animals. Several investigators have shown, for example, that the imposition of hypertension or aortic stenosis on rat ventricle shifts the normally V1 predominant isomyosin to V3, which is associated with reduced ATPase activity and with depressed mechanical properties. Conversely, the superimposition of physical training or hyperthyroidism increases the percentage of V1, the associated ATPase activities, and the velocity of contraction of the intact muscle.3 5-In human ventricular tissue, which is composed almost exclusively of an isomyosin homodimer with a From

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Distribution of myosin isozymes in human atrial and ventricular myocardium: comparison in normal and overloaded heart

Cited by 44 publications

References 0 publications

Expression of intercellular adhesion molecule-1 in murine hearts with acute myocarditis caused by coxsackievirus B3.

Expression of intercellular adhesion molecule-1 in murine hearts with acute myocarditis caused by coxsackievirus B3.

Roles of programmed death-1 (PD-1)/PD-1 ligands pathway in the development of murine acute myocarditis caused by coxsackievirus B3

Myosin isoenzyme distribution in overloaded human atrial tissue.

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