Disease relevance of LOC396903

• The previously described animal model of autoimmune myocarditis induced by immunization of Lewis rats with cardiac myosin was investigated pathologically, ultrastructurally and immunohistologically [1].
• We recently showed that a shift ( approximately 44%) in cardiac myosin isozyme from V3 to V1 occurs in the hearts of malignant hyperthermia (MH)-susceptible pigs and may be important in the disease [2].
• Single-headed myosin was prepared by digestion of porcine aorta smooth muscle myosin with Staphylococcus aureus V8 protease in the presence of actin [3].

High impact information on LOC396903

• Single-headed myosin VI S1 constructs take nonprocessive 12 nm steps, suggesting that most of the processive step is covered by a diffusive search for an actin binding site [4].
• Changes in the [Ca2+]i sensitivity of myosin light-chain phosphorylation are not an artifact of the [Ca2+]i measurement technique [5].
• Depolarization decreases the [Ca2+]i sensitivity of myosin light-chain kinase in arterial smooth muscle: comparison of aequorin and fura 2 [Ca2+]i estimates [5].
• The [Ca2+]i sensitivity of myosin light-chain kinase extracted from KCl depolarized tissues was lower than the [Ca2+]i sensitivity of myosin light-chain kinase extracted from unstimulated or histamine stimulated tissues [5].
• When LLC-PK1 cells were injected with two monoclonal antibodies against pig brain nonmuscle myosin, in concentrations yielding a 1:1 ratio of antibody to myosin, neither microvillar number nor length was affected [6].

Biological context of LOC396903

• The sliding velocity of actin filaments, which is an index of the motile activity of myosin, also correlated with the resting heart rate but the relationship was not proportional [7].
• The SA channels reported here could affect the motile response by altering the membrane potential or by allowing the entry of free Ca2+ which could lead to a change in OHC length through the interaction of actin and myosin [8].
• Modification of myosin light chain phosphorylation in sustained arterial muscle contraction by phorbol dibutyrate [9].

Anatomical context of LOC396903

• Synthetic peptides based on the sequence Lys11-Lys12-Arg13-Ala-Ala-Arg16-Ala-Thr-Ser19 -Asn-Val21-Phe22-Ala of the chicken gizzard myosin light chain were tested as inhibitors of pig carotid-artery myosin light-chain kinase [10].
• Involvement of rho in GTP gamma S-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity [11].
• An antigen-specific T cell proliferation assay was performed with CD4-positive T cells isolated from control rats immunized with cardiac myosin [12].
• Muscle power output, ATPase rate, and myosin filament density also have the same dependence on muscle cell length: increased by 35.4% +/- 6.7, 34.6% +/- 3.4, and 35.6% +/- 10.6, respectively, for a 50% increase in cell length [13].
• Fast fibres in a large animal: fibre types, contractile properties and myosin expression in pig skeletal muscles [14].

Associations of LOC396903 with chemical compounds

• Histamine stimulation of swine arterial smooth muscle is associated with a high [Ca2+]i sensitivity for increases in myosin light-chain phosphorylation [5].
• Both Y27632 and PD98059 inhibited myosin light chain phosphorylation [15].
• The two heads of porcine aorta smooth muscle myosin can be cross-linked by a disulfide bridge between the two 17-kDa essential light chains with 5,5'-dithiobis(2-nitrobenzoic acid) [Katoh, T., Tanahashi, K., Hasegawa, Y. & Morita, F. (1995) Eur. J. Biochem. 227, 459-465] [16].
• Moreover, myosin light chain II and triose phosphate isomerase I were also found to correlate significantly to shear force [17].
• Unlike EMD 53998, levosimendan did not increase myosin ATPase activity, indicating that it did not increase the cycling rate of myosinactin crossbridges [18].

Other interactions of LOC396903

• Ca2+, calmodulin-dependent myosin light chain phosphorylation is generally considered to be an important regulatory mechanism of smooth muscle contraction [19].

Analytical, diagnostic and therapeutic context of LOC396903

• Additionally, we showed by Western blot that the CCR1 antagonist suppressed ERK1/2 and JNK activities in T cells stimulated with myosin and that IL-2 reversed this suppression [12].
• The filaments of the cross-linked myosin sample were visualized by electron microscopy and appeared morphologically similar to those of uncross-linked myosin [16].
• Below 0.2 M NaCl, the single-headed myosin showed a decrease in Ca2+-ATPase activity and an increase in the elution time on gel filtration HPLC in a phosphorylation-dependent manner, indicating a phosphorylation-dependent conformational transition between the extended and folded forms [3].

References