beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
enzyme activity measured with the natural substrate 2-phospho-D-glycerate, conversion of reaction products determined by spectroscopy, kinetics of binding studies to tubulin by ELISA and surface plasmon resonance
enzyme activity measured with the natural substrate 2-phospho-D-glycerate, conversion of reaction products determined by spectroscopy, kinetics of binding studies to tubulin by ELISA and surface plasmon resonance
enzyme activity tested, kinetics of binding studies to tubulin estimated by ELISA and surface plasmon resonance, association of beta,beta enolase to microtubules in differentiating myotubes but not in myoblasts
enzyme activity tested, kinetics of binding studies to tubulin estimated by ELISA and surface plasmon resonance, association of beta,beta enolase to microtubules in differentiating myotubes but not in myoblasts
satellite cell differentiation, alpha,alpha-enolase highly expressed during early ontogenesis, concentration of alpha,alpha-enolase in skeletal muscle varies from 0.1 mM to 0.01 mM until differentiation, binding affinity to tubulin is about 0.2 microM, alpha,beta heteroassociation with tubulin in muscle under physiological conditions
alpha,beta heterodimer and beta,beta homodimer in striated muscle, interaction with tubulin during differentiation of muscle satellite cells but not in undifferentiated myoblasts, immobilized beta,beta-enolase interacts with tubulin in vitro
the embryonic alpha,alpha isoform remains distributed in many adult cell types, wheras a transition towards beta,beta-isoform and gamma,gamma-isoform occurs in striated muscle cells and neurons respectively
cytosolic fractions of myoblasts and myotubes, microtubule-association of alpha,alpha-enolase in undifferentiated myoblasts and in myotubes, also nuclear localization in myoblasts but not in myotubes determined, role of enolases in cytoskeletal dynamics during myoblast differentiation assumed
nuclear localization in myoblasts not detected, direct interaction with microtubules and tubulin during myoblast differentiation identified, role in cytoskeletal dynamics during myoblast differentiation assumed
enolase 1 and calreticulin siRNA reduce the [Ca2+]i levels, amounts of total TNF-alpha, and the release of TNF-alpha and leukotrienes, all of which are increased in the bone marrow-derived mast cells activated with antigen/antibody reaction
enolase 1 gene silencing by siRNA leading to reduced the mRNA and protein expressions of surface receptor Fc-RIalpha, surface molecules, such as c-kit, CD40, CD40 ligand and 373 VCAM-1, and also reduced granular tryptase in the culture periods, as well as expressions of enolase 1 and calreticulin. Enolase 1 or calreticulin siRNA transfected-bone marrow-derived mast cells remarkably reduce [Ca2+]i levels compared to wild-type bone marrow-derived mast cells. Both protein siRNA transfected-bone marrow-derived mast cells reduced [Ca2+]i levels more than by individual protein transfection, but does not show additive effect
Merkulova, T.; Lucas, M.; Jabet, C.; Lamande, N.; Rouzeau, J.D.; Gros, F.; Lazar, M.; Keller, A.
Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins