IndraLab
Statements
sparser
"An involvement of mTORC2 in calcium regulation in muscle is also supported by the decrease in the phosphorylation of calmodulin 1 (CALM1) in Ric mKO muscle, since
calmodulins are calcium ion sensor proteins that transduce most of the calcium signalling to downstream protein kinases and phosphatases (Marcelo et al. 2016)."
rlimsp
"The availability of alternative substrates for AMPKK and CaMKIK allowed the unequivocal demonstration that AMP and Ca2+/calmodulin promote the activation of AMPK and Ca2+/calmodulin promote the activation of AMPK and CaMKI, respectively, via three independent mechanisms: 1) direct activation of AMPK and CaMKI, 2) activation of AMPKK and CaMKIK, and 3) by binding to AMPK and CaMKI, inducing exposure of their phosphorylation sites."
rlimsp
"The enzyme activation induced by the pH increase up to 8.2 does not affect the enzyme interaction with calmodulin [2.14 +/- 0.58 mol calmodulin per mol of (alpha beta gamma delta)]; Kd = (4.14 +/- 1.22).10(-8) M. However, the enzyme activation during its autocatalytic phosphorylation eliminates this effect practically completely."
rlimsp
"A magnetic dependence has been previously reported by others in an homologous system, CaM dependent myosin light chain phosphorylation, implying that there may be an underlying magnetic interaction that involves the initial Ca(2+)/CaM binding process common to both enzymatic pathways."
sparser
"Furthermore, CSC (25 microgram/ml) both increases the rate of transendothelial migration of vitamin D3-differentiated monocyte-like cells across the HUVEC monolayer by 200% and causes an approximately 10-fold increases in the phosphorylation of platelet endothelial CAM (PECAM-1), an adhesion molecule located at intercellular junctions and involved in endothelial cell-cell adhesion."
sparser
"All
reactions were monitored by thin layer chromatography (TLC) carried
out on either Merck silica gel plates (0.25 mm thick, 60F254) or Millipore
Silica gel aluminum sheets (60F254) and visualized by using UV (254
nm) or dyes such as KMnO 4 , p -anisaldehyde,
and CAM (Hannesian’s Stain)."
rlimsp
"Day and night forms of phosphoenolpyruvate carboxylase (EC 4.1.1.31) (PEPC) were extracted from leaves of the CAM plants Kalanchoe daigremontiana, K. tubiflora and K. blossfeldiana previously fed with [32P] labelled phosphate solution. A one-step immunochemical purification followed by SDS polyacrylamide gel electrophoresis and autoradiography showed that, in all species, the night form of the enzyme was phosphorylated and not the day form. Limited acid hydrolysis of the night form and two-dimensional separation identified predominantly labelled phosphoserine and phosphothreonine. In vitro addition of exogenous acid phosphatase (EC 3.1.3.2) to desalted night form-containing extracts resulted within 30 min in a shift in PEPC enzymic properties similar to the in vivo changes from night to day form. It is suggested that phosphorylation-dephosphorylation of the enzyme could be the primary in vivo process which might explain the observed rhythmicity of enzymic properties."
sparser
"The current understanding of the exact pathophysiological mechanism and how it links to the structural components of calmodulin structure is not clear, however, it is likely related to the large sarcoplasmic Ca 2 + release channel RyR2 sharing the same phenotypic expression.[ xref ] Proof of concept studies using knock-in animal models and human-induced pluripotent stem cells are missing and are another area of research.[ xref ] A recent study making use of nuclear magnetic resonance was able to provide insight into the particular structural effects of CALM1 p."
rlimsp
"Day and night forms of phosphoenolpyruvate carboxylase (EC 4.1.1.31) (PEPC) were extracted from leaves of the CAM plants Kalanchoe daigremontiana, K. tubiflora and K. blossfeldiana previously fed with [32P] labelled phosphate solution. A one-step immunochemical purification followed by SDS polyacrylamide gel electrophoresis and autoradiography showed that, in all species, the night form of the enzyme was phosphorylated and not the day form."