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    ABSTRACT: The cyclic AMP sensor, EPAC1, activates AP1-mediated transcription in HUVECs. Correspondingly, induction of the SOCS3 minimal promoter by EPAC1 requires a single AP1 site that constitutively binds phosphorylated (Ser63) c-Jun in DNA-pull-down assays. c-Jun (Ser63) becomes further phosphorylated following cyclic AMP stimulation and specific activation of protein kinase A (PKA), but not through selective activation of EPAC1. Moreover, despite a requirement for c-Jun for SOCS3 induction in fibroblasts, phospho-null c-Jun (Ser63/73Ala) had little effect on SOCS3 induction by cyclic AMP in HUVECs. AP1 activation and SOCS3 induction by EPAC1 in HUVECs therefore occur independently of c-Jun phosphorylation on Ser63.
    Full-text · Article · Mar 2014 · FEBS letters
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    ABSTRACT: Evidence is provided from studies on natural and artificial biofluids that the sequestration of amorphous calcium phosphate by peptides or proteins to form nanocluster complexes is of general importance in the control of physiological calcification. A naturally occurring mixture of osteopontin peptides was shown, by light and neutron scattering, to form calcium phosphate nanoclusters with a core-shell structure. In blood serum and stimulated saliva, an invariant calcium phosphate ion activity product was found which corresponds closely in form and magnitude to the ion activity product observed in solutions of these osteopontin nanoclusters. This suggests that types of nanocluster complexes are present in these biofluids as well as in milk. Precipitation of amorphous calcium phosphate from artificial blood serum, urine and saliva was determined as a function of pH and the concentration of osteopontin or casein phosphopeptides. The position of the boundary between stability and precipitation was found to agree quantitatively with the theory of nanocluster formation. Artificial biofluids were prepared that closely matched their natural counterparts in calcium and phosphate concentrations, pH, saturation, ionic strength and osmolality. Such fluids, stabilised by a low concentration of sequestering phosphopeptides, were found to be highly stable and may have a number of beneficial applications in medicine.
    Full-text · Article · Jan 2014 · Journal of Structural Biology
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    ABSTRACT: Over the past decade, confocal microscopy and the ever-expanding toolchest of fluorescent protein (xFP) markers and technologies have become routine methods for the biological laboratory. A common use of xFP fluorophores is in localizing proteins and the subcellular structures with which they associate, including analyzing their distribution and dynamics and the interactions of proteins in vivo. Additionally, a number of so-called optical highlighters have proven especially useful in analyzing the kinetics of these processes in pulse-chase studies of protein relocation(s) following an experimental challenge. Here we focus on exemplary methods in transformation and live-cell imaging in plant cells, with the expectation that researchers will find these and the accompanying resources useful as a starting point in developing their own expertise.
    No preview · Article · Jan 2014 · Methods in molecular biology (Clifton, N.J.)
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