178,086 research outputs found
Pathophysiological role of TLQP-21: gastrointestinal and metabolic functions.
The present review summarizes recent findings on the metabolic and gastroenteric role of the VGF gene and a peptide derived by post-translational cleavage of the VGF pro-hormone, i.e. TLQP-21. The vgf gene is widely expressed through the central nervous system as well as in the peripheral nervous system, in myenteric plexus ganglia and also in the glandular portion of the stomach. A few VGF derived peptide have been shown to possess biological activity, among them TLQP-21 attracted particular interest following its identification within rat nervous system. In particular, recent studies from our and other groups implicated TLQP-21 in both the modulation of energy homeostasis, body weight regulation and neuroendocrine functions as well as in the central control of gut functions. Overall, findings available point to a role for TLQP-21 in negatively affecting the body energy balance
A NOVEL NEUROENDOCRINE GENE PRODUCT: SELECTIVE VGF8a GENE EXPRESSION AND IMMUNO-LOCALISATION OF THE VGF PROTEIN IN ENDOCRINE AND NEURONAL POPULATIONS
Application of ammonium phosphate to marble. Investigation of newly-formed calcium phosphates with synchrotron light and high lateral resolution FTIR microspectroscopy
Inorganic-mineral treatments exhibit great potentialities for the consolidation of stone materials due to their high compatibility with the substrate. Their reaction mechanism is based on the diffusion, inside weathered stone matrixes, of water soluble precursors that, reacting with the substrate, supply a crystal network able to reconnect detached grain boundaries. The newly-formed crystalline phases are stable and due to their low solubility provide a passivating action toward atmospheric agents even in acid environment. Diammonium hydrogen phosphate [DAP, (NH4)2HPO4] has been recently suggested for the treatment of sedimentary and metamorphic carbonatic decayed stones. The reaction of DAP with calcite of the substrate involves a pseudomorphic replacement and favours the growth of calcium phosphates inside the porosity. Preliminary studies (Matteini et al., 2013; Possenti et al., 2016) show that the reaction at room temperature is non-stoichiometric and induces the formation of hydroxyapatite [HAP, Ca5(PO4)3(OH)] (Ni & Ratner, 2003) and other metastable phases. In this pilot study we characterized the complex assemblages of calcium phosphates formed after DAP treatments on Carrara marble specimens with a multi-analytical approach (scanning electron microscopy, vibrational spectroscopies and powder X-ray diffraction). A set of quarried and thermally decayed samples were treated by poultice and capillarity using DAP solutions at different molarities. Ground-breaking techniques such as X-ray diffraction with synchrotron light in transmitting geometry and high lateral resolution FTIR microspectroscopy were employed to overcome some of the analytical limits of conventional approach, assessing the overall composition of main and trace phases as well as
their arrangement on the substrate. Preliminary findings show the formation of a shell-like layer around the calcite grains, composed by a mixture of crystalline and amorphous calcium phosphates; the formation of specific phases, their morphologies and the relative amount depend on the solution molarity and the treatment duration. Moreover, our data show a correlation between the kind of crystalline phase and its morphology and position within the shell structure.
Matteini, M., Colombo, C., Botticelli, G., Casati, M., Conti, C., Negrotti, R., Possenti, E., Realini M. (2013): Ammonium phosphates
to consolidate carbonatic stone materials: an inorganic-mineral treatment greatly promising. Proceedings of the Built Heritage
2013 Monitoring Conservation Management, 1278-1286.
Ni, M. & Ratner, B.D. (2003): Nacre surface transformation to hydroxyapatite in a phosphate buffer solution. Biomaterials, 24, 4323-
4331.
Possenti, E., Colombo, C., Bersani, D., Bertasa, M., Botteon, A., Conti, C., Lottici, P.P., Conti C. (2016): New insight on the
interaction of diammonium hydrogenphosphate conservation treatment with carbonatic substrates: a multi-analytical approach.
Microchem. J., 127, 79-86
Access to social and health services as a health opportunity. Effects of pandemic on older people
Hannah Arendt: la banalità del male e il mondo degli Eichmann
Contributo dedicato alla riflessione arendtiana su Adolf Eichmann come figura della "mancanza di pensiero" (thoughtlessness)
Cloning, structural organization analysis, and chromosomal assignment of the human gene for the neurosecretory protein Vgf
The Vgf gene was originally identified as a 2.7-kb cDNA fragment isolated from nerve growth factor-treated PC12 cells by differential display against PC12 cells. It is transcribed solely in subpopulations of neuroendocrine cells in vivo and it is induced by neurotrophins in target cells in vitro. The single-copy human VGF gene was isolated from a genomic library. The gene spans approximately 6 kb and contains two exons. The entire VGF protein is encoded by exon 2, while exon 1 contains only 5'-untranslated sequence. The structural organization of the human gene is similar to that described for the rat Vgf gene (S. R. J. Salton et al., 1991, Mol. Cell. Biol. 11: 2335-2349) and both the translated and the untranslated regions show a high degree of sequence homology to the rat gene. Northern blot analysis revealed a single transcript of approximately 2.7 kb that was detected only in mRNA preparations from brain. The gene was assigned to chromosome 7q22 by fluorescence in situ hybridization
Cloning, structural organization analysis, and chromosomal assignment of the human gene for the neurosecretory protein VGF
The Vgf gene was originally identified as a 2.7-kb cDNA fragment isolated from nerve growth factor-treated PC12 cells by differential display against PC12 cells. It is transcribed solely in subpopulations of neuroendocrine cells in vivo and it is induced by neurotrophins in target cells in vitro. The single-copy human VGF gene was isolated from a genomic library. The gene spans approximately 6 kb and contains two exons. The entire VGF protein is encoded by exon 2, while exon 1 contains only 5'-untranslated sequence. The structural organization of the human gene is similar to that described for the rat Vgf gene (S. R. J. Salton et al., 1991, Mol. Cell. Biol. 11: 2335-2349) and both the translated and the untranslated regions show a high degree of sequence homology to the rat gene. Northern blot analysis revealed a single transcript of approximately 2.7 kb that was detected only in mRNA preparations from brain. The gene was assigned to chromosome 7q22 by fluorescence in situ hybridization
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