Publications by authors named "Veronica Drudi-Metalli"

A 'locally acting' IGF1 (insulin-like growth factor 1) isoform has been recently identified in the skeletal muscle and neural tissues where it accelerates injury repair. No information exist on the expression and function of IGF1 isoforms in the liver. We investigated IGF1 isoforms in rat hepatocytes and cholangiocytes and evaluated their involvement in cell proliferation or damage induced by experimental cholestasis (bile duct ligation, BDL) or hydrophobic bile salts.

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Article Synopsis
  • The study examined how the growth hormone (GH) and insulin-like growth factor 1 (IGF1) influence the growth of cholangiocytes (cells in bile ducts) in rat livers.
  • The research showed that these cells express various receptors related to GH and IGF1, and after bile duct ligation (BDL), their proliferation increases along with higher IGF1 secretion.
  • Results indicated that GH triggers IGF1 production, which in turn promotes cholangiocyte growth through specific signaling pathways, suggesting that these cells are significantly affected by the GH/IGF1 axis in the liver.
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Background & Aims: We evaluated the expression of neurotrophins in rat cholangiocytes and the role and mechanisms by which nerve growth factor (NGF) modulates cholangiocyte proliferation.

Methods: The expression of neurotrophins and their receptors was investigated by immunohistochemistry in liver sections and reverse-transcription polymerase chain reaction and immunoblots in isolated cholangiocytes. In vitro, the effect of NGF on cholangiocyte proliferation and signal transduction was investigated by immunoblotting for proliferating cell nuclear antigen, phosphorylated AKT (p-AKT), phosphorylated extracellular signal-regulated kinase 1/2 (p-ERK1/2), phosphorylated c-jun-N-terminal kinase, and phosphorylated p38.

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The aim of this study was to explore the intracellular signaling pathways involved in the stimulatory effects of estrogens on cholangiocyte proliferation. We investigated the tyrosine kinase-receptor pathway by evaluating the protein expression of total and phosphorylated mitogen-activated protein kinase (MAPK) isoform p44/p42 (e.g.

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