Inositide signaling in the nucleus: from physiology to pathology. (Articolo in rivista)

Type
Label
  • Inositide signaling in the nucleus: from physiology to pathology. (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Alternative label
  • Cocco L, Follo MY, Faenza I, Billi AM, Ramazzotti G, Martelli AM, Manzoli L, Weber G. (2010)
    Inositide signaling in the nucleus: from physiology to pathology.
    in Advances in enzyme regulation
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cocco L, Follo MY, Faenza I, Billi AM, Ramazzotti G, Martelli AM, Manzoli L, Weber G. (literal)
Pagina inizio
  • 2 (literal)
Pagina fine
  • 11 (literal)
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  • 20 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Cellular Signaling Laboratory Department of Anatomical Sciences, University of Bologna, via Irnerio 48, 40126 Bologna, Italy; IGM-CNR, Bologna Unit, c/o IOR, Bologna, Italy; School of Pharmacy, University of Bologna, Bologna, Italy; Indiana University School of Medicine, Indianapolis, IN, USA. (literal)
Titolo
  • Inositide signaling in the nucleus: from physiology to pathology. (literal)
Abstract
  • Phospholipids in chromosomes have been detected firstly by the work of La Cour et al. (1958). Later, Manzoli and colleagues demonstrated that addition of phospholipids to purified nuclei could influence in vitro transcription (Manzoli et al., 1978). The same group demonstrated that negatively charged lipids led to chromatin decondensation, while positive charged lipids had the opposite effect. In 1987, the first demonstration came from Cocco laboratory that a nuclear PI metabolism exists and it is regulated during erithroid cells differentiation (Cocco et al., 1987). Since then, progress has been made on the regulation of nuclear phosphoinositides (PI), as well as their role in cellular functions, i.e. growth and differentiation. Nevertheless, much still needs to be understood about the function, regulation and physical properties of this nuclear component. For example, while it is clear that these PIs are not part of the nuclear envelope but they reside within the nuclear domains, the physicochemical form of nuclear lipids still needs to be clarified (Irvine, 2006. Inositol lipid signaling molecules are essential components of the extremely complicated, multistep process that allowsone extracellular signal to be transduced inside the cell, to the nucleus. In the nuclear compartment, lipid second messengers elicit reactions that regulate gene transcription, DNA replication or repair, and DNA cleavage, eventually resulting in cellular differentiation, proliferation, apoptosis and other cell functions. Inositol-containing phospholipids are the most intensively studied lipid second messengers. Albeit most of the research on signal transduction pathways based on PI has been devoted to phenomena that take place at the cell periphery and plasma membrane, it has become clear that the nuclear PI cycle is regulated in a totally independent manner from that at the plasma membrane level. This suggests that nuclear inositol lipids themselves can modulate nuclear processes, as important as transcription and pre-mRNA splicing, growth, proliferation, cell cycle regulation and differentiation. Phosphatidylinositol(4,5)bisphosphate (PIP2) is a key lipid molecule in the PI cycle. It is the substrate of enzymes involved in signal transduction, such as phosphatidylinositol-specific phospholipase C (PI-PLC) and phosphoinositide 30-OH kinase (PI3K), thus producing the second messengers diacylglycerol (DAG), inositol trisphosphate (IP3) and phosphatidylinositol(3,4,5)trisphosphate (PIP3). PIP2 has also been shown to be directly involved in chromatin remodeling, by binding to proteins such as histone H1 and the Brahma-related gene associated factor (BAF) complex (Yu et al., 1998; Zhao et al., 1998). This double function of PIP2 in the nucleus, both as substrate for second messenger generation and as chromatin remodeling element, adds further emphasis to the importance of the enzymes responsible for nuclear PIP2 metabolism. In this review we shall focus to the nuclear PI-PLC b1 Fig. 1and namely, we shall review the most updated literature on PI-PLC b1 and its role in haematological malignancies, but it should be kept in mind that also others PI-PLCs isoform are present in the nucleus with some still undefined roles (Cocco et al., 2009). (literal)
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