Abstract |
Osteoarthritis (OA) and rheumatoid arthritis (RA) are common joint diseases that can lead to destruction of cartilage and structural changes in the subchondral bone. In this study we show by western blot and quantitative immunocytochemistry that nuclear phospholipase C beta(1) ( PLC beta(1)) and phosphatidylinositol 4,5-bisphosphate (PIP(2)), two key elements of the polyphosphoinositide signal transduction system that regulate different cellular processes, increase in primary osteoblast cultures of RA patients when compared with post-traumatic after fall (PT) patients, whilst those of OA are not significantly affected. Moreover, we demonstrate that these alterations could be induced in PT osteoblasts by proinflammatory cytokines IL-1 beta and TNF-alpha. This suggests that proinflammatory cytokines, highly produced by RA infiltrating mononuclear cells, can modulate the nuclear polyphosphoinositide signalling pathway of the osteoblasts involved in bone remodelling.
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Authors | Nicoletta Zini, Gina Lisignoli, Liliana Solimando, Alberto Bavelloni, Francesco Grassi, Lia Guidotti, Carmela Trimarchi, Andrea Facchini, Nadir Mario Maraldi |
Journal | Histochemistry and cell biology
(Histochem Cell Biol)
Vol. 120
Issue 3
Pg. 243-50
(Sep 2003)
ISSN: 0948-6143 [Print] Germany |
PMID | 12915944
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Interleukin-1
- Isoenzymes
- Nerve Tissue Proteins
- Tumor Necrosis Factor-alpha
- synaptojanin
- Phosphoric Monoester Hydrolases
- Type C Phospholipases
- PLCB1 protein, human
- Phospholipase C beta
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Topics |
- Arthritis, Rheumatoid
(enzymology)
- Cell Nucleus
(enzymology)
- Cells, Cultured
- Female
- Humans
- Immunoblotting
- Interleukin-1
(pharmacology)
- Isoenzymes
(metabolism)
- Leg Bones
(enzymology)
- Male
- Middle Aged
- Nerve Tissue Proteins
(metabolism)
- Osteoarthritis
(enzymology)
- Osteoblasts
(enzymology)
- Phospholipase C beta
- Phosphoric Monoester Hydrolases
(metabolism)
- Tumor Necrosis Factor-alpha
(pharmacology)
- Type C Phospholipases
(metabolism)
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