Role of phospholipase C in cell invasion and metastasis
Phospholipases are enzymes that use phospholipids as substrate and are classified in three major classes A, C and D based on the reaction they catalyse. Phosphatidylinositol-specific Phospholipase C enzymes utilize phosphatidylinositol 4,5-bisphosphate as substrate and cleave the bond between the gl...
| Main Authors: | , , |
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| Format: | Journal Article |
| Published: |
2013
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| Online Access: | http://hdl.handle.net/20.500.11937/38308 |
| _version_ | 1848755285148041216 |
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| author | Lattanzio, R. Piantelli, M. Falasca, Marco |
| author_facet | Lattanzio, R. Piantelli, M. Falasca, Marco |
| author_sort | Lattanzio, R. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Phospholipases are enzymes that use phospholipids as substrate and are classified in three major classes A, C and D based on the reaction they catalyse. Phosphatidylinositol-specific Phospholipase C enzymes utilize phosphatidylinositol 4,5-bisphosphate as substrate and cleave the bond between the glycerol and the phosphate to produce important second messenger such as inositol trisphosphate and diacylglycerol. The Phospholipase C members are the most well-known phospholipases for their role in lipid signalling and cell proliferation and comprise 13 isoforms classified in 6 distinct sub-families. In particular, signalling activated by Phospholipase C γ, mostly activated by receptor and non-receptor tyrosine kinases, is well characterized in different cell systems. Increasing evidence suggest that Phospholipase C γ plays a key role in cell migration and invasion. Because of its role in cell growth and invasion, aberrant Phospholipase C γ signalling can contribute to carcinogenesis. A major challenge facing investigators who seek to target Phospholipase C γ directly is the fact that it is considered an “undruggable” protein. Indeed, isoform specificity and toxicity represents a big hurdle in the development of Phospholipase C γ small molecule inhibitors. Therefore, a future development in the field could be the identification of interacting partners as therapeutic targets that could be more druggable than Phospholipase C γ. |
| first_indexed | 2025-11-14T08:53:52Z |
| format | Journal Article |
| id | curtin-20.500.11937-38308 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T08:53:52Z |
| publishDate | 2013 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-383082017-09-13T14:10:12Z Role of phospholipase C in cell invasion and metastasis Lattanzio, R. Piantelli, M. Falasca, Marco Phospholipases are enzymes that use phospholipids as substrate and are classified in three major classes A, C and D based on the reaction they catalyse. Phosphatidylinositol-specific Phospholipase C enzymes utilize phosphatidylinositol 4,5-bisphosphate as substrate and cleave the bond between the glycerol and the phosphate to produce important second messenger such as inositol trisphosphate and diacylglycerol. The Phospholipase C members are the most well-known phospholipases for their role in lipid signalling and cell proliferation and comprise 13 isoforms classified in 6 distinct sub-families. In particular, signalling activated by Phospholipase C γ, mostly activated by receptor and non-receptor tyrosine kinases, is well characterized in different cell systems. Increasing evidence suggest that Phospholipase C γ plays a key role in cell migration and invasion. Because of its role in cell growth and invasion, aberrant Phospholipase C γ signalling can contribute to carcinogenesis. A major challenge facing investigators who seek to target Phospholipase C γ directly is the fact that it is considered an “undruggable” protein. Indeed, isoform specificity and toxicity represents a big hurdle in the development of Phospholipase C γ small molecule inhibitors. Therefore, a future development in the field could be the identification of interacting partners as therapeutic targets that could be more druggable than Phospholipase C γ. 2013 Journal Article http://hdl.handle.net/20.500.11937/38308 10.1016/j.jbior.2013.07.006 restricted |
| spellingShingle | Lattanzio, R. Piantelli, M. Falasca, Marco Role of phospholipase C in cell invasion and metastasis |
| title | Role of phospholipase C in cell invasion and metastasis |
| title_full | Role of phospholipase C in cell invasion and metastasis |
| title_fullStr | Role of phospholipase C in cell invasion and metastasis |
| title_full_unstemmed | Role of phospholipase C in cell invasion and metastasis |
| title_short | Role of phospholipase C in cell invasion and metastasis |
| title_sort | role of phospholipase c in cell invasion and metastasis |
| url | http://hdl.handle.net/20.500.11937/38308 |