Essential role of the tyrosine kinase substrate phospholipase C-γ1 in mammalian growth and development

Qun Sheng Ji; Glenn E. Winnier; Kevin D. Niswender; Debra Horstman; Ron Wisdom; Mark A. Magnuson; Graham Carpenter

doi:10.1073/pnas.94.7.2999

Essential role of the tyrosine kinase substrate phospholipase C-γ1 in mammalian growth and development

Qun Sheng Ji, Glenn E. Winnier, Kevin D. Niswender, Debra Horstman, Ron Wisdom, Mark A. Magnuson, Graham Carpenter

Houston Methodist

Research output: Contribution to journal › Article › peer-review

225 Scopus citations

Abstract

The activation of many tyrosine kinases leads to the phosphorylation and activation of phospholipase C-γ1 (PLC-γ1). To examine the biological function of this protein, homologous recombination has been used to selectively disrupt the Plcg1 gene in mice. Homozygous disruption of Plcg1 results in embryonic lethality at approximately embryonic day (E) 9.0. Histological analysis indicates that Plcg1 (-/-) embryos appear normal at E 8.5 but fail to continue normal development and growth beyond E 8.5-E9.0. These results clearly demonstrate that PLC-γ1 with, by inference, its capacity to mobilize second messenger molecules is an essential signal transducing molecule whose absence is not compensated by other signaling pathways or other genes encoding PLC isozymes.

Original language	English (US)
Pages (from-to)	2999-3003
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	94
Issue number	7
DOIs	https://doi.org/10.1073/pnas.94.7.2999
State	Published - Apr 1 1997

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title = "Essential role of the tyrosine kinase substrate phospholipase C-γ1 in mammalian growth and development",

abstract = "The activation of many tyrosine kinases leads to the phosphorylation and activation of phospholipase C-γ1 (PLC-γ1). To examine the biological function of this protein, homologous recombination has been used to selectively disrupt the Plcg1 gene in mice. Homozygous disruption of Plcg1 results in embryonic lethality at approximately embryonic day (E) 9.0. Histological analysis indicates that Plcg1 (-/-) embryos appear normal at E 8.5 but fail to continue normal development and growth beyond E 8.5-E9.0. These results clearly demonstrate that PLC-γ1 with, by inference, its capacity to mobilize second messenger molecules is an essential signal transducing molecule whose absence is not compensated by other signaling pathways or other genes encoding PLC isozymes.",

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T1 - Essential role of the tyrosine kinase substrate phospholipase C-γ1 in mammalian growth and development

AU - Ji, Qun Sheng

AU - Winnier, Glenn E.

AU - Niswender, Kevin D.

AU - Horstman, Debra

AU - Wisdom, Ron

AU - Magnuson, Mark A.

AU - Carpenter, Graham

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AB - The activation of many tyrosine kinases leads to the phosphorylation and activation of phospholipase C-γ1 (PLC-γ1). To examine the biological function of this protein, homologous recombination has been used to selectively disrupt the Plcg1 gene in mice. Homozygous disruption of Plcg1 results in embryonic lethality at approximately embryonic day (E) 9.0. Histological analysis indicates that Plcg1 (-/-) embryos appear normal at E 8.5 but fail to continue normal development and growth beyond E 8.5-E9.0. These results clearly demonstrate that PLC-γ1 with, by inference, its capacity to mobilize second messenger molecules is an essential signal transducing molecule whose absence is not compensated by other signaling pathways or other genes encoding PLC isozymes.

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Essential role of the tyrosine kinase substrate phospholipase C-γ1 in mammalian growth and development

Abstract

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