Related Experiment Video
Updated: May 5, 2026

Mechanisms Underlying Gut Hormone Secretion Using the Isolated Perfused Rat Small Intestine
Published on: February 26, 2019
Ontogenic regulation of phospholipase C-gamma 1 activity and expression in the rat small intestine
1Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee.
Insights
During weaning, rat intestinal phospholipase C-gamma 1 (PLC gamma 1) expression and activity increase, showing age-dependent regulation by epidermal growth factor (EGF). This study demonstrates in vivo EGF-dependent PLC gamma 1 tyrosine phosphorylation.
Area of Science:
- Developmental biology
- Molecular biology
- Gastroenterology
Background:
- The postnatal rat small intestine undergoes significant developmental changes during weaning.
- Phospholipase C-gamma 1 (PLC gamma 1) is a key enzyme in growth and development pathways, acting as a substrate for the epidermal growth factor receptor (EGFR).
Purpose of the Study:
- To investigate developmental changes in intestinal PLC gamma 1 expression, catalytic activity, and its regulation by growth factors.
- To define the role of PLC gamma 1 in intestinal development during the weaning period.
Main Methods:
- Immunodetection was employed to assess the expression and tyrosine phosphorylation of PLC gamma 1, EGFR, PI 3-kinase, GAP, and SHC in postnatal rat intestines.
- Comparative analysis was performed between suckling, weanling, and adult animals.
Main Results:
- Both the catalytic activity and expression of PLC gamma 1 significantly increased in the rat intestine during weaning.
- Epidermal growth factor (EGF) stimulation led to increased PLC gamma 1 activity and tyrosine phosphorylation in weanling animals, but not in suckling animals.
- Expression of EGFR and SHC was elevated in weanling rats compared to suckling and adult rats.
Conclusions:
- Intestinal PLC gamma 1 expression and catalytic activity peak during the weaning period in rats.
- EGF-dependent regulation of PLC gamma 1 tyrosine phosphorylation and activity is modulated by age.
- This study provides the first in vivo evidence of EGF-dependent PLC gamma 1 tyrosine phosphorylation in normal animal tissue.
Background/Aims:
The postnatal rat small intestine undergoes major morphological, biochemical, and physiological changes during weaning. Phospholipase C-gamma 1 (PLC gamma 1), a tyrosine kinase substrate of the epidermal growth factor receptor (EGFR) hydrolyzes phosphatidylinositol-4,5-bisphosphate to products that may serve as mediators of growth and development. The aim of this study was to define developmental changes in intestinal PLC gamma 1 expression, catalytic activity, and growth factor regulation of PLC gamma 1.
Methods:
Immunodetection was used to compare the expression and tyrosine phosphorylation state of PLC gamma 1, EGFR, phosphatidylinositol 3-kinase (PI 3-kinase), ras guanosine triphosphatase activating protein (GAP), and src homologous collagen-like protein (SHC) in the postnatal rat intestine.
Results:
The catalytic activity and expression of PLC gamma 1 markedly increased during weaning. Significant EGF-induced increases in the activity and tyrosine phosphorylation of PLC gamma 1 occurred in weanling but not suckling animals. EGFR and SHC expression were increased in weanling compared with suckling and adult animals; however, differences in expression of PI 3-kinase and GAP did not occur during weaning.
Conclusions:
The expression and catalytic activity of rat intestinal PLC gamma 1 are greatest during weaning. A functional consequence is the age-dependent modulation of EGF regulation of PLC gamma 1 tyrosine phosphorylation state and catalytic activity. This is the first in vivo demonstration of EGF-dependent tyrosine phosphorylation of PLC gamma 1 in normal animal tissue.
More Related Videos
Related Concept Videos
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Amplifying Signals via Second Messengers
Amplifying Signals via Enzymatic Cascade
GPCRs Regulate Adenylyl Cylase Activity
IP3/DAG Signaling Pathway
Feedback Regulation of Calcium Concentration
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...

