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Tyrosine phosphorylated proteins in different tissues during chick embryo development
1Department of Biology, University of California, San Diego, LaJolla 92093.
The Journal of Cell Biology
|May 1, 1988
Summary
Tyrosine phosphorylated proteins are abundant in embryonic chicken tissues but diminish in adults. These proteins, particularly at 120 and 70 kD, show structural similarities across various developing tissues.
Area of Science:
- Developmental Biology
- Molecular Biology
- Biochemistry
Background:
- Tyrosine phosphorylation is a critical regulatory mechanism in cellular processes.
- Understanding the role of tyrosine phosphorylated proteins during embryonic development is essential.
Purpose of the Study:
- To survey embryonic chicken tissues for tyrosine phosphorylated proteins.
- To characterize the presence, molecular mass, and structural relationships of these proteins during development.
Main Methods:
- Immunoblotting using a high-affinity polyclonal antibody specific for phosphotyrosyl residues.
- Analysis of protein extracts from various embryonic chicken tissues (7-21 days in ovo) and adult tissues.
- One-dimensional peptide mapping of specific protein bands.
Main Results:
- Tyrosine phosphorylated proteins were detected in all examined embryonic tissues but were significantly reduced in adult tissues.
- Major tyrosine phosphorylated proteins observed across tissues ranged from 35 to 220 kD, with common bands at 120, 70, 60, and 35 kD.
- Peptide mapping revealed structural similarities among 120 kD and 70 kD phosphotyrosine-containing proteins from different tissues.
Conclusions:
- Tyrosine protein kinases and their substrates play a significant role during embryonic development in chickens.
- The presence of related phosphotyrosine-containing proteins across diverse tissues suggests conserved functional roles.
- The developmental regulation of tyrosine phosphorylation highlights its importance in tissue differentiation and growth.