Abstract

The normal cellular protein pp60 c-src is a tyrosine-specific protein kinase that is homologous to the transforming protein of Rous sarcoma virus (RSV) but its function is unknown. The expression of pp60 c-src in chick and human embryonic tissues was monitored by the immune complex protein kinase assay, Western transfer analysis, and immunocytochemical staining at the light microscope level. pp60 c-src kinase was expressed in the head and trunk regions of the chick embryo at all stages of development examined; however, expression increased significantly during the major period of organogenesis (Hamburger and Hamilton stages 21 to 32). Western transfer analysis showed that the amount of pp60 c-src protein increased in parallel with the increase in kinase activity. Highest levels of pp60 c-src kinase were present in the neural tube, brain, and heart of the stage 32 chick embryo. Lower levels of activity were found in eye, limb bud, and liver. Immunocytochemical staining of the neural tube region and heart of the chick confirmed the results of biochemical analysis and showed immunoreactive pp60 c-src distributed throughout the neural tube and heart. The distribution of pp60 c-src kinase in human fetal tissues was similar to that in the chick embryo; elevated levels of pp60 c-src kinase were present in cerebral cortex, spinal cord, and heart, but all other tissues examined expressed some pp60 c-src kinase. The results of our studies suggest that pp60 c-src plays a fundamental role in an aspect of cellular metabolism that is particularly important in electrogenic tissues.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.