Morphological Characterization of Transgenic Murine Myocardium
Location
CSU 255
Start Date
26-4-2005 10:00 AM
End Date
26-4-2005 12:00 PM
Student's Major
Biological Sciences
Student's College
Science, Engineering and Technology
Mentor's Name
Marilyn C. Hart
Mentor's Department
Biological Sciences
Mentor's College
Science, Engineering and Technology
Description
Capping protein (CP) is a heterodimer made up of both alpha and beta subunits. In striated muscle, CP binds to the barbed end of the actin filament at the Z-line, directing and maintaining the proper organization of the thin filament in the sarcomere. Vertebrates have three alpha (ctl, a2, a3) and three beta isoforms (pi, p2, p3). In previous studies, transgenic mice were generated that replace the pi isoform of CP (the specific isoform of the sarcomere) with the p2 isoform of CP (the nonsarcomeric isoform) using the cardiac-specific promoter of the a-myosin heavy chain (a-MyHC) gene. The purpose of my research is to characterize the structural abnormalities in transgenic murine myocardium expressing forms of CP defective in attaching thin filaments to Z lines. Transgenic and wild-type mice, approximately one year old, were sacrificed, heart to body weight ratios determined and gross cardiac morphology assessed. The hearts were fixed in 10% buffered formaldehyde, dehydrated thru a graded series of ethanol washes and embedded in paraffin. Thin sections of the paraffin embedded tissue were prepared using a microtome and collected onto gelatin coated slides. The tissue sections were stained with hematoxylin and eosin, visualized by transmission brightfield microscopy and the digitized images captured using a cooled ccd camera and image acquisition software. Preliminary results will be presented.
Morphological Characterization of Transgenic Murine Myocardium
CSU 255
Capping protein (CP) is a heterodimer made up of both alpha and beta subunits. In striated muscle, CP binds to the barbed end of the actin filament at the Z-line, directing and maintaining the proper organization of the thin filament in the sarcomere. Vertebrates have three alpha (ctl, a2, a3) and three beta isoforms (pi, p2, p3). In previous studies, transgenic mice were generated that replace the pi isoform of CP (the specific isoform of the sarcomere) with the p2 isoform of CP (the nonsarcomeric isoform) using the cardiac-specific promoter of the a-myosin heavy chain (a-MyHC) gene. The purpose of my research is to characterize the structural abnormalities in transgenic murine myocardium expressing forms of CP defective in attaching thin filaments to Z lines. Transgenic and wild-type mice, approximately one year old, were sacrificed, heart to body weight ratios determined and gross cardiac morphology assessed. The hearts were fixed in 10% buffered formaldehyde, dehydrated thru a graded series of ethanol washes and embedded in paraffin. Thin sections of the paraffin embedded tissue were prepared using a microtome and collected onto gelatin coated slides. The tissue sections were stained with hematoxylin and eosin, visualized by transmission brightfield microscopy and the digitized images captured using a cooled ccd camera and image acquisition software. Preliminary results will be presented.
