Event Title

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.

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Apr 26th, 10:00 AM Apr 26th, 12:00 PM

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.