Morphometric and autoradiographic study of developing ventricular and atrial myocardium in fetal rats.

P Anversa, L Vitali-Mazza, AV Loud - Laboratory investigation; a …, 1975 - europepmc.org
P Anversa, L Vitali-Mazza, AV Loud
Laboratory investigation; a journal of technical methods and pathology, 1975europepmc.org
The ventricular and atrial myocardia of 19-to 21-day-old rat fetuses have been studied by
electron microscopic morphometry and quantitative autoradiography following the injection
of 3H-leucine. The myocytes in both these regions contain numerous myofibrils located
predominantly near the sarcolemma and oriented parallel to each other and to the long axis
of the cell. The width of myofibrils at this stage of development is 0.428+/-0.240 mum. in the
ventricle and 0.365+/-0.185 mum. in the atrium. The volume fractions of myofibrils …
The ventricular and atrial myocardia of 19-to 21-day-old rat fetuses have been studied by electron microscopic morphometry and quantitative autoradiography following the injection of 3H-leucine. The myocytes in both these regions contain numerous myofibrils located predominantly near the sarcolemma and oriented parallel to each other and to the long axis of the cell. The width of myofibrils at this stage of development is 0.428+/-0.240 mum. in the ventricle and 0.365+/-0.185 mum. in the atrium. The volume fractions of myofibrils, mitochondria, smooth endoplasmic reticulum, sarcoplasmic matrix, and sarcolemma in ventricular myocytes are nearly equal to the corresponding fractions in atrial cells. A similarity between ventricular and atrial myocytes was also found in the distribution of newly synthesized proteins as indicated autoradiographically by the concentration of grains over various sarcoplasmic structures. In both tissues the concentration of grains was consistently above average over the sarcolemma, smooth endoplasmic reticulum, and myofibrils; average over the mitochondria; and below average in association with the sarcoplasmic matrix. The specificity of this autoradiographic procedure for labeled amino acids actually incorporated into protein was tested biochemically, and it was found that glutaraldehyde-paraformaldehyde fixation leads to a negligible contamination with non-specifically bound leucine. It is suggested that the high concentration of protein labeling near the sarcolemma is related to the imminent development of the T-system and its associated channels of sarcoplasmic reticulum.
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