Transmural distribution of isomyosin in rabbit ventricle during maturation examined by immunofluorescence and staining for calcium-activated adenosine triphosphatase.
نویسندگان
چکیده
Mammalian ventricle contains two major isomyosins, V1 and V3, which differ in the primary structure of their heavy chains (HC alpha alpha and HC beta beta, respectively) and in their adenosine triphosphatase activity. The distribution of the HC alpha isomyosin in the left ventricle of the rabbit was followed as a function of age and transmural location. HC alpha was detected with a monoclonal antibody found to be specific for the hinge region of V1 myosin molecules when viewed in the electron microscope after low-angle rotary shadowing. Frozen sections were observed with indirect immunofluorescence developed to this anti-HC alpha hinge antibody. Serial sections were observed with the histochemical assay for calcium-activated myosin adenosine triphosphatase, using preincubation at various pH levels. Results show that all the ventricular myocytes in baby rabbits (2 weeks) are stained by the HC alpha-antibody from the epi- to endocardium. The isomyosin content of myocytes varies through the epi- to endocardium of the right ventricular wall of the adult (1-year-old) rabbit, with the HC alpha form predominating in the outer epicardial third of the wall and the lowest amount of HC alpha in the middle third of the wall. A mixture of stained and unstained myocytes is seen in the endo- and subendocardial regions. The spatial distribution of HC alpha in 4-month-old rabbits varies between that of the baby and adult. There is good agreement between myocyte classifications made by histochemical and antibody staining methods.(ABSTRACT TRUNCATED AT 250 WORDS)
منابع مشابه
Developmental changes in contractile protein adenosine 5'-triphosphatase in the rabbit heart.
This study was designed to investigate developmental changes in contractile protein adenosine 5'-triphosphatase in the rabbit heart. Myofibrils and myosin were isolated from ventricular muscles from the fetal, newborn, and adult rabbits. Actin and troponin-tropomyosin complex were isolated from the adult skeletal muscle. Myofibrillar (actomyosin) adenosine 5'-triphosphatase measured at low ioni...
متن کاملThe mode of inhibition by calcium of cell-membrane adenosine-triphosphatase activity.
1. The mechanism of the inhibition of Na(+)-plus-K(+)-activated adenosine triphosphatase by calcium was investigated with an enzyme preparation from rabbit kidney cortex and with membranes of human erythrocytes. 2. CaATP, rather than ionic Ca(2+), acts as a competitive inhibitor, competing with MgATP in the Na(+)-plus-K(+)-activated adenosine-triphosphatase reaction. 3. There appears to be no c...
متن کاملIsomyosin distribution in normal and pressure-overloaded rat ventricular myocardium. An immunohistochemical study.
We have used affinity-purified antibodies reacting with guinea pig soleus muscle and ventricular myosin heavy chains to analyze the distribution of specific isomyosin in the ventricular myocardium of normal and renal hypertensive rats. Immunofluorescent staining of cardiac tissue sections with the two antimyosins revealed striking variations in reactivity among ventricular muscle fibers, reacti...
متن کاملFiber types and myosin types in human atrial and ventricular myocardium. An anatomical description.
Hybridomas were prepared from mice immunized with myosin from the enlarged left ventricle of a 53-year-old female with an obstructive cardiomyopathy. The specificity of 15 monoclonal antibodies to myosin heavy chains was assessed by the reactivity of muscle extracts and of chymotryptic myosin fragments of different sizes with these antibodies, as determined by the immune replicate technique; so...
متن کاملStudies on myosin from red and white skeletal muscles of the rabbit. I. Adenosine triphosphatase activity.
Myosin obtained from red skeletal muscle of rabbit has a lower adenosine triphosphatase activity than myosin from white skeletal muscle. Structural differences between the two types of myosin are suggested by the higher apparent activation energy of the calcium-activated adenosine triphosphatase reaction catalyzed by red muscle myosin, by the higher rate of inactivation at pH 7.5 to 9.5, and by...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Circulation research
دوره 56 4 شماره
صفحات -
تاریخ انتشار 1985