Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle

Parvalbumin (PV) is a soluble Ca++ binding protein which is particularly concentrated in fast muscles of rodents. We have developed a new protocol to fix frozen sections of muscle by formaldehyde vapor, which enabled us to immunochemically stain serial frozen sections for PV. Fiber types were define...

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Bibliographic Details
Published in:The journal of histochemistry and cytochemistry 1991-03, Vol.39 (3), p.355-361
Main Authors: Fuchtbauer, EM, Rowlerson, AM, Gotz, K, Friedrich, G, Mabuchi, K, Gergely, J, Jockusch, H
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cell structures and functions
Frozen Sections
Fundamental and applied biological sciences. Psychology
Humans
Immunohistochemistry
Mice
Mice, Inbred C57BL
Molecular and cellular biology
Muscles - metabolism
Myosins - metabolism
Parvalbumins - metabolism
Rats
Rats, Inbred Strains
Succinate Dehydrogenase - metabolism
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Description
Summary:Parvalbumin (PV) is a soluble Ca++ binding protein which is particularly concentrated in fast muscles of rodents. We have developed a new protocol to fix frozen sections of muscle by formaldehyde vapor, which enabled us to immunochemically stain serial frozen sections for PV. Fiber types were defined on the basis of myosin ATPase stability, and of isomyosins identified by a variety of antibodies because ATPase stability alone yielded ambiguous results in the mouse. Slow Type I fibers in mouse and rat were devoid of PV and had intermediate to high SDH levels. Fast fiber subtypes IIA, IIB, and IIX-like were defined in the mouse on the basis of the similarity of their myosin heavy chain immunoreactivity to these types in the rat. The soleus muscle was usually PV negative, but a small population of strongly PV-positive IIX-like fibers was present in the mouse. In mouse fast muscle, small diameter IIA fibers were PV negative with high SDH activity. In both mouse and rat, PV reactivities of IIB and IIX fibers were higher than those of IIA and I, whereas SDH levels of IIA, IIX, and I fibers were higher than those of IIB. Thus, PV content correlated with the type of myosin ATPase but not with SDH levels. The method described for immunocytochemistry of PV may be applicable to other highly soluble proteins.
ISSN:0022-1554
1551-5044
DOI:10.1177/39.3.1825216