Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle. 182 16

The presence of parvalbumin, a calcium-binding protein, has been correlated with the maturation of locomotor activity in developing striated muscle. In the present study, postnatal parvalbumin immunoreactivity is examined in the tibialis anterior, intercostal, diaphragm and intrinsic muscles of the tongue of the rat to gather a better understanding of the different developmental patterns. Parvalbumin immunoreactivity appears in the anterior tibialis muscle by day 4, and reaches an adult checkerboard pattern 2 days later. In contrast, parvalbumin immunoreactivity in the intrinsic muscles of the tongue, and in diaphragm and intercostal muscles, which are active near birth, does not appear until the 2nd week. Therefore, these features suggest that parvalbumin immunoreaction is not exclusively dependent on functional activity. In addition, the finding that differences in parvalbumin expression do not correlate in time with the differentiation of fiber types as judged by myosin ATPase activity, suggests that myosin and parvalbumin might be regulated by different mechanisms.
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PMID:Postnatal development of parvalbumin immunoreactivity in striated muscles of the rat. 781