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AMP deaminase histochemical activity and immunofluorescent isozyme localization in rat skeletal muscleThe cellular distribution of AMP deaminase (AMPda) isozymes was documented for rat soleus and plantaris muscles, utilizing immunofluorescence microscopy and immunoprecipitation methods. AMPda is a ubiquitous enzyme existing as three distinct isozymes, A, B and C, which were initially purified from skeletal muscle, liver (and kidney), and heart, respectively. AMPda-A is primarily concentrated subsarcolemmally and intermyofibrillarly within muscle cells, while isozymes B and C are concentrated within non-myofiber elements of muscle tissue. AMPda-B is principally associated with connective tissues surrounding neural elements and the muscle spindle capsule, and AMPda-C is predominantly associated with circulatory elements, such as arterial and venous walls, capillary endothelium, and red blood cells. These specific localizations, combined with documented differences in kinetic properties, suggest multiple functional roles for the AMPda isozymes or temporal segregation of similar AMPda functions. Linkage of the AMPda substrate with adenosine production pathways at the AMP level and the localization of isozyme-C in vascular tissue suggest a regulatory role in the microcirculation.
Document ID
Document Type
Reprint (Version printed in journal)
Thompson, J. L.
(Medical College of Wisconsin Milwaukee)
Sabina, R. L.
Ogasawara, N.
Riley, D. A.
Date Acquired
August 22, 2013
Publication Date
July 1, 1992
Publication Information
Publication: The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
Volume: 40
Issue: 7
ISSN: 0022-1554
Subject Category
Life Sciences (General)
Distribution Limits
Non-NASA Center
NASA Discipline Musculoskeletal

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