Presence in Human Skeletal Muscle of an AMP Deaminase-associated Protein That Reacts with an Antibody to Human Plasma HistidineProline-rich GlycoproteinAntonietta R. M. Sabbatinia, Maria RanieriRaggia, Luca Pollinab, Paolo Viacavab, John R. Ashbyc, Arthur J. G. Moirc, and Antonio Raggiaa Dipartimento di Scienze dell'Uomo e dell'Ambiente, Chimica e Biochimica Medica, Università di Pisa, Pisa, Italy b Dipartimento di Oncologia, Divisione di Anatomia Patologica, Università di Pisa, Pisa, Italy c Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom Correspondence to: Antonio Raggi, Dipartimento di Scienze dell’Uomo e dell’Ambiente, Chimica e Biochimica Medica, Università di Pisa, via Roma 55, 56126 Pisa, Italy. Histidineproline-rich glycoprotein (HPRG) is a protein that is synthesized by parenchimal liver cells. The protein has been implicated in a number of plasma-specific processes, including blood coagulation and fibrinolysis. We have recently reported the association of an HPRG-like protein with rabbit skeletal muscle AMP deaminase (AMPD). The results of the immunological analysis reported here demonstrate that an antibody against human plasma HPRG reacts with an AMPD preparation from human skeletal muscle. To probe the localization of the putative HPRG-like protein in human skeletal muscle, serial sections from frozen biopsy specimens were processed for immunohistochemical and histoenzymatic stains. A selective binding of the anti-HPRG antibody to Type IIB muscle fibers was detected, suggesting a preferential association of the novel protein to the AMPD isoenzyme contained in the fast-twitch glycolytic fibers. (J Histochem Cytochem 47:255260, 1999) Key Words: histidineproline-rich glycoprotein, AMP deaminase, human skeletal muscle, Western blot analysis, immunohistochemical analysis, histoenzymatic analysis
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