Presence in human skeletal muscle of an AMP deaminase-associated protein that reacts with an antibody to human plasma histidine-proline-rich glycoprotein
Arm. Sabbatini et al., Presence in human skeletal muscle of an AMP deaminase-associated protein that reacts with an antibody to human plasma histidine-proline-rich glycoprotein, J HIST CYTO, 47(2), 1999, pp. 255-260
Histidine-proline-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. W
e have recently reported the association of an HPRG-like protein with rabbi
t skeletal muscle AMP deaminase (AMPD). The results of the immunological an
alysis reported here demonstrate that an antibody against human plasma HPRG
reacts with an AMPD preparation from human skeletal muscle. To probe the l
ocalization of the putative HPRG-like protein in human skeletal muscle, ser
ial sections from frozen biopsy specimens were processed for immunohistoche
mical and histoenzymatic stains. A selective binding of the anti-HPRG antib
ody to Type IIB muscle fibers was detected, suggesting a preferential assoc
iation of the novel protein to the AMPD isoenzyme contained in the fast-twi
tch glycolytic fibers.