Adult human masseter muscle fibers express myosin isozymes characteristic of development.
Masseter muscle biopsies were obtained from nine patients undergoing orthognatic surgery or surgery for parotid tumors. A detailed enzyme-histochemical and immunocytochemical study of these muscles was performed using antibodies specific to the various isozymes of the myosin heavy chain (MHC) in order to identify the MHC isozymes that were present in the different fiber types. The contractile proteins in these same biopsies were analyzed by two-dimensional gel electrophoresis, native pyrophosphate gel electrophoresis, and by an immunopolypeptide mapping approach. These studies have shown that there is a very heterogeneous distribution of the myosin isozymes, with many fibers containing more than one myosin type. We also present evidence that in addition to adult fast and slow myosin, the human masseter muscle contains two proteins, neonatal MHC and embryonic myosin light chain, that are characteristic of developing muscle.
Butler-Browne
G S
GS
Departement de Biologie Moléculaire, Institut Pasteur, Paris, France.
Eriksson
P O
PO
Laurent
C
C
Thornell
L E
LE
D004586:Electrophoresis; D006801:Humans; D007150:Immunohistochemistry; D008406:Masseter Muscle / Q000201:enzymology*; D008410:Masticatory Muscles / Q000201:enzymology*; D009218:Myosins / Q000032:analysis*
D009218:Myosins