Pr. Sears et Pf. Dillon, Differential coupling of smooth and skeletal muscle pyruvate kinase to creatine kinase, BIOCHEM, 38(45), 1999, pp. 14881-14886
The interaction of pyruvate kinase from skeletal (SKPK) and smooth (SMPK) m
uscle with MM-creatine kinase (MMCK) and BB-creatine kinase (BBCK) was asse
ssed using temporal absorbance changes, variations in absorbance at differe
nt wavelengths, concentration dependence, association in an electric field,
and PK kinetic activity. SKPK exhibits a time course of absorbance increas
e in the presence of MMCK with a time constant of 29.5 min. This increase o
ccurs at all wavelength from 240 to 1000 nm. At 195 nm, the combination of
SKPK and MMCK produces: a decrease in absorption with electric fields of bo
th 0 and 204 V/cm. The change in SKPK-MMCK is saturable. SKPK activity is s
ignificantly increased by the presence of MMCK in solutions of 0-32% ethano
l. These results indicate specific SKPK-MMCK interaction. SMPK and BBCK did
not exhibit similar coupling when the BBCK concentration dependence of abs
orbance or SMPK activity in solutions of 0-32% ethanol was determined. Both
MMCK and BBCK increased SKPK activity; neither MMCK nor BBCK increased SMP
K activity. The ability to form diazymatic complexes with creatine kinase a
ppears;to reside in SKPK. This coupling may account for the increased flux
through PK without significant substrate changes seen during skeletal muscl
e activation. This coupling will not occur in smooth muscle.