Differential coupling of smooth and skeletal muscle pyruvate kinase to creatine kinase

Citation
Pr. Sears et Pf. Dillon, Differential coupling of smooth and skeletal muscle pyruvate kinase to creatine kinase, BIOCHEM, 38(45), 1999, pp. 14881-14886
Citations number
14
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMISTRY
ISSN journal
00062960 → ACNP
Volume
38
Issue
45
Year of publication
1999
Pages
14881 - 14886
Database
ISI
SICI code
0006-2960(19991109)38:45<14881:DCOSAS>2.0.ZU;2-T
Abstract
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.