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Regulation of human skeletal muscle phosphorylase...
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Regulation of human skeletal muscle phosphorylase and glycogenolysis during maximal exercise

Abstract

In six subjects, the transformation of phosphorylase and glycogenolytic rate were studied in the first and third of three 30-s bouts of maximal cycling, separated by 4 min of rest. Vastus biopsies were taken before, at 15s and 30s of bouts 1 and 3. In bout 1, the mole fraction of active phosphorylase (PHOS a) was 9.9+2.2% at rest, increased to 47.4±6.4% at 15s and by 30s, decreased to 21.8+4.2%. During the first and last 15s of bout 1, glycogenolytic rates were 183 and 34 mmol/min/kg dw, respectively. The 15s [AMP,] of 3.8+0.6 umol/kg dw and [P,2-] of 29.1±5.7 mmol/kg dw were 20.0+0.3 and 28.7+3.5, respectively at 30s. [H] was 157.4+9.8 at 15s and 182.9±12.4 nmol/l at 30s. Bout 3 resting PHOS a of 10.5+2.7% increased to 20.5+1.6% at 15s and decreased to 16.2+5.7% at 30s. Glycogenolytic rates were 28 and 11 mmol/min/kg dw during the first and last 15s of bout 3, respectively. The bout 3 15s [AMP,] of 5.1 ±1.6 Mmol/kg dw and [P,2-] of 28.3+5.0 mmol/kg dw, were 15.6+4.1 and 26.5+5.9, respectively at 30s. [H4] was 231.4+13.0 and 254.5+36.1 nmol/l at 15s and 30s, respectively. Elevated [HJ during the last 1?s of bout 1 may result in decreased PHOS a and glycogenolysis despite increased [AMPJ and [P,2"]. Both PHOS a and glycogenolysis are further reduced in bout 3 compared to bout 1, despite similar [AMPJ and [P,2-] suggesting [H] is again responsible for the decreased flux. Funded by MRC and NSERC.

Authors

Parolin M; Cheslev A; Malsos M; Spriet LL; Jones NL; Heinenhauser GJF

Volume

10

Publication Date

December 1, 1996

Conference proceedings

FASEB Journal

Issue

3

ISSN

0892-6638

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