TY - JOUR
T1 - Myofibrillar ATPase activity in skinned human skeletal muscle fibres
T2 - Fibre type and temperature dependence
AU - Stienen, G. J M
AU - Kiers, J. L.
AU - Bottinelli, R.
AU - Reggiani, C.
PY - 1996/6/1
Y1 - 1996/6/1
N2 - 1. Myofibrillar ATP consumption and isometric tension (P0) were determined in chemically skinned skeletal muscle fibres from human rectus abdominis and vastus lateralis muscle. Fibres were classified in four groups (I, II A, IIB, IIA/B or mixed) based on myosin heavy chain composition. 2. ATP consumption (± S.E.M.) at 20°C varied from 0·41 ± 0·06 mmol l-1 s-1 in type IIB fibres (n = 5) to 0·10 ± 0·01 mmol l-1 s-1 in type I fibres (n = 13). 3. The ratio between ATPase activity and P0 (tension cost) differed significantly between fast type II and slow type I fibres. At 12°C tension cost was lower than the values found previously in corresponding fibre types in the rat. 4. The relative increase in ATPase activity for a 10°C temperature change (Q10), determined in the range from 12 to 30°C, was temperature independent and amounted to 2·60 ± 0·06. The increase in P0 with temperature was smaller and declined when the temperature increased. 5. From these measurements, estimates were obtained for the maximum rate of isometric ATP consumption and force development at muscle temperature in vivo (35°C).
AB - 1. Myofibrillar ATP consumption and isometric tension (P0) were determined in chemically skinned skeletal muscle fibres from human rectus abdominis and vastus lateralis muscle. Fibres were classified in four groups (I, II A, IIB, IIA/B or mixed) based on myosin heavy chain composition. 2. ATP consumption (± S.E.M.) at 20°C varied from 0·41 ± 0·06 mmol l-1 s-1 in type IIB fibres (n = 5) to 0·10 ± 0·01 mmol l-1 s-1 in type I fibres (n = 13). 3. The ratio between ATPase activity and P0 (tension cost) differed significantly between fast type II and slow type I fibres. At 12°C tension cost was lower than the values found previously in corresponding fibre types in the rat. 4. The relative increase in ATPase activity for a 10°C temperature change (Q10), determined in the range from 12 to 30°C, was temperature independent and amounted to 2·60 ± 0·06. The increase in P0 with temperature was smaller and declined when the temperature increased. 5. From these measurements, estimates were obtained for the maximum rate of isometric ATP consumption and force development at muscle temperature in vivo (35°C).
UR - http://www.scopus.com/inward/record.url?scp=0030007659&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030007659&partnerID=8YFLogxK
M3 - Article
C2 - 8782097
AN - SCOPUS:0030007659
SN - 0022-3751
VL - 493
SP - 299
EP - 307
JO - Journal of Physiology
JF - Journal of Physiology
IS - 2
ER -