TY - JOUR
T1 - Protein breakdown on whole-body and organ level in non-cachectic tumour-bearing mice undergoing surgery
AU - Vissers, Y.L.
AU - von Meyenfeldt, M.F.
AU - Argiles, J.M.
AU - Luiking, Y.C.
AU - Dejong, C.H.
AU - Deutz, N.E.
PY - 2007/1/1
Y1 - 2007/1/1
N2 - BACKGROUND & AIMS: Since both cancer and surgery are known to alter protein turnover, we investigated how the presence of tumour affects post-operative protein breakdown. METHODS: Controls and tumour-bearing non-cachectic mice were studied, both with and without laparotomy (n=8 per group). One day after laparotomy, stable isotopes of phenylalanine and 3-methylhistidine were used in a steady-state protocol to assess total protein breakdown on whole-body level and in muscle, intestines, liver and kidney, in addition to whole-body myofibrillar protein breakdown and body composition. Proteasomal chymotrypsin-like activity was measured to determine activity of the ATP-dependent ubiquitin pathway. RESULTS: On whole-body level, the presence of tumour increased total protein breakdown from 47+/-6 to 58+/-4nmol/10g/min (p<0.05) and myofibrillar protein breakdown from 0.70+/-0.04 to 1.22+/-0.14nmol/10g/min (p<0.05) without affecting protein breakdown in organs, body composition or proteasomal activity. Laparotomy increased myofibrillar protein breakdown in controls (from 0.70+/-0.04 to 0.98+/-0.12nmol/10g/min, p<0.05) and tumour-bearing mice (from 1.22+/-0.14 to 1.54+/-0.22nmol/10g/min, p=0.15) to a similar extent. CONCLUSIONS: Whole-body total protein breakdown, total protein breakdown across organs, body composition or proteasomal activity were not affected by laparotomy. Tumour-bearing mice had increased total and myofibrillar protein breakdown on whole-body level even before weight loss was obvious. However, this did not affect the post-operative response in protein breakdown or body composition.
AB - BACKGROUND & AIMS: Since both cancer and surgery are known to alter protein turnover, we investigated how the presence of tumour affects post-operative protein breakdown. METHODS: Controls and tumour-bearing non-cachectic mice were studied, both with and without laparotomy (n=8 per group). One day after laparotomy, stable isotopes of phenylalanine and 3-methylhistidine were used in a steady-state protocol to assess total protein breakdown on whole-body level and in muscle, intestines, liver and kidney, in addition to whole-body myofibrillar protein breakdown and body composition. Proteasomal chymotrypsin-like activity was measured to determine activity of the ATP-dependent ubiquitin pathway. RESULTS: On whole-body level, the presence of tumour increased total protein breakdown from 47+/-6 to 58+/-4nmol/10g/min (p<0.05) and myofibrillar protein breakdown from 0.70+/-0.04 to 1.22+/-0.14nmol/10g/min (p<0.05) without affecting protein breakdown in organs, body composition or proteasomal activity. Laparotomy increased myofibrillar protein breakdown in controls (from 0.70+/-0.04 to 0.98+/-0.12nmol/10g/min, p<0.05) and tumour-bearing mice (from 1.22+/-0.14 to 1.54+/-0.22nmol/10g/min, p=0.15) to a similar extent. CONCLUSIONS: Whole-body total protein breakdown, total protein breakdown across organs, body composition or proteasomal activity were not affected by laparotomy. Tumour-bearing mice had increased total and myofibrillar protein breakdown on whole-body level even before weight loss was obvious. However, this did not affect the post-operative response in protein breakdown or body composition.
U2 - 10.1016/j.clnu.2007.03.005
DO - 10.1016/j.clnu.2007.03.005
M3 - Article
C2 - 17513024
SN - 0261-5614
VL - 26
SP - 483
EP - 490
JO - Clinical Nutrition
JF - Clinical Nutrition
IS - 4
ER -