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Role of AMP-Activated Protein Kinase in the Glycolysis of Postmortem Muscle

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Role of AMP-Activated Protein Kinase in the Glycolysis of Postmortem Muscle Journal of the Science of Food and Agriculture J Sci Food Agric 85:2401–2406 (2005) DOI: 10.1002/jsfa.2252 Role of AMP-activated protein kinase in the glycolysis of postmortem muscle Qingwu W Shen and Min Du∗ Department of Animal Science, University of Wyoming, Laramie, WY 82071, USA Abstract: AMP-activated protein kinase (AMPK) is a newly identified kinase controlling energy metabolism in vivo. The objective of this study was to show the role of AMPK in postmortem glycolysis. Rapid and excessive postmortem glycolysis is directly related to the incidence of PSE (pale, soft and exudative) meat in pork, chicken and turkey, while insufficient glycolysis leads to dark cutters in beef and lamb, which causes significant loss to the meat industry. A total of 24 two-month-old C57BL/6J mice were assigned to three treatments: (1) wild-type mice without pre-slaughter treatment; (2) wild-type mice with a 2 min swim before slaughter; and (3) wild-type mice intraperitoneally injected with AICAr (50 mg kg−1), a specific activator of AMPK, to stimulate the activity of AMPK. In addition, 16 two- month-old C57BL/6J mice with AMPK knockout were assigned to two treatments: (4) AMPK knockout mice without pre-slaughter treatment; and (5) AMPK knockout mice with a 2 min swim before slaughter. The longissimus dorsi muscle was sampled at 0, 1 and 24 h postmortem for pH and enzyme activity measurements. Results showed that AMPK activity had a major role in determining the ultimate muscle pH. Pre-slaughter stress induced by swimming significantly accelerated the glycogenolysis in postmortem muscle through activating glycogen phosphorylase. AMPK is important for maintaining the activity of glycogen phosphorylase and pyruvate kinase, and glycogenolysis/glycolysis in postmortem muscle. Thus, AMPK has an important role in the control of postmortem glycolysis and is crucial for a lower ultimate pH in postmortem muscle. However, the activation of AMPK cannot fully account for the initial rapid glycogenolysis/glycolysis induced by stress and another mechanism must exist for the accelerated glycolysis induced by pre-slaughter stress. 2005 Society of Chemical Industry Keywords: AMPK; muscle; postmortem; glycolysis; pH value; PSE INTRODUCTION beef and lamb is another problem associated with PSE (pale, soft, exudative) meat has a high drip loss, a postmortem glycolysis, which, however, is due to low cooking yield and a dry texture after cooking. Fast insufficient glycolysis. Owing to its inferior quality, glycolysis in postmortem muscle causes PSE syndrome the dark cutter in beef also causes significant loss in pork, turkey and chicken while excessive glycolysis to the meat industry.8 In order to solve these is related to ‘acid meat’ in Hampshire pigs.1–3 The problems, it is necessary to understand the underlying Pork Chain Quality Audit stated that ‘10.2% of the mechanisms. carcasses were classified as having PSE muscle’.4 For AMP-activated protein kinase (AMPK) is mainly turkey, observations in the slaughterhouse (especially recognized as a crucial kinase controlling energy in the USA) have shown that PSE meat could metabolism.9 Recent biomedical studies have indi- represent from 5% to 30% of the slaughtered turkeys.5 cated that AMPK plays a crucial role in the initiation of In chicken, using colour L∗ values of 3 h and 24 h glycogenolysis/glycolysis in skeletal and cardiac mus- postmortem fillets as an indicator, ∼47% of the 3554 cle in vivo.9 AMPK, a heterotrimeric enzyme with α, fillets tested were pale and could potentially exhibit β and γ subunits, is mainly recognized as a critical poor water-holding capacity.6 The high incidence of regulator of energy metabolism.9 Each subunit exists PSE syndrome causes significant losses to the meat as isoforms encoded by two or three genes (α1, α2, industry.6,7 However, the mechanisms associated with β1, β2, γ 1, γ 2, γ 3).10 The α subunit is the catalytic this abnormal glycolysis in postmortem muscle and the unit, the γ subunit has a regulatory function, and incidence of PSE meat are largely unclear. The dark the β unit provides anchorage sites for α and γ .11 cutter, or DFD (dark, firm and dry), syndrome in The γ 3 subunit is expressed at high levels in skeletal ∗ Correspondence to: Min Du, Department of Animal Science, University of Wyoming, Laramie, WY 82071, USA E-mail: [email protected] Contract/grant sponsor: USDA Cooperative State Research, Education, and Extension Service; contract/grant number: National Research Initiative Competitive Grant USDACSRE45101 Contract/grant sponsor: University of Wyoming (Received 9 December 2004; revised version received 15 February 2005; accepted 15 March 2005) Published online 13 July 2005 2005 Society of Chemical Industry. J Sci Food Agric 0022–5142/2005/$30.00 2401 QW Shen, M Du muscle only.12 AMPK is switched on by an increase Enzyme activity measurements in the AMP/ATP ratio in muscle cells, which leads Muscle homogenate to the phosphorylation of AMPK at Thr172 by an Frozen longissimus dorsi muscle samples were unidentified kinase.9 Once activated, AMPK switches cut into small pieces and mixed. Longissimus on glycogenolysis/glycolysis.10,11 The important role dorsi muscles (0.01 g) were weighed and then of AMPK in the control of glycolysis in vivo has been homogenized in a Polytron homogenizer (7 mm demonstrated by several studies. Administration of diameter generator) (IKA Works Inc, Wilming- AICAr, a specific activator of AMPK, to stimulate ton, NC, USA) with 5 vol. of ice-cold lysis −1 −1 AMPK activity dramatically increases the lactic acid buffer (137 mmol L NaCl, 1 mmol L MgCl2, 13 −1 content in muscle. Also, knockout AMPK signifi- 1mmolL CaCl2, 1% nonylphenyl-polyethylene − cantly reduced the pH decline in ischaemic cardiac glycol, 10% glycerol, 2 mmol L 1 phenylmethane- − muscle.14 No study has been conducted on the role of sulfonyl fluoride, 10 mmol L 1 sodium pyrophos- − AMPK in the glycolysis of postmortem muscle. It is phate, 2.5 mmol L 1 ethylenediaminetetraacetic acid − − hypothesized that AMPK plays an important role in (EDTA), 10 µgmL 1 aprotinin, 10 µgmL 1 leu- − the glycolysis of postmortem muscle and the incidence peptin, 100 mmol L 1 NaF). Following centrifuging of PSE meat. Using transgenic mice, the objective of at 12 000 × g for 5 min at 4 ◦C, the supernatant was this study was to show the role of AMPK in the used for enzyme activity measurements. glycolysis of postmortem muscle. AMPK AMPK activity was measured using a method EXPERIMENTAL based on its specific phosphorylation of a SAMS Dietary treatments peptide.16,17 Briefly, a SAMS peptide substrate A total of 24 two-month-old C57BL/6J mice† (half was used (His-Met-Arg-Ser-Ala-Met-Ser-Gly-Leu- male, half female) were assigned to three treatments His-Leu-Val-Lys-Arg-Arg; Invitrogen, Carlsbad, CA, (4 male and 4 female mice per treatment): (1) normal USA). The muscle homogenate obtained above was mice without any treatment; (2) mice with a 2 min centrifuged at 13 000 × g for 5 min at 4 ◦C. The super- swim before slaughter; and (3) mice intraperitoneally natant (10 µL) was incubated for 10 min at 37 ◦C − injected with AICAr (50 mg kg 1) (Calbiochem, La in 40 mmol L−1 4-2-hydroxyethyl-1-piperazineethane- Jolla, CA 92 039, USA), a specific activator of AMPK, sulfonic acid (HEPES), 0.2mmolL−1 SAMS pep- to stimulate the activity of AMPK, and then a wait of tide, 0.2 mmol L−1 AMP, 80 mmol L−1 NaCl, 8% 15 min to let the AICAr go into muscle cells before (w/v) glycerol, 0.8 mmol L−1 EDTA, 0.8mmolL−1 −1 slaughter. In addition, 16 two-month-old C57BL/6J dithiothreitol (DDT), 5 mmol L MgCl2,and mice with AMPK knockout were assigned to two 0.2mmolL−1 ATP + 2 µCi [32P]ATP, pH 7.0, in a treatments (4 male and 4 female mice per treatment): final volume of 50 µL. An aliquot (20 µL) was removed (4) AMPK knockout mice without any treatment; and and spotted on a 2 cm × 2 cm piece of Whatman P81 (5) AMPK knockout mice with a 2 min swim before filter paper. The [32P]ATP was removed with six slaughter. The AMPK knockout mice were origi- washes in 1% phosphoric acid, and the radioactiv- nally obtained from Dr MJ Birnbaum (Department ity was quantified after immersing the filter paper in of Medicine and Howard Hughes Medical Institute, 3 mL Scintiverse (Fisher Scientific, Hanover Park, IL, University of Pennsylvania) and bred in our labora- USA). The activity was expressed as the phosphory- tory. These AMPK knockout mice express a dominant lation of nanomolar peptide per minute per gram of negative AMPKα2 under the control of the muscle- muscle. specific creatine kinase promoter.15 The mice were anaesthetized by CO2 and then killed immediately. Glycogen phosphorylase ∼ Within 4 min, the pelt was removed and 0.2 g each of Glycogen phosphorylase-a activity was measured by upper-right and lower-left longissimus dorsi muscle was the incorporation of [U-14C] glucose into glyco- ∼ removed and combined. Part of this muscle ( 0.1g) gen when a high level of glucose-1-phosphate was was used for pH measurement and the rest was snap- present.18 Briefly, 200 µL of the supernatant of frozen in liquid nitrogen for analysis of enzyme activity. muscle homogenate obtained above was diluted Carcasses were eviscerated and suspended in a glass −1 ◦ 1:1 with ice-cold solution B (50 mmol L 2-(N- chamber at 4 C. Subsequent samples was taken in a morpholino)ethanesulfonic acid (MES), 50 mmol L−1 similar fashion from the middle part of both sides of the KF and 60 mmol L−1 β-mercaptoethanol, pH 6.1).
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