Wooden breast myopathy links with poorer gait in broiler chickens.

Wooden breast myopathy, a condition where broiler breast muscles show a hardened consistency post-mortem, has been described recently. However, it is not known how wooden breast myopathy affects the bird activity or welfare. Altogether, over 340 birds of five commonly used commercial hybrids were housed in 25 pens, and sample birds killed at ages of 22, 32, 36, 39 and 43 days. Their breast muscle condition was assessed post-mortem by palpation. The birds were gait scored and their latency to lie was measured before killing. For further behavior observations, one affected and healthy bird in 12 pens were followed on 5 days for 20 minutes using video recordings. The connection of myopathy to gait score and activity was analyzed with mixed models. A higher gait score of wooden-breast-affected birds than that of unaffected birds (2.9 ± 0.1 v. 2.6 ± 0.1, P < 0.05) indicated a higher level of locomotor difficulties over all age groups. The wooden-breast-affected birds had fewer crawling or movement bouts while lying down compared with unaffected (P < 0.05). Wooden breast myopathy-affected birds were heavier (2774 ± 91 v. 2620 ± 91 g; P < 0.05) and had higher breast muscle yield (21 ± 1 v. 19 ± 1%; P < 0.05) than unaffected birds overall. Older birds had longer lying bouts, longer total lying time, fewer walking bouts, more difficulties to walk and to stand compared with younger birds (P < 0.05). Birds with poorer gait had longer total lying time and fewer walking bouts (P < 0.05). Birds with greatest breast muscle yield had the largest number of lying bouts (P < 0.05). It was concluded that wooden breast myopathy was associated with an impairment of gait scores, and may thus be partly linked to the common walking abnormalities in broilers.

Pectoral Vessel Density and Early Ultrastructural Changes in Broiler Chicken Wooden Breast Myopathy.

In wooden breast myopathy (WBM) of broiler chickens, the pectoralis major muscles show abnormally hard consistency and microscopical myodegeneration of unknown aetiology. To date, previous studies have focused primarily on chronic WBM and ultrastructural descriptions of early WBM are lacking. The aim of this study was to elucidate the pathogenesis of WBM by light microscopical morphometry of vessel density and the ultrastructural description of early WBM changes with transmission electron microscopy. The pectoral vessel density was compared between unaffected chickens (n = 14) and two areas of focal WBM in affected chickens (n = 14). The transverse myofibre area per vessel was highest in the unaffected area of muscle from cases of focal WBM, significantly higher (P = 0.01) than in macroscopically unaffected tissue, indicating that relatively decreased blood supply may trigger the development of WBM. The ultrastructural study included unaffected chickens (n = 3), two areas of focal WBM from affected chickens (n = 3) and areas of diffuse WBM from affected chickens (n = 3). The morphologically least affected myofibres within the WBM lesion areas in light microscopy exhibited ultrastructural changes of increased sarcoplasmic reticulum diameter and mitochondrial hyperplasia. Such changes originate typically from osmotic imbalance, for which the most likely aetiologies in WBM include tissue hypoxia or myodegeneration of the surrounding myofibres. The findings suggest that a relative reduction of blood supply in the major pectoral muscle occurs in the early phase of WBM, which may be linked to the ultrastructural changes of osmotic imbalance.

Evolution of proteolytic indicators during storage of broiler wooden breast meat.

In the past few yr, an emerging muscle abnormality termed wooden breast (WB) was found to affect broilers' Pectoralis major muscles. Although different studies have been performed in order to evaluate the effect of WB on meat quality, there is no evidence concerning its impact on the proteolytic processes taking place during meat aging. Thus, this study aimed at investigating the effect of a 7-day storage of broiler breast fillets on free calcium concentration, calpain activity, and proteolysis. Both the superficial and the deep layers of the Pectoralis major muscles were considered. Although similar electrophoretic profiles were observed by comparing the corresponding sampling positions, an evident lack of a high-molecular weight protein band, ascribed to nebulin, was found in the superficial layer of the WB fillets at 10 h postmortem. Compared to normal fillets (NB), both the superficial and the deep layer of WB exhibited a significantly higher amount of free calcium at 168 h postmortem (96 and 88 vs. 20 and 53 µM; P ≤ 0.001). Casein zymograms evidenced the presence of µ/m-calpain and its autolyzed form migrating as a doublet within the gel. Interestingly, neither the occurrence of WB nor the intra-fillet sampling position exerted any relevant effect on calpain activity. Indeed, a significant reduction (P ≤ 0.05) in the unautolyzed µ/m-calpain activity coupled with a remarkable increase (P ≤ 0.05) in the autolyzed form activity was observed during storage. Concurrently, if compared to NB, a significantly larger (P ≤ 0.05) amount of desmin was detected in both the superficial and the deep layers of the WB samples at 10 h postmortem. Then, a sharp decrease of the intact desmin band coupled with a progressive accumulation of its 39-kDa degradation fragment was observed without any significant difference among groups. In conclusion, the increased hardness that typically affects the WB cases seemed not to be exclusively attributable to differences in the proteolytic processes taking place within the postmortem period.

Chronic activation of AMP-activated protein kinase increases monocarboxylate transporter 2 and 4 expression in skeletal muscle.

Acute activation of AMP-activated protein kinase (AMPK) increases monocarboxylate transporter (MCT) expression in skeletal muscle. However, the impact of chronic activation of AMPK on MCT expression in skeletal muscle is unknown. To investigate, MCT1, MCT2, and MCT4 mRNA expression and protein abundance were measured in the longissimus lumborum (glycolytic), masseter (oxidative), and heart from wild-type (control) and AMPK γ3 pigs. The AMPK γ3 gain in function mutation results in AMPK being constitutively active in glycolytic skeletal muscle and increases energy producing pathways. The MCT1 and MCT2 mRNA expression in muscle was lower ( < 0.05) from both wild-type and AMPK γ3 animals compared to other tissues. However, in both genotypes, MCT1 and MCT2 mRNA expression was greater ( < 0.05) in the masseter than the longissimus lumborum. The MCT1 protein was not detected in skeletal muscle, but MCT2 was greater ( < 0.05) in muscles with an oxidative muscle phenotype. Monocarboxylate transporter 2 was also detected in muscle mitochondria and may explain the differences between muscles. The MCT4 mRNA expression was intermediate among all tissues tested and greater ( < 0.05) in the longissimus lumborum than the masseter. Furthermore, MCT4 protein expression in the longissimus lumborum from AMPK γ3 animals was greater ( < 0.05) than in the longissimus lumborum from wild-type animals. In totality, these data indicate that chronic AMPK activation simultaneously increases MCT2 and MCT4 expression in skeletal muscle.

Wooden Breast Myodegeneration of Pectoralis Major Muscle Over the Growth Period in Broilers.

Wooden breast (WB) myopathy of broiler chickens is a myodegenerative disease of an unknown etiology and is macroscopically characterized by a hardened consistency of the pectoralis major muscle. Our aim was to describe the development and morphology of WB over the growth period in broilers. Additionally, the effect of restricted dietary selenium on the occurrence of WB was examined by allocating the birds in 2 dietary groups: restricted and conventional level of selenium. The experiment included 240 male broilers that were euthanized at ages of 10, 18, 24, 35, 38, or 42 days and evaluated for WB based on abnormal hardness of the pectoralis major muscle. The severity and the distribution of the lesion and presence of white striping were recorded. The first WB cases were seen at 18 days; 13/47 birds (28%) were affected and the majority exhibited a mild focal lesion. In subsequent age groups the WB prevalence varied between 48% and 73% and the lesion was usually diffuse and markedly firm. White striping often coexisted with WB. Histological evaluation performed on 111 cases revealed a significant association of myodegeneration and lymphocytic vasculitis with WB. Vasculitis and perivascular cell infiltration were restricted to the veins. Restricted dietary selenium did not affect the occurrence of WB ( P = .44). Our results indicate that WB starts focally and spreads to form a diffuse and more severe lesion.

Technological quality, mineral profile, and sensory attributes of broiler chicken breasts affected by White Striping and Wooden Breast myopathies.

The aim of the research was to study the impact of white striping and wooden breast myopathies on the technological quality, mineral, and sensory profile of poultry meat. With this purpose, a total of 138 breasts were selected for a control group with normal breasts (N), a group of breasts characterised by white striping (WS) myopathy, and a group of breasts having both white striping and wooden breast myopathies (WSWB). Data revealed that the simultaneous presence of the two myopathies, with respect to the WS lesion individually considered, had a further detrimental effect on pH (6.04 vs. 5.96; P < 0.05), yellowness (11.4 vs. 10.3; P < 0.01), cooking losses (30.4 vs. 27.6%; P < 0.05), toughness instrumental values (22.8 vs. 20.0 N; P < 0.01), and perception (6.22 vs. 5.56; P < 0.01). In addition, mineral contents suggest that a defective ions regulation is also present in white striping and wooden breast myopathies.

Myodegeneration with fibrosis and regeneration in the pectoralis major muscle of broilers.

A myopathy affecting the pectoralis major muscle of the commercial broiler has emerged creating remarkable economic losses as well as a potential welfare problem of the birds. We here describe the macroscopic and histologic lesions of this myopathy within 10 pectoralis major muscles of 5- to 6-week-old broilers in Finland. Following macroscopic evaluation and palpation of the muscles, a tissue sample of each was fixed in formalin, processed for histology, and histologically evaluated. The muscles that were macroscopically hard, outbulging, pale, and often accompanied with white striping histologically exhibited moderate to severe polyphasic myodegeneration with regeneration as well as a variable amount of interstitial connective tissue accumulation or fibrosis. All affected cases also exhibited perivenular lymphocyte accumulation. The etiology of this myodegenerative lesion remains yet open. Polyphasic myodegeneration is associated with several previously known etiologies, but palpatory hardness focusing on the pectoralis major, together with perivenular lymphocytes, has not been described in relation to them. The results of this study provide the pathological basis for further studies concerning the etiology of the currently described myopathy.

High early post-mortem temperature induces activation of AMP-activated protein kinase and development of pale, soft and exudative characteristics in turkey muscles.

This study investigated the effect of early post-mortem temperature on development of a turkey muscle's pale, soft and exudative (PSE) characteristics. Muscles obtained at 20 min post-mortem were incubated at 0, 20 and 40 °C until 4 h post-mortem and then stored at 4 °C. During incubation, the 40 °C group had greater rate of pH decline, lactate accumulation and R-values increase than other groups. Moreover, AMP-activated protein kinase (AMPK) activation at 1h post-mortem was higher in the 40 °C group than the other groups. At 24 h post-mortem, the 40 °C group had higher L* values and drip loss; SDS-PAGE and western blotting indicated that lower protein solubility (sarcoplasmic, myofibrillar) in the 40 °C group resulted from phosphorylase denaturation and further adhere to myofibrillar fraction. These results suggest that high temperature early post-mortem could induce AMPK activation, which results in rapid glycolysis, thus affecting protein solubility and generating PSE characteristics.

The effects of high salt and low pH on the water-holding of meat.

The study investigated the water-holding (WH) in meat in the pH-NaCl (ionic strength) combinations that prevail in dry sausages during fermentation and drying. WH in raw beef homogenates, with 230% added water, was determined by centrifugation at pH values of 5.47-4.60, and ionic strengths (µ) 0.50-1.50. The minimum WH in relation to pH was at pH 4.8, but at higher pH values, the WH optimum was at 1.0-1.5 µ; at lower pH-values (<5.0) the optimum was more pronounced at 1.0 µ. The WH reducing effect by pH decrease was stronger than the effect of µ. At lower pH values, the relative effect of µ on WH was higher compared to that of pH than at higher pH values. The pH-salt combinations prevailing in fermented sausage in the beginning of the ripening produced a high WH, which decreased, first with pH decrease and then in the last period of ripening mainly due to the increase of ionic strength.

Gas composition in controlled atmosphere stunning affects turkey meat quality traits.

1. Investigations were made into the breast and leg muscle energy metabolism, and the quality of breast meat of turkeys after controlled atmosphere stunning or stun-killing (CAS) with various gas mixtures. In addition, the effect on meat quality of an increase in the chilling rate of turkey breast meat after hypercapnic or anoxic stun-killing was studied. 2. A total of 35 turkey toms within two replicate pens were individually stunned during consecutive weeks using one of 4 CAS methods. The stunning gases tested were high CO(2) concentration (60% CO(2) in air), high N(2) concentration (98% N(2), < 2% O(2)), a mixture of 76% N(2) and 24% CO(2), and a biphasic method (first minute in mixture containing 40% CO(2), 30% N(2), and 30% O(2;) followed by two minutes in a mixture containing 60% CO(2) in air). 3. The birds stunned with N(2) displayed the highest initial reduction in muscle pH, but after 4 h post mortem there were no differences in pH values associated with the various CAS methods. 4. The CAS method alone had no statistically significant effect on the quality of turkey breast muscle when the chilling speed was rapid (0°C for 4 h, followed by storage at 4°C). When the chilling rate was slowed (20°C for 4 h followed by storage at 4°C), a significant decrease in cooking loss and in Warner-Bratzler shear force was recorded for birds stun-killed with CO(2). 5. This study shows that anoxic stun-killing with N(2) had no adverse effects on meat quality despite the rapid post mortem pH decrease. The CAS with N(2) allows rapid cooling of carcases without the risk of cold shortening, whereas with CO(2)-stun-killing of turkeys, the rate of chilling should be slower. Concerning meat quality, all the CAS methods tested were suitable for stunning turkeys.

High number of Yersinia enterocolitica 4/O:3 in cold-stored modified atmosphere-packed pig cheek meat.

Yersinia enterocolitica is a psychrotrophic, facultative anaerobic zoonotic bacterium belonging to family Enterobacteriaceae and it can be transmitted from pigs to humans through pork. The growth of bacteria belonging to Enterobacteriaceae and aerobic spoilage bacteria is usually effectively restricted by 20% or more CO(2) enriched atmosphere at refrigerated temperatures. In this study, 40 samples of meat strips from pig cheek (musculus masseter) and 40 samples from hind leg (m. semimembranosus) muscles were packaged in modified atmosphere (MA) (30% CO(2)/70% O(2)) and stored at 6°C for 12d. Twenty naturally contaminated samples per muscle type were studied on days 1 and 13. Violet red bile glucose (VRBG) and de Man Rogosa Sharpe (MRS) agar plates were used for enumeration of Enterobacteriaceae including Y. enterocolitica and lactic acid bacteria, respectively. During the 12-d storage at 6°C in MA, the mean number of bacteria on pork strips of cheek meat was increasing from 1.6 to 4.5 log cfu/g and from 3.1 to 7.2 log cfu/g on VRBG and MRS agar plates, respectively. Most of the oxidase-negative isolates on VRBG plates, which were isolated from the cheek meat samples after 12-d cold storage in MA, were identified as Y. enterocolitica 4/O:3. The mean number of this pathogen was 4.1 log cfu/g varying between 2.3 and 5.4 log cfu/g. The pH of the cheek meat and leg meat was measured on days 1 and 13, and it remained high (pH>6) in most cheek meat samples during the storage. No Y. enterocolitica 4/O:3 was isolated from meat strips of hind leg. This study shows that cheek meat of slaughter pigs is contaminated with Y. enterocolitica 4/O:3 and that this pathogen can grow well on raw pork packaged in MA at 6°C even in the presence of high number of lactic acid bacteria.

Theoretical aspects of water-holding in meat.

As myofibrils consist of a three-dimensional network of long, solid protein particles with the shortest dimension of less than 20 nm, the theoretical foundations of water-holding in meat should be studied from a colloid or surface chemistry point of view. The classical hypotheses for water-holding in meat are based on electrostatic forces or osmotic forces, which cause the swelling of the myofibrils. The more recent research adds to those the structure of water, whether it is low density water induced by kosmotropic effects dominating in the system, or high density water induced by chaotropes, respectively. The phenomena in the one to three molecules thick water layers on protein surfaces do not, however, explain the bulk water-holding.The interactions of ions and non-polar kosmotropes with water and proteins have a relevant effect on water-holding. The chaotropic/kosmotropic effects of different ions will be of importance especially when reducing sodium contents in meat-based foods. Rough estimates of the surface areas of different constituents of the myofibrils showed that transverse elements have larger contact surfaces with the liquid phase than longitudinal. Therefore, more attention should be paid to heavy meromyosin, Z-line and other elements of molecular size or colloidal size. Short range surface forces seem to dominate theories of water-protein interactions, and the theoretical foundations of bulk water-holding are still lacking. Irrespective of the lack of theoretical explanation on the mechanism of water-holding in meat, the meat industry is able to control the macroscopic behaviour of meat-based ingredients rather well.

Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels.

UNLABELLED: The effects of Trichoderma reesei tyrosinase-catalyzed cross-linking of isolated chicken breast myofibril proteins as a simplified model system were studied with special emphasis on the thermal stability and gel formation of myofibrillar proteins. In addition, tyrosinase-catalyzed cross-linking was utilized to modify the firmness, water-holding capacity (WHC), and microstructure of cooked chicken breast meat homogenate gels. According to SDS-PAGE, the myosin heavy chain (MHC) and troponin T were the most sensitive proteins to the action of tyrosinase, whereas actin was not affected to the same extent. Calorimetric enthalpy (DeltaH) of the major thermal transition associated with myosin denaturation was reduced and with actin denaturation increased in the presence of tyrosinase. Low-amplitude viscoelastic measurements at constant temperatures of 25 degrees C and 40 degrees C showed that tyrosinase substantially increased the storage modulus (G') of the 4% myofibrillar protein suspension in the 0.35 M NaCl concentration. The effect was the most pronounced with high-enzyme dosages and at 40 degrees C. Without tyrosinase, the G' increase was low. Tyrosinase increased the firmness of the cooked phosphate-free and low-meat chicken breast meat homogenate gels compared to the corresponding controls. Tyrosinase maintained gel firmness at the control level of the low-salt homogenate gel and weakened it when both salt and phosphate levels were low. Tyrosinase improved the WHC of the low-meat and low-salt homogenate gels and maintained it at the level of the corresponding controls of phosphate-free and low-salt/low-phosphate homogenate gels. Microstructural characterization showed that a collagen network was formed in the presence of tyrosinase. KEYWORDS: Chicken myofibrillar proteins; protein modification; cross-linking; tyrosinase; gelation; thermal stability; texture; water-holding capacity; microstructure.

Thermal stability of connective tissue from porcine muscles.

Connective tissue of three porcine muscles (M. infraspinatus, IS; M. longissimus dorsi, LD; M. semimembranosus, SM) from 27 animals [populations A (n=13, reared in Ireland) and B (n=14, reared in Finland)] was studied by measuring the collagen content, collagen solubility and thermal shrinkage temperature of the connective tissue. Colour and pH were also determined. Collagen solubility was highest in IS (p<0.05) and lowest in SM (p<0.05) although no difference between LD and SM was found in population B. The onset and peak temperatures of thermal shrinkage (T(o) and T(p)) were highest in IS (p<0.05). The lowest T(o) and T(p) were found in SM from population B whereas no differences were seen between LD and SM muscles in population A. It was concluded that the thermal stability of the connective tissue in the three porcine muscles differ. IS, as a dark muscle has high thermal shrinkage temperatures and high collagen solubilities in comparison to the lighter LD and SM muscles which have lower thermal shrinkage temperatures and collagen solubilities. Collagen contents were highest in IS and lowest in LD.

Temperature shows greater impact on bovine Longissimus dorsi muscle glycogen debranching enzyme activity than does salt concentration.

The degradation of glycogen progresses by the co-operation of two enzymes: glycogen phosphorylase (phosphorylase) and glycogen debranching enzyme (GDE). We studied the effect of temperature (4-42°C) and salt concentration (0-3% NaCl) on bovine M. longissimus dorsi GDE activity. GDE activity (n=4) decreased significantly with decreasing temperature from about 40-4°C. GDE exhibited 52% activity at 25°C and 11% at 4°C compared to its optimum activity measured at 39°C. In rapidly chilled meat, the reduction in GDE activity may substantially delay the rate of glycolysis. However, residual GDE activity at 4°C seems sufficient to enable the attainment of normal ultimate pH if the available time is long enough. An increase in salt concentration from 0% to 2% and to 3% induced a significant (P<0.001) increase in the ultimate pH of ground bovine meat (n=6), but showed no effect on GDE activity.

Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability.

The effect of laccase and transglutaminase (TG) on cross-linking, gelation, and thermal stability of salt-soluble chicken-breast myofibril proteins was investigated at pH 6. Both enzymes modified the protein pattern detected by SDS-PAGE. Identification of proteins by peptide mass mapping showed that myosin heavy chain (MHC) and troponin T were the most affected proteins. These proteins faded or disappeared as a function of the incubation time with both enzymes on SDS-PAGE. The molecular weight of actin was not, however, affected by either enzyme. The effects that the enzymes had on the gel formation of chicken-breast myofibrils were studied in 0.35 and 0.60 M NaCl solutions at 3% protein content and a constant temperature of 40 degrees C by using a small deformation viscoelastic measurement. TG substantially increased the storage modulus (G') of 3% protein in 0.35 M NaCl. Without the enzymes, gelation was insignificant in 0.35 M NaCl. The increased solubility of the proteins at 0.60 M NaCl intensified gelation with TG. G' increased 32 and 64% at dosages of 10 and 100 nkat of TG, respectively. Also, laccase increased G' of the gel in 0.60 M salt concentration. However, a high laccase dosage decreased the magnitude of G' below the control level. Differential scanning calorimetric (DSC) measurements indicated slightly reduced myosin heat stability after TG pretreatment and increased actin heat stability with both enzymes. Maximum transition temperatures did not alter with either enzyme.

A 7-week reduction in salt intake does not contribute to markers of bone metabolism in young healthy subjects.

BACKGROUND: Sodium intake increases urinary calcium excretion and may thus lead to negative calcium balance and bone loss. OBJECTIVE: We hypothesised that reducing sodium intake would reduce urinary calcium excretion and have a beneficial influence in bone metabolism. DESIGN: A total of 29 subjects, 14 males and 15 females, were divided into two study groups. One group (low-sodium group (LS)) reduced sodium intake for 7 weeks by substituting low-salt alternatives for the most important dietary sources of sodium. The other group, serving as a control group (C), was given the same food items in the form of normally salted alternatives. Fasting serum samples as well as 24-h urine samples were obtained in the beginning and at the end of the study. Urinary sodium, urinary calcium, urinary creatinine, serum calcium, serum phosphate, serum creatinine, serum parathyroid hormone (s-PTH), serum C-terminal telopeptides of Type-I collagen and serum bone alkaline phosphatase (s-B-ALP) were analysed. RESULTS: The LS group showed a significant decline (P = 0.001) in urinary sodium/creatinine ratio without a significant effect on urinary calcium/creatinine ratio. In the LS group, s-PTH increased (P = 0.03). The C group showed an increase in s-PTH (P = 0.05) and in s-B-ALP, but no differences were observed between the study groups in the changes of serum markers of calcium and bone metabolism. CONCLUSIONS: We have shown that reducing the sodium intake of young, healthy people with adequate calcium intake over a 7-week period does not affect the markers of bone metabolism.

Carbohydrate metabolism in meat animals.

Oxidative energy production is by far dominant in living animal muscles, with the exception the short periods of severe stress, where the aerobic capacity is exceeded, and formation of large amounts of lactate and protons will take place. Energy consumption in muscle cells continues post-mortem with formation of large amounts of lactate and protons, because the aerobic processes for energy production are not available. Post-mortem, the fall in pH is delayed only by buffering capacity of the muscle fibres. In living animals, in addition to buffering capacity, both respiration and transport of lactate and protons out of the muscle fibres by monocarboxylate transporters participate in the regulation of muscle fibre pH which never falls as low as the ultimate pH of the meat. Understanding the regulation of pH in muscle is important both for the welfare of living animals and from the technological point of view as a factor influencing meat quality.

Distribution of monocarboxylate transporter isoforms MCT1, MCT2 and MCT4 in porcine muscles.

AIM: Monocarboxylate transporters (MCT), which cotransport lactate anions and protons across cell membranes, are important for regulation of muscle pH. We measured amounts of MCT1, MCT2 and MCT4 by immunoblotting in five different porcine muscles, to study MCT-isoform distribution both in oxidative and highly glycolytic muscles. METHODS: Samples from the longissimus dorsi, gluteus superficialis, semimembranosus, infraspinatus and masseter were taken from 18 slaughtered pigs. RESULTS: Oxidative capacity, estimated on the basis of the activities of lactate dehydrogenase (LDH), citrate synthase (CS) and 3-OH-acyl-CoA dehydrogenase (HAD), was highest in the infraspinatus and masseter, and was very low in the gluteus, semimembranosus and longissimus dorsi. In all muscles, the amount of MCT1 was small but variable. The amount of MCT2 was more abundant in the glycolytic than in the oxidative muscles, while MCT4 was found in equal amounts in all muscles. MCT2, but not MCT4, correlated negatively with CS and HAD. CONCLUSIONS: The results together with measured concentrations of lactate suggest that MCT2 may function as the housekeeping lactate transporter, preventing acidification especially in highly glycolytic muscles in which the capacity to oxidize lactate is low. The results also support the view that, as in other species, MCT4 would be important at high lactate concentrations that occur during stress.