27
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Lactate, Fructose and Glucose Oxidation Profiles in Sports Drinks and the Effect on Exercise Performance

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Exogenous carbohydrate oxidation was assessed in 6 male Category 1 and 2 cyclists who consumed CytoMax™ ( C) or a leading sports drink ( G) before and during continuous exercise (CE). C contained lactate-polymer, fructose, glucose and glucose polymer, while G contained fructose and glucose. Peak power output and VO 2 on a cycle ergometer were 408±13 W and 67.4±3.2 mlO 2·kg −1·min −1. Subjects performed 3 bouts of CE with C, and 2 with G at 62% VO 2peak for 90 min, followed by high intensity (HI) exercise (86% VO 2peak) to volitional fatigue. Subjects consumed 250 ml fluid immediately before (−2 min) and every 15 min of cycling. Drinks at −2 and 45 min contained 100 mg of [U- 13C]-lactate, -glucose or -fructose. Blood, pulmonary gas samples and 13CO 2 excretion were taken prior to fluid ingestion and at 5,10,15,30,45,60,75, and 90 min of CE, at the end of HI, and 15 min of recovery. HI after CE was 25% longer with C than G (6.5±0.8 vs. 5.2±1.0 min, P<0.05). 13CO 2 from the −2 min lactate tracer was significantly elevated above rest at 5 min of exercise, and peaked at 15 min. 13CO 2 from the −2 min glucose tracer peaked at 45 min for C and G. 13CO 2 increased rapidly from the 45 min lactate dose, and by 60 min of exercise was 33% greater than glucose in C or G, and 36% greater than fructose in G. 13CO 2 production following tracer fructose ingestion was greater than glucose in the first 45 minutes in C and G. Cumulative recoveries of tracer during exercise were: 92%±5.3% for lactate in C and 25±4.0% for glucose in C or G. Recoveries for fructose in C and G were 75±5.9% and 26±6.6%, respectively. Lactate was used more rapidly and to a greater extent than fructose or glucose. CytoMax significantly enhanced HI.

          Related collections

          Most cited references50

          • Record: found
          • Abstract: found
          • Article: not found

          Role of mitochondrial lactate dehydrogenase and lactate oxidation in the intracellular lactate shuttle.

          To evaluate the potential role of mitochondrial lactate dehydrogenase (LDH) in tissue lactate clearance and oxidation in vivo, isolated rat liver, cardiac, and skeletal muscle mitochondria were incubated with lactate, pyruvate, glutamate, and succinate. As well, alpha-cyano-4-hydroxycinnamate (CINN), a known monocarboxylate transport inhibitor, and oxamate, a known LDH inhibitor were used. Mitochondria readily oxidized pyruvate and lactate, with similar state 3 and 4 respiratory rates, respiratory control (state 3/state 4), and ADP/O ratios. With lactate or pyruvate as substrates, alpha-cyano-4-hydroxycinnamate blocked the respiratory response to added ADP, but the block was bypassed by addition of glutamate (complex I-linked) and succinate (complex II-linked) substrates. Oxamate increased pyruvate (approximately 10-40%), but blocked lactate oxidation. Gel electrophoresis and electron microscopy indicated LDH isoenzyme distribution patterns to display tissue specificity, but the LDH isoenzyme patterns in isolated mitochondria were distinct from those in surrounding cell compartments. In heart, LDH-1 (H4) was concentrated in mitochondria whereas LDH-5 (M4) was present in both mitochondria and surrounding cytosol and organelles. LDH-5 predominated in liver but was more abundant in mitochondria than elsewhere. Because lactate exceeds cytosolic pyruvate concentration by an order of magnitude, we conclude that lactate is the predominant monocarboxylate oxidized by mitochondria in vivo. Mammalian liver and striated muscle mitochondria can oxidize exogenous lactate because of an internal LDH pool that facilitates lactate oxidation.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Active muscle and whole body lactate kinetics after endurance training in men.

            We evaluated the hypotheses that endurance training decreases arterial lactate concentration ([lactate](a)) during continuous exercise by decreasing net lactate release () and appearance rates (R(a)) and increasing metabolic clearance rate (MCR). Measurements were made at two intensities before [45 and 65% peak O(2) consumption (VO(2 peak))] and after training [65% pretraining VO(2 peak), same absolute workload (ABT), and 65% posttraining VO(2 peak), same relative intensity (RLT)]. Nine men (27.4 +/- 2.0 yr) trained for 9 wk on a cycle ergometer, 5 times/wk at 75% VO(2 peak). Compared with the 65% VO(2 peak) pretraining condition (4.75 +/- 0.4 mM), [lactate](a) decreased at ABT (41%) and RLT (21%) (P < 0.05). decreased at ABT but not at RLT. Leg lactate uptake and oxidation were unchanged at ABT but increased at RLT. MCR was unchanged at ABT but increased at RLT. We conclude that 1) active skeletal muscle is not solely responsible for elevated [lactate](a); and 2) training increases leg lactate clearance, decreases whole body and leg lactate production at a given moderate-intensity power output, and increases both whole body and leg lactate clearance at a high relative power output.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Colocalization of MCT1, CD147, and LDH in mitochondrial inner membrane of L6 muscle cells: evidence of a mitochondrial lactate oxidation complex.

              Results of previous studies suggested a role of mitochondria in intracellular and cell-cell lactate shuttles. Therefore, by using a rat-derived L6 skeletal muscle cell line and confocal laser-scanning microscopy (CLSM), we examined the cellular locations of mitochondria, lactate dehydrogenase (LDH), the lactate-pyruvate transporter MCT1, and CD147, a purported chaperone protein for MCT1. CLSM showed that LDH, MCT1, and CD147 are colocalized with the mitochondrial reticulum. Western blots showed that cytochrome oxidase (COX), NADH dehydrogenase, LDH, MCT1, and CD147 are abundant in mitochondrial fractions of L6 cells. Interactions among COX, MCT1, and CD147 in mitochondria were confirmed by immunoblotting after immunoprecipitation. These findings support the presence of a mitochondrial lactate oxidation complex associated with the COX end of the electron transport chain that might explain the oxidative catabolism of lactate and, hence, mechanism of the intracellular lactate shuttle.
                Bookmark

                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                PLoS ONE
                plos
                PLoS ONE
                Public Library of Science (San Francisco, USA )
                1932-6203
                2007
                26 September 2007
                : 2
                : 9
                : e927
                Affiliations
                [1]Exercise Biology Laboratory, Department of Kinesiology, California State University Chico, Chico, California, United States of America
                University of Louisville, United States of America
                Author notes
                * To whom correspondence should be addressed. E-mail: JLAzevedo@ 123456csuchico.edu

                Conceived and designed the experiments: JA. Performed the experiments: JA ET TT JP. Analyzed the data: JA KC. Contributed reagents/materials/analysis tools: JA. Wrote the paper: JA.

                Article
                07-PONE-RA-01316R1
                10.1371/journal.pone.0000927
                1976551
                17895968
                e2e2364d-3f29-4039-b59e-20c47105efed
                Azevedo Jr, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                : 16 May 2007
                : 5 September 2007
                Page count
                Pages: 8
                Categories
                Research Article
                Nutrition
                Biochemistry/Membrane Proteins and Energy Transduction
                Physiology/Muscle and Connective Tissue

                Uncategorized
                Uncategorized

                Comments

                Comment on this article