Creatine and protein synthesis -
However, the total amount you can obtain from eating meat is rather small. This is why many people who are looking to increase muscle mass and performance take creatine supplements.
Creatine in supplement form is synthetically produced in a commercial laboratory. The most common form is creatine monohydrate, though other forms exist 1. Whey is one of the primary proteins found in dairy products.
In terms of protein quality, whey is at the top of the list, hence why its supplements are so popular among bodybuilders and other athletes. Consuming whey protein following a bout of exercise has been linked to enhanced recovery and increased muscle mass. These benefits can help improve strength, power, and muscular function 3 , 4.
Getting in a good source of protein after resistance exercise is important for maximizing muscle-building. About 20—25 grams of protein is a good amount to aim for 3. Whey protein powder can be an efficient way to meet this recommendation, considering a typical gram serving provides around 20 grams of protein.
Creatine is an organic compound that, when taken as a supplement, can help increase muscle mass, strength, and exercise performance. Whey protein is a dairy protein commonly consumed with resistance exercise to increase muscle mass and strength.
Both creatine and whey protein powder have been shown to increase muscle mass when taken in combination with resistance exercise 1 , 3.
Creatine increases exercise capacity during high-intensity exercise. This leads to improved recovery and adaptations such as increased muscle mass 1. Meanwhile, ingesting whey protein in combination with exercise provides your body a high-quality source of protein , enhancing muscle protein synthesis and leading to increased muscle gains over time 3.
While both creatine and whey protein promote muscle gain, they differ in the ways they work. Creatine increases strength and muscle mass by increasing exercise capacity, whereas whey protein does so by stimulating increased muscle protein synthesis.
Both whey protein powder and creatine supplements have been shown to increase muscle mass, though they accomplish this in different ways. Some people have proposed that taking whey protein and creatine together may lead to benefits beyond those associated with taking either one alone.
One study in 42 middle-aged and older men found that participants did not experience any additional training adaptations when they took both whey protein and creatine, compared with taking either supplement alone 5.
Additionally, a study in 18 resistance-trained women found that those who took whey protein plus creatine for 8 weeks experienced no difference in muscle mass and strength than those who took whey protein alone 6. The results seem to suggest there is no added benefit of taking whey protein and creatine together.
However, some people may decide to take them together for convenience 7. Additionally, no evidence suggests that taking creatine and whey protein at the same time causes any negative effects. Choosing whether to take whey protein, creatine, or both comes down to your individual goals.
If you are a recreational gym-goer just looking to stay in shape, whey protein may be a good option to aid muscle building and recovery.
On the other hand, if you are looking to maximize muscle mass and strength, it may be beneficial to take both whey protein and creatine. Studies have observed that taking whey protein and creatine together with exercise offers no additional muscle or strength gains than taking each individually.
Taking either alone likely provides the same benefits. The growing fetus relies at least partially on the maternal supply of creatine via the placenta, but after birth the newborn must rely on endogenous synthesis 6 , 8 , 9.
It remains to be determined whether the prematurely born infant has the capacity to synthesize creatine effectively, particularly if a dietary creatine source is not supplied.
Following preterm birth, total parenteral nutrition PN is often required as a means of nutritional support for infants with gastrointestinal disorders or prolonged intolerance of enteral feeding. However, creatine is not a component of pediatric PN products. In this situation, the entire creatine requirement must be met by de novo synthesis, which must create considerable demand for the amino-acid precursors, arginine and methionine.
Arginine is a conditionally essential amino acid for neonates, although de novo arginine synthesis does occur in the small intestinal mucosa during first-pass metabolism, predominantly from dietary proline 10 , 11 , PN feeding bypasses the gut metabolism and thus causes gut atrophy; therefore, PN feeding interferes with normal arginine synthesis, and whether this affects optimal creatine accretion in the growing neonate has not yet been investigated.
The neonatal period is characterized by rapid growth and very high rates of protein synthesis to support the growth. Compromised de novo arginine synthesis during PN feeding, as well as an increased demand for arginine to support creatine synthesis, may limit arginine availability for protein synthesis.
Alternatively, the sparing of arginine through the provision of preformed creatine in PN may lead to enhanced protein synthesis in growing neonates. We hypothesized that the addition of creatine to PN would reduce the need for de novo creatine synthesis and spare arginine for protein synthesis in a PN-fed piglet model.
Fourteen Yucatan miniature piglets 3—5days old were obtained from the breeding herd Animal Care Services, Memorial University of Newfoundland as littermate pairs. The animals immediately underwent surgical implantation of two silastic venous catheters jugular and femoral under general anesthesia.
Detailed descriptions of the surgical procedure and post-surgical care were published elsewhere Immediately following surgery, the piglets were housed individually in metabolic cages with a single-port swivel and a tether system Lomir Biomedical, Notre-Dame-de-l'Île-Perrot, QC, Canada that facilitates continuous PN feeding while allowing the piglets to move freely.
The piglets were weighed each morning and diet infusion rates were adjusted daily according to the piglet body weight. Five additional piglets were identified in the herd but were left with the sow until the end of the study. These piglets were of similar age to the catheterized piglets, but were not littermates.
Piglets were randomized to either creatine-supplemented PN Creatine or creatine-free PN Control. Both diets provided similar amounts of the total amino acids Sigma-Aldrich, Oakville, ON, Canada; Supplementary Table S1 online.
Creatine-supplemented piglets received 0. The diets provided 0. Piglets were maintained on the same PN for 14 days. After 14 days, a flooding dose of L-phenylalanine 1.
Thirty minutes after dosing, the piglets were anesthetized with halothane and were delivered with oxygen by a mask. Samples of brain, skeletal muscle, and liver were also removed and frozen for the analysis of creatine and GAA concentrations.
Small intestinal mucosa, liver, and skeletal muscle samples were taken to analyze the rates of protein synthesis. The five SF piglets underwent the same necropsy protocol for the purpose of establishing SF reference data.
Creatine concentration of the gastrocnemius muscle was determined using the simplified method of Lamarre et al. Creatine was eluted with an isocratic mobile phase of 0. The total creatine concentrations were determined by reference to a standard curve that was run with the samples.
AGAT activity was assayed using a modified method of Van et al. The assay measured the amount of ornithine converted from arginine because of AGAT activity transamidinase.
The whole kidney was pulverized and a representative sample was used to measure the activity of transamidinase. The protein content of the homogenates was assayed using the Pierce BCA protein assay kit Thermo Fisher Scientific, Mississauga, ON, Canada.
Ornithine produced by AGAT was presented as nmol of ornithine per mg of protein per min. GAMT activity was assayed, as described previously by da Silva et al. Creatine synthesized by GAMT activity was measured via HPLC and ninhydrin derivatization 15 and activity was expressed per mg of protein per min.
The isotopic enrichment of L-[ring- 2 H 5 ] phenylalanine in tissue-free and protein-bound fractions was determined by gas chromatography-mass spectrometry and pentafluorobenzyl bromide PFBBr derivative Sigma-Aldrich with a model GC linked to a N quadrupole MS Agilent Technologies operating in the electron ionization mode A mixed sample of L-[ring- 2 H 5 ] phenylalanine and unlabeled phenylalanine was run in the scan mode, in which 91 and 96 ions or and were identified as potential ions.
A standard curve was run before analyzing the samples to identify the linear ranges. Ions with a mass-to-charge ratio of 91 and 96 ions were monitored via selected-ion monitoring for the liver, small intestinal mucosa, and muscle tissues; for kidney and pancreas samples, and ions were monitored.
Tissues were homogenized as previously described Plasma- and tissue-free amino-acid concentrations were measured with reverse-phase HPLC C18 column , following the derivatization with phenylisothiocyanate Waters, Woburn, MA , as per the method of Bidlingmeyer et al. Lipid was extracted using the method of Folch et al.
Extracted lipid from triplicate liver samples was dried under nitrogen gas and weighed to quantify the lipid content. The data are expressed as means±SD. Data collected from the SF reference group were used for reference only and were not included in the statistical analyses, as this group was not treated identically to the treatment groups i.
SF reference group means±SD are presented for comparison purposes. The liver GAMT activity in the SF piglets was quite variable Figure 2. AGAT enzyme activity in kidney and pancreas tissues.
a kidney and b pancreas. AGAT, L-arginine:glycine amidinotransferase. GAMT enzyme activity in the liver. The values are expressed as means±SD. GAMT, guanidinoacetate N -methyltransferase. GAA concentrations in the kidney, pancreas, liver, and the brain did not differ between treatment groups Table 1.
The kidney and pancreas GAA concentrations were highly variable in both treatment groups Table 1. GAA concentrations were comparable to SF reference piglets for most tissues, except the liver where the mean concentration in the SF group was approximately twice that of the experimental piglets Table 1.
Creatine supplementation resulted in significantly higher creatine concentrations in the kidney, pancreas, and liver compared with the Control group Table 2.
Total creatine content i. SF pigs tended to have creatine concentrations between those of the treatment groups for most tissues.
Lack of creatine in Control piglets did not alter GAA Table 1 or creatine Table 2 concentrations in the brain. Furthermore, the mean brain GAA and creatine concentrations measured in both Creatine and Control groups were within the SF reference range Tables 1 and 2. Creatine supplementation resulted in a significantly lower plasma GAA concentration Table 1 , but in a higher creatine concentration Table 2 compared with Control pigs.
Liver and kidney fractional protein synthesis rates were significantly higher in Creatine piglets compared with those in the Control group Figure 3. There were no differences in protein synthesis rates in the pancreas, small intestinal mucosa, or skeletal muscle between experimental groups Figure 3.
Tissue-specific rates of protein synthesis. a the liver, b kidneys, c pancreas, d small intestinal mucosa, and e in the skeletal muscle.
SI, small intestine. No differences in free amino-acid concentrations between treatments were found in the liver or kidney tissues Supplementary Tables S4 and S5. Liver cholesterol in the Creatine piglets was significantly lower than in the Control group Table 3. However, the TG concentration, total lipid, or liver weights were not different between the groups.
Regardless of the treatment, both PN-fed groups had liver weights, liver lipid concentrations, and liver TG concentrations that were 1. Plasma cholesterol and TG were not different between the treatment groups.
However, the mean cholesterol SF value was approximately two times higher than that of the PN-treated piglets. The mean plasma TG concentrations measured in the two PN-treated groups were within the range of values measured in the SF piglets Table 3.
In PN-fed piglets, arginine synthesis is diminished with gut atrophy 10 , and we demonstrated that tissue creatine concentrations were proportionate to the intravenous arginine delivery unpublished data , suggesting that the availability of arginine limited de novo creatine synthesis.
In this study, we hypothesized that the addition of creatine to PN would spare arginine for protein synthesis. Indeed, an important finding is that liver and kidney protein synthesis was higher with creatine supplementation.
However, there was no difference in muscle protein synthesis. The concentration of arginine supplied in the PN diet was designed to be lower than that necessary to maximize protein synthesis in the muscle 14 to allow spared arginine to affect muscle protein synthesis; however, the amount of arginine spared by creatine was not conveyed to the muscle.
In the liver, the enhanced protein synthesis may be due to greater arginine availability, but this was not demonstrated by liver-free arginine concentrations, which were not different between the treatment groups. A similar situation occurred in the kidney, with greater protein synthesis but no difference in free arginine concentrations.
However, free concentrations are not necessarily reflective of arginine availability; it may be that arginine turnover was more rapid in the Creatine group, directing more arginine toward protein synthesis without changing the free concentrations. This possibility could be clarified with a tracer study to quantify arginine flux rates.
Alternatively, creatine may increase tissue protein synthesis via the mechanisms unrelated to arginine. In vitro and in vivo studies have identified a number of mechanisms by which creatine stimulates protein synthesis in the muscle.
Myogenic cells in culture exposed to oxidative stress have diminished proliferation and differentiation, and creatine attenuated these effects Creatine also upregulates the expression of a number of trophic factors in the muscle, including IGF-1, which can stimulate protein synthesis through the activation of mTOR pathway intermediates To our knowledge, none of these mechanisms related to creatine have been studied in the liver or the kidney.
The lack of response to creatine in muscle may have been due to the limited amino-acid substrate in that tissue, or due to the relatively low dose of creatine used in this study compared with human supplementation trials. Creatine kinase activity is found in the cytoplasm of several tissues, including the skeletal muscle, cardiac muscle, and the brain.
We hypothesized that 2 weeks of creatine supplementation to PN would increase skeletal muscle and brain creatine concentrations. Interestingly, the skeletal muscle total creatine concentration was higher in our creatine-fed piglets; however, we found no difference in the brain creatine concentrations, and both groups were similar to SF reference piglets.
However, adequate brain creatine must be of physiological importance, as profound negative neurodevelopmental effects have been reported secondary to inborn errors of creatine synthesis or transport 26 ; thus, creatine is critical to normal neurological developmental processes in neonates.
Previously, we reported that the brain AGAT activity was not detected, and GAMT activity was very low in neonatal piglets 6. Alternatively, it may be that the brain creatine pool was not measurably affected during the short-term use of creatine-free PN.
The rate of creatine degradation in the neonatal brain is also unknown but is likely very slow. In infants with AGAT deficiency, neurological symptoms do not become apparent until the second year of life Thus, brain creatine likely degrades too slowly to create a deficit after only 14 days of creatine-free PN.
With the addition of dietary creatine, downregulation of creatine synthesis was evident by a lower AGAT activity in the kidney and pancreas, as well as by lower GAA concentrations in plasma.
AGAT has been demonstrated as the rate-limiting step in creatine biosynthesis in humans 28 and in rodents 7 , 17 , 29 , 30 as creatine feeding induced a lower AGAT activity with no change in the liver GAMT activity. Similarly, in our piglets, the AGAT activity was affected with a dietary supply of creatine, and the liver GAMT activity did not change.
Therefore, it appears that creatine synthesis is regulated at the level of AGAT in neonatal piglets as well. The kidney has been identified as the major organ responsible for GAA synthesis in rodents 5. However, considering that piglet kidneys are approximately four times the mass of the pancreas 6 , the kidneys are likely still the organ responsible for the most of endogenous GAA synthesis in neonatal piglets.
Although the pancreas has a higher AGAT-specific activity than the kidney, its GAMT-specific activity is relatively low i. Therefore, the high pancreatic AGAT-specific activity may contribute some GAA directly to the liver for creatine synthesis, although this requires confirmation.
Because prolonged PN can lead to hepatic fat accumulation and PN-associated liver disease 31 , we also measured lipid parameters in the liver as a secondary objective. As expected, the PN-fed groups had a higher liver lipid content and heavier livers compared with those of SF piglets of the same age.
Lipid accumulation in the liver has been associated with impaired methionine metabolism Both phosphatidyl choline PC and creatine synthesis require hepatic methylation reactions, which rely on an adequate methionine pool to serve as a methyl donor.
Moreover, adequate PC synthesis is required for very low density lipoprotein assembly and secretion of lipids from the liver. It is possible that creatine supplementation might spare methionine for transmethylation to PC, thereby reducing liver lipids in this PN-fed model.
We found that creatine supplementation lowered the total liver cholesterol concentration, but no differences in liver weight or TG concentration were detected.
While creatine supplementation may have enhanced PC synthesis, allowing for more efficient transport of cholesterol out of the liver, it is unclear why total lipids or TGs were also not measurably reduced.
An in vivo electrical stimulation protocol was used for determination of muscle contractile activity. For twitch force analysis, the stimulus consisted of μs pulse at 1 Hz with adjusted voltage to produce maximum force.
Electrical stimulus frequency was increased to Hz to determine the tetanic force. Ten 1-s successive tetanic contractions at Hz allowed the determination of fatigue resistance, with 10 s of recovery between them, by measuring the decrease in force production during the experimental protocol used.
Maximal twitch and tetanic forces were recorded using the AqDados software version 4. Muscle strength and fatigue resistance were analyzed using the AqAnalysis software version 4. We used a similar procedure in previous studies 28 Fortes MA, Pinheiro CH, Guimaraes-Ferreira L, Vitzel KF, Vasconcelos DA, Curi R.
Overload-induced skeletal muscle hypertrophy is not impaired in STZ-diabetic rats. Physiol Rep ; 3. Serial sections were taken from the central portion of the soleus and EDL muscles according to Bodine and Baar 29 Bodine SC, Baar K.
Analysis of skeletal muscle hypertrophy in models of increased loading. Methods Mol Biol ; —, doi: The slides were stained with hematoxylin and eosin HE for analysis of CSA of the soleus and EDL muscles fibers fibers per muscle.
Photographs were taken using an optical microscope Nikon Eclipse E, Japan attached to a digital camera Nixon DXM The images were analyzed using the AxioVision program version 4. We used the same measurements in a previous study 2 2.
We used a similar procedure in previous studies 2 2. Fortes MA, Marzuca-Nassr GN, Vitzel KF, da Justa Pinheiro CH, Newsholme P, Curi R. Housekeeping proteins: How useful are they in skeletal muscle diabetes studies and muscle hypertrophy models? Anal Biochem ; 38—40, doi: Total RNA was extracted from skeletal muscles using RNeasy RNA isolation kit Qiagen Inc, USA according to the manufacturer's protocol and as used in our previous study 28 The following genes were evaluated: FST follistatin ; MSTN myostatin ; FAK focal adhesion kinase ; IGF-1 insulin-like growth factor ; MGF mechano growth factor ; Akt ; mTOR mammalian target of rapamycin ; atrogin-1 , and MuRF1.
The primers sequences used in the experiments are displayed in Supplementary Table S1. Statistical analysis was performed using the GraphPad Prism ® software version 4. Results are reported as means±SE and were analyzed by two-way analysis of variance ANOVA followed by the Bonferroni post-hoc test for comparison between three or more groups.
Outlier results were detected using the Grubbs' test of GraphPad Software graphpad. The HS group had lower body weight than the other groups after 5 days of experiment Table 1.
Creatine supplementation had an effect on preventing muscle mass loss that was more notable in the EDL muscle, in the rats submitted to HS Table 1. The absolute twitch force in the soleus and EDL muscles and the specific tetanic force in the EDL muscle were not changed as indicated by the inter-group analysis.
The specific twitch force and fatigue resistance did not change significantly in the soleus and EDL muscles due to either creatine supplementation or HS Figure 1A and 2A. S6 and p-S6 protein contents were not altered by HS or supplementation Figure 1B d,e,f. The p-4EBP1 content was not significantly changed in the inter-group analysis.
In the EDL muscle, the contents of phosphorylated and total Akt and GSK3B proteins did not change after the HS or creatine supplementation Figure 2B.
The CSA of the EDL muscle fibers did not change due to HS in both groups compared to non-HS Figure 3B. Creatine supplementation did not alter muscle fiber CSA in both soleus and EDL muscles. The expressions of MSTN , FAK , IGF-1 , MGF , and Akt did not change in soleus muscle after the HS or with creatine supplementation Supplementary Figure S1A.
In the EDL muscle, the expressions of FST , IGF , Akt , and MuRF1 also did not change after the HS period or creatine supplementation Supplementary Figure S1B.
We investigated the effects of short-term creatine supplementation on skeletal muscle mass and strength and signaling pathways associated with protein synthesis or degradation in rats submitted to HS-induced atrophy.
Despite the attenuating effects on protein metabolism signaling changes induced by HS, creatine supplementation, started concomitantly with HS, slighted prevented the decrease in skeletal muscle mass but had no effect on muscle CSA and strength after five days of muscle disuse main results observed in this study are in Figure 5.
The mentioned findings may be associated to the length of the supplementation period, the intensity of the muscle disuse atrophy, or the dose of creatine. Although, in the current study, creatine and phosphocreatine contents were not measured in the target muscles, the supplementation protocol used was reported to increase creatine content in type I fiber-rich muscles such as the soleus.
The already described switch of type I to type II fibers during HS 31 Baldwin KM, Haddad F, Pandorf CE, Roy RR, Edgerton VR. Front Physiol ; 4: , doi: may affect creatine accumulation in soleus muscle.
The content of total creatine is dependent on the skeletal muscle fiber type. Type II fibers have higher levels of creatine and phosphocreatine. Therefore, creatine uptake and accumulation is a muscle fiber type-dependent process 9 9.
Persky AM, Brazeau GA. Clinical pharmacology of the dietary supplement creatine monohydrate. Pharmacol Rev ; — Willott CA, Young ME, Leighton B, Kemp GJ, Boehm EA, Radda GK, et al.
Creatine uptake in isolated soleus muscle: kinetics and dependence on sodium, but not on insulin. Acta Physiol Scand ; 99—, doi: More intense atrophy due to HS was found in the soleus muscle based on the percentage of decrease in muscle mass and muscle fibers CSA, as also previously reported 1 1.
To evaluate protein synthesis signaling Akt-mTOR-S6 , we analyzed the phosphorylation and activation of the key upstream enzyme Akt and the phosphorylation of the S6 protein as a downstream signaling of mTOR activation. The activation of this pathway contributes to an increase in skeletal muscle mass by stimulating protein synthesis.
This pathway also inhibits the activation of MuRF1 and atrogin-1 , associated with the activation of the ubiquitin-proteasome degradation pathway, and promotes an inhibition of phosphorylation of GSK3b and 4EBP1 that can act as repressors of protein translation 33 Bonaldo P, Sandri M.
Cellular and molecular mechanisms of muscle atrophy. Dis Model Mech ; 6: 25—39, doi: In the soleus muscle, HS reduced p-Akt content, which is one of the main activators of mTOR complex. HS did not change p-S6 protein but enhanced p-4EBP1 protein.
The lowered phosphorylation and inhibition of GSK3B followed the lower activation of its upstream kinase Akt. Activation of GSK3B leads to inhibition of eukaryotic translation initiation factor 2 beta eIF2β and to suppression of protein translation.
Degradation pathway may be enhanced as indicated by increased atrogin-1 mRNA expression. The lowered phosphorylation of Akt stops inhibiting FoXO protein and increases the atrogin-1 content, which is an activating factor of the ubiquitin-proteasome pathway 34 Bodine SC, Baehr LM.
Am J Physiol Endocrinol Metab ; EE, doi: Even though FST is associated with muscle hypertrophy by inhibiting myostatin , our findings agreed with another study that reported an increase of this marker at the beginning of the HS period 35 Stevenson EJ, Giresi PG, Koncarevic A, Kandarian SC.
Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle. J Physiol ; 33—48, doi: Creatine supplementation reduced FST and increased atrogin-1 expression during HS.
Creatine supplementation had no marked hypertrophic effects in the soleus muscle. Conversely, it promoted an attenuation of the increase in FST expression and a greater increase in MuRF1 expression due to HS.
Based on these findings, creatine would not be expected to markedly attenuate soleus muscle atrophy under the experimental conditions investigated. Indeed, soleus muscle atrophy, evaluated by muscle mass and fiber size, was not significantly different between groups.
The mentioned findings also contributed to the lack of significant creatine effect on preventing leg muscle strength decrease induced by HS. The EDL muscle suffered less atrophy than the soleus due to HS, which is in accordance with previous studies 1 1.
This was reflected in the molecular analysis as well, with few changes induced by HS, including the reduction of p-S6 protein content and increase of MSTN expression.
Myostatin is a member of the transforming growth factor-beta TGF-β family that acts on muscle mass control 36 McPherron AC, Lawler AM, Lee SJ.
Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature ; 83—90, doi: This factor activates ubiquitin ligases and proteasome proteolysis 37 Lokireddy S, McFarlane C, Ge X, Zhang H, Sze SK, Sharma M, et al.
Myostatin induces degradation of sarcomeric proteins through a Smad3 signaling mechanism during skeletal muscle wasting. Mol Endocrinol ; —, doi: Trendelenburg AU, Meyer A, Rohner D, Boyle J, Hatakeyama S, Glass DJ.
Am J Physiol Cell Physiol ; CC, doi: In opposition to the soleus, promising effects of creatine on reduction of EDL muscle mass loss were found; the supplementation increased FAK expression.
We speculate that the increase in the expression of FAK could produce an increase in the activation of this marker. Fak, an enzyme involved in the mechanical signaling associated with skeletal muscle hypertrophy, has the ability to phosphorylate p70S6K1 in Tyr , independently of Akt and mTOR 39 Klossner S, Durieux AC, Freyssenet D, Flueck M.
Mechano-transduction to muscle protein synthesis is modulated by FAK. In the same line, creatine supplementation reversed the S6 phosphorylation trend changes, which tended to decrease with HS but it was increased by concomitant creatine supplementation.
These effects were not enough to counteract EDL mass loss induced by HS in the period studied but they may represent an advantage for muscle recovery after facing an atrophy-promoting condition.
An increased expression of FAK may not be important during HS because there is no mechanical loading to elicit marked FAK expression.
In fact, Hespel et al. concluded that creatine supplementation improves muscle mass recovery during rehabilitation using resistance training after a period of 2 weeks of immobilization in young healthy volunteers. Along with our study, other authors investigated the effects of creatine supplementation starting concomitantly with distinct atrophic models such as dexamethasone treatment 17 or immobilization 19 Hespel et al.
Cayenne pepper and cancer suggest there is no added benefit of taking whey Gut-friendly recipes and creatine together. But both contain different orotein and Creatine and protein synthesis differently. In the world wynthesis sports nutrition, people use Anc supplements to increase their performance and enhance exercise recovery. Creatine and whey protein are two popular examples, with a great deal of data backing their effectiveness. While their effects are similar in some regards, they are distinctly different compounds that work in different ways. This article reviews what creatine and whey protein powder are, their main differences, and whether you should take them together for optimal benefits. Creatine is an organic compound produced naturally in your muscle cells.
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