Fitness Seller

Milos Sarvec ... de contest prep goeroe

Bezoekers in dit topic

is idd veel beter met milos, hoewel zen benen percies kleiner zijn geworden, maar wel meer in verhouding, kuiten zijn wel goed verbeterd!
ik zie anders toch een HUGE verschil!
Charles Glass is een amateur, kijk wat hij Gunter heeft aangedaan. WORSE SHAPE EVER!!!

Dat zou ik nu ook weer niet durven zeggen, qua training en oefeningen kennis is er mijn inziens niemand beter. Contest prep en voeding houd hij zich volgens mij niet mee bezig. Dus als Gunter op een bepaalde wedstrijd een vettige vochtbal is, dan ligt dat niet aan Charles Glass. Als Gunter achterliggende spiergroepen had dan lag dat wel aan Glass...
Ja maar lage reps verhoogt het myostatine gehalte wat de spieropbouw tegengaat dus waar zit de logica dan? Ik train gewoon: eens 12 reps, 8 reps, 15 reps, 6 reps, door elkaar.

ik heb dat vaker gehoord inderdaad dat hoe hoger je in% van je max komt hoe meer myostatine word aangemaakt, maar heb geen idee hoe groot dat verschil is heb jij hier meer info over?
Myostatin info/studies:

Myostatin (a.k.a. GDF-8) ia a member of the TGF-beta family and is specific to skeletal muscles (not found in smooth or cardiac muscles). It is secreted in the inactive (propeptide) form and circulates in the blood. At some point the protein is activated via an as yet unknown mechanism. In vitro studies have pointed to tissue specific (skeletal muscle) metalloproteinases (just an enzyme that cleaves proteins) in the activation but in vivo mechs have not yet been demonstrated. In circulation it has been found to be bound by FLRG and GASP-1; which inhibit its action (Two possible mechs for future control of myostatin activity). Post activation myostatin can then bind to specific receptors on skeletal muscle and activate a signaling cascade which activates factors to regulate transcription of the myostatin target genes. It helps to regulate differentiation, proliferation, and fiber size.

Myostatin, or GDF-8 (growth and differentiation factor-8), was first identified through sequence identity with members of the BMP (bone morphogenetic protein)/TGF-β (transforming growth factor-β) superfamily. The skeletal-muscle-specific expression pattern of myostatin suggested a role in muscle development. Mice with a targeted deletion of the myostatin gene exhibit a hypermuscular phenotype. In addition, inactivating mutations in the myostatin gene have been identified in ‘double muscled’ cattle breeds, such as the Belgian Blue and Piedmontese, as well as in a hypermuscular child. These findings define myostatin as a negative regulator of skeletal-muscle developmentt. Myostatin binds with high affinity to the receptor serine threonine kinase ActRIIB (activin type IIB receptor), which initiates signalling through a smad2/3-dependent pathway. In an effort to validate myostatin as a therapeutic target in a post-embryonic setting, a neutralizing antibody was developed by screening for inhibition of myostatin binding to ActRIIB. Administration of this antimyostatin antibody to adult mice resulted in a significant increase in both muscle mass and functional strength. Importantly, similar results were obtained in a murine model of muscular dystrophy, the mdx mouse. Unlike the myostatin-deficient animals, which exhibit both muscle hypertrophy and hyperplasia, the antibody-treated mice demonstrate increased musculature through a hypertrophic mechanism. These results validate myostatin inhibition as a therapeutic approach to muscle wasting diseases such as muscular rdystrophy, sarcopenic frailty of the elderly and amylotrophic lateral sclerosis.

Purpose of review
Myostatin is an endogenous, negative regulator of muscle growth. Selective inhibition of myostatin may have broad clinical utility by improving regeneration in diverse and burdensome muscle disorders. An understanding of this potential is relevant because inhibitors of myostatin have recently entered clinical trials.
Recent findings: This article reviews the structure and function of myostatin, the effect of inhibiting myostatin in models of disease, and potential therapeutic approaches to blocking myostatin pharmacologically. The possibility that a myostatin inhibitor will promote muscle regeneration in human disease, as seen in animal models, is suggested by the observation that loss of myostatin results in muscle hypertrophy in a human subject.
Summary: Multiple approaches to inhibiting myostatin are suggested by the recent elucidation of its signaling pathway. An inhibitor of myostatin may be the first drug specifically designed to enhance muscle growth and regeneration.

Advances in recombinant DNA technology have created one of the most powerful weapons in the current doping arsenal: recombinant proteins [Sweeney HL. Gene doping. Sci Am 2004;291:62–9; Unal M, Ozer Unal D. Gene doping in sports. Sports Med 2004;34:357–62]. Recombinant erythropoietin (EPO) and human growth hormone (hGH) are currently being abused but are fortunately detectable either directly by employing isoelectric focusing and immunoassays or indirectly by assessing changes in selected hematopoietic parameters. The detection is technically demanding due to the extent of similarity between the recombinant proteins and their endogenous counterparts.
Another issue facing detection efforts is the speed and conditions at which blood samples are collected and analyzed in a sports setting. Recently, gene doping, which stemmed out of legitimate gene therapy trials, has emerged as the next level of doping. Erythropoietin (EPO), human growth hormone (hGH), insulin-like growth factor-1 (IGF-1), peroxisome proliferator-activated receptor-delta (PPAR δ), and myostatin inhibitor genes have been identified as primary targets for doping. Sports clinical scientists today are racing against the clock because assuring the continued integrity of sports competition depends on their ability to outpace the efforts of dopers by developing new detection strategies.

MEER over het verband tussen het aantal herhalingen en het myostatin gehalte in het bloed.

PURPOSE: Myostatin is a negative regulator of muscle mass and its effects seem to be exacerbated by glucocorticoids; however, its response to resistance training is not well known. This study examined 12 wk of resistance training on the mRNA and protein expression of myostatin, follistatin-like related gene (FLRG), activin IIb receptor, cortisol, glucocorticoid receptor, myofibrillar protein, as well as the effects on muscle strength and mass and body composition. METHODS: Twenty-two untrained males were randomly assigned to either a resistance-training [RTR (N = 12)] or control group [CON (N = 10)]. Muscle biopsies and blood samples were obtained before and after 6 and 12 wk of resistance training. RTR trained 3 x wk(-1) using three sets of six to eight repetitions at 85-90% 1-RM on lower-body exercises, whereas CON performed no resistance training. Data were analyzed with two- and three-way ANOVA. RESULTS: After 12 wk of training, RTR increased total body mass, fat-free mass, strength, and thigh volume and mass; however, they increased myostatin mRNA, myostatin, FLRG, cortisol, glucocorticoid receptor, and myofibrillar protein after 6 and 12 wk of training (P < 0.05). CONCLUSIONS: Resistance training and/or increased glucocorticoid receptor expression appears to up-regulate myostatin mRNA expression. Furthermore, it is possible that any plausible decreases in skeletal muscle function from the observed increase in serum myostatin were attenuated by increased serum FLRG levels and the concomitant down-regulation of the activin IIb receptor. It is therefore concluded that the increased myostatin in response to cortisol and/or resistance training appears to have no effects on training-induced increases in muscle strength and mass.

-> In deze studie deed men 6-8 herhalingen met een load van 85%-90% van de 1-RM. In deze studie was het myostatin gehalte gestegen door deze training.

Myostatin inhibits myoblast proliferation and differentiation in developing muscle. Mounting evidence suggests that myostatin also plays a limiting role in growth/repair/regeneration of differentiated adult muscle by inhibiting satellite cell activation. We tested the hypothesis that myostatin mRNA expression would decrease after resistance loading (RL) with a blunted response in older (O) females (F) who have shown minimal hypertrophy [vs. males (M)] after long-term RL. As myostatin is thought to modulate cell cycle activity, we also studied the response of gene transcripts key to stimulation (cyclin B1 and D1) and inhibition (p21cip and p27kip) of the cell cycle, along with the muscle-specific load-sensitive mitogen mechano-growth factor (MGF). Twenty young (Y; 20-35 yr, 10 YF, 10 YM) and 18 O (60-75 yr, 9 OF, 9 OM) consented to vastus lateralis biopsy before and 24 h after a bout of RL (3 sets x 8-12 repetitions to volitional fatigue of squat, leg press, knee extension). Gene expression levels were determined by relative RT-PCR with 18S as an internal standard and analyzed by age x gender x load repeated-measures ANOVA. A load effect was found for four transcripts (P < 0.005) including myostatin, cyclin D1, p27kip, and MGF as mRNA levels decreased for myostatin (-44%) and p27kip (-16%) and increased for cyclin D1 (34%) and MGF (49%). For myostatin, age x load and gender x load interactions (P < 0.05) were driven by a lack of change in OF, while marked declines were noted in YM (-56%), YF (-48%), and OM (-40%). Higher cyclin D1 levels in OF led to a main age effect (36%, O > Y) and an age x gender interaction (66%, OF > YF vs. 10%, OM > YM; P < 0.05). An age x gender x load interaction (P < 0.05) for cyclin D1 resulted from a 48% increase in OF. Post hoc testing within groups revealed a significant increase in MGF after RL in YM only (91%, P < 0.05). Higher levels of cyclin B1 in O (27%, O > Y) led to a main age effect (P < 0.05). An age x load interaction for cyclin B1 (P < 0.05) was driven by a 26% increase in Y with no change in O after RL. No age or gender differences, or load-mediated changes, were detected in levels of p21cip mRNA expression. These data clearly demonstrate that RL downregulates myostatin expression and alters genes key to cell cycle progression. However, failure to reduce myostatin expression may play a role in limiting RL-induced hypertrophy in OF.
-> In deze studie deed men 8-12 herhalingen en hier daalde het myostatin gehalte in het bloed.

Als je er vanuit gaat dat deze studies correct zijn dan kan je zeggen dat meer herhalingen het myostatin gehalte verminderen waardoor je meer spiermassa gaat aanzetten. Klinkt wel logisch als je weet dat de gemiddelde bodybuilder traint met veel herhalingen en minder gewicht en toch veel spiermassa heeft. Terwijl een powerlifter het tegenovergestelde doet en dus krachtiger is maar minder spiermassa heeft.
Laatst bewerkt:
op de Ironman staat hij er net ff ietsje beter bij hoor, de belichting en alles helpt ook mee, maar op zeker dat hij daar net ff voller en vasculairder is, no doubt.
Hij zag er duidelijk beter uit en nu hij niet meer met Milos werkt scoort hij hoger, strange :o
Hij zag er duidelijk beter uit en nu hij niet meer met Milos werkt scoort hij hoger, strange :o

je naam en je begeleider zijn belangrijker dan je shape;)

dat moet je nu ondertussen al weten he :D
Je naam ok, dat was idd al tijdje zo... maar als men nu zo ver al gaat van je lager te plaatsen omdat je begeleidt wordt door de (in IFBB termen) "verkeerde" mensen... wat n kloteboel...
waarom kakken ze op Milos? Omdat ze jaloers zijn omdat ze niet begeleid worden door hem. Ik zou meteen tekenen moest hij mij komen vragen om nog maar een maand mij te begeleiden.
Naar boven