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Diario Azzyz Rumo Aos Palcos Em 2014 Ec On (70 Dias Para Perder 4 Kilos)Contagem Regressiva


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os artigos são com base em o que fisiculturistas que estão usando doses monstrar de trembolona, gh, insulina, testo, etc

eles tem uma sintese proteica milhões de vezes maior que a nossa falam :D

só vejo motivo para usar prot em 2,2gr/kg+ em dietas cetogenicas como falei antes, pois uma parte vai sofrer gliconeogênese

fora isso, estou em cutting fazem 2 mêses ou mais (contando com a fase de adaptação) e até agora mantive as proteinas em 1,7-2gr/kg, não tive perda alguma de massa muscular.

Editado por Matheus_

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http://bodybuilding-is-life.blogspot.com.br/2011/04/dieta-para-cutting-sem-perda-de-massa.html

foi o primeiro post q coloquei no google pesquise hehe' nao adianta tentar provar nada..cada um faz o que lhe faz ter mais resultados..por mim eu matei o assunto.

abraços

Mais um topic...nao aguentei rsrs..

http://musculacaobrasil.forumeiros.org/t276-fixo-como-montar-uma-dieta-para-perda-de-gordura-cutting

Tudo detalhado nesse ultimo....

Meu amigo LUCASGFRANGAO quase me mate qnd falei que ia comer 3g ..ele ''Só isso em cutting''?? rsrs

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Cara como disse o fe rato , quando for se embasar em algo procure o artigo de alguém com um bom nome em sua área não algo do blog do fulano e tal , muitas vezes é alguém relatando algo empírico testado em si mesmo , mas todo mundo aqui sabe que você vai emagrecer comendo 3 ou 2g de prot por kilo e de ambas maneiras vai segurar massa mas uma das duas tem que ser a melhor , e é ai que entra pesquisas sérias feitas por pessoas renomadas

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na verdade eu axo q ai entra pesquisas seriaas feitas no proprio corpo...estudo nenhum garante que seus receptores ,metabolismo e demais funções sejam a ideais para algo especifico...so coloquei duas ''referencias'' de que isso nao é nenhuma loucura..3g de proteinas. enfim..continuarei acompanhando.Agora sim parei de falar sobre rs

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1- Proteina não mantém metabolismo algum acelerado, alias, o seu metabolismo é de um jeito a cada dia, não tem como calcular a velocidade de metabolismo nenhum. O maximo que se pode dizer sobre proteina nesse quisito, é que, sua termogense é maior, logo gasta mais kcal pra ser digerida, e é mais saciante.

2-3g de proteina pra quem é natural é um exagero, além de voce ficar eliminando o excesso pela urina (proteriuna ou proteurina , algo do tipo) , voce corre o risco de saturar o mTOR(Hormonio responsavel pela sintesse proteica) e de quebra, ocorrer o processo de gliconeogense (aminoacidos convertido em glicose) .

:handlebars:

Bota fonte ae ferato, vlw.

Postado

ja vi o ney felipe afirmar q mais q 2g/kg de proteina oxida a maior parte tb , porem conheço gente q usa 6g/kg de proteina com 85 kg masssss os ganhos dele n é fora do normal nao viu ... entao vai saber

Postado

O processo, de gliconeogenese.

Gluconeogenesis (abbreviated GNG) is a metabolic pathway that results in the generation of glucose from non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.

It is one of the two main mechanisms humans and many other animals use to keep blood glucose levels from dropping too low (hypoglycemia). The other means of maintaining blood glucose levels is through the degradation of glycogen(glycogenolysis).[1]

Gluconeogenesis is a ubiquitous process, present in plants, animals, fungi, bacteria, and other microorganisms.[2] In vertebrates, gluconeogenesis takes place mainly in the liver and, to a lesser extent, in the cortex of kidneys. This process occurs during periods of fasting, starvation, low-carbohydrate diets, or intense exercise and is highly endergonic. For example, the pathway leading from pyruvate to glucose-6-phosphate requires 4 molecules of ATP and 2 molecules of GTP. Gluconeogenesis is often associated with ketosis. Gluconeogenesis is also a target of therapy for type II diabetes, such as metformin, which inhibits glucose formation and stimulates glucose uptake by cells.

Sobre 3g/kg ser exagero. (Vide bodyrecomposition, autor : Lyle Mcdonald)

http://www.bodyrecomposition.com/muscle-gain/protein-requirements-for-strength-and-power-athletes.html

Em especial, destaco essa parte. Mas vale a pena ler tudo.

Reaching a Consensus

And yet, I’m going to tell you how to rationalize all of the above stuff that I imagine most of you skimmed in the first place. Two researchers, named Tipton and Wolfe wrote a cool paper about this argument. In it they first detailed all of the stuff I just bored you with. At the end they gave their recommendations where they basically argued that

  • We don’t know how much protein is required to optimize all of the potential pathways important to athletes.
  • We know that a protein intake of 1.4 g/lb (3.0 g/kg) isn’t harmful and may have benefits that are too small to be measured in research
  • As long as eating lots of protein doesn’t keep an athlete from eating too few of the other nutrients (carbs/fats), there’s no reason to not eat a lot. And there may be benefits.

Sobre o mTOR.

The mammalian target of rapamycin (mTOR) also known as mechanistic target of rapamycin or FK506 binding protein 12-rapamycin associated protein 1 (FRAP1) is aprotein which in humans is encoded by the FRAP1 gene.[1][2] mTOR is a serine/threonine protein kinase that regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis, and transcription.[3][4] mTOR belongs to the phosphatidylinositol 3-kinase-related kinase protein family.

O excesso de proteina, pode desregular o mTOR.

mTORC1

mTOR Complex 1 (mTORC1) is composed of mTOR, regulatory-associated protein of mTOR (Raptor), mammalian LST8/G-protein β-subunit like protein (mLST8/GβL) and the recently identified partners PRAS40 and DEPTOR.[9][10] This complex is characterized by the classic features of mTOR by functioning as a nutrient/energy/redox sensor and controlling protein synthesis.[3][9] The activity of this complex is stimulated by insulin, growth factors, serum, phosphatidic acid, amino acids (particularly leucine), and oxidative stress.[9][11]

mTORC1 integrates four major signal inputs: nutrients, growth factors, energy and stress. Amino acids are imported into the cell by amino acid transporters. The presence of amino acids causes Rag GTPases heterodimers to switch to its active conformation. Active Rag heterodimers interact with RAPTOR, localizing mTORC1 to the surface of late endosomes and lysosome where the Rag GTPases are located.[12] This allows mTORC1 to physically interact with RHEB, which is activated by growth factors such as insulin.[13] Thus, nutrient and growth factor signals are integrated at this point where both inputs are required for mTORC1 activation. RHEB has an essential role in mTORC1 signaling in that its loss prevents activation of mTORC1, while its overexpression can maintain mTORC1 activity when nutrients and growth factor have been withdrawn.[14] Growth factors such as insulin regulate the GTP loading of RHEB by activating the PI3K pathway which leads to the phosphorylation and activation of Akt.[15] In turn, Akt phosphorylates TSC2, which is part of the TSC1-TSC2 complex that acts as a GAP for RHEB.[15] TSC-2 phosphorylation by Akt inhibts its GAP activity for RHEB, promoting mTORC1 activation. Akt also phosphorylates PRAS40, preventing it from inhibiting mTORC1. Growth factors can also signal the ERK and Wnt pathway to activate mTORC1.[16] The mTORC1 pathway also senses energy through the AMP-activated kinase (AMPK). When the AMP:ATP ratio increases, AMPK phosphorylates TSC2 and RAPTOR, leading to inhibition of mTORC1.[17] Various stressors including hypoxiaand DNA damage can also inhibit mTORC1.[18]

The two best characterized targets of mTORC1 are p70-S6 Kinase 1 (S6K1) and 4E-BP1, the eukaryotic initiation factor 4E (eIF4E) binding protein 1.[3] mTORC1 phosphorylatesS6K1 on at least two residues, with the most critical modification occurring on a threonine residue (T389) .[19][20] This event stimulates the subsequent phosphorylation of S6K1 byPDK1.[20][21] Active S6K1 can in turn stimulate the initiation of protein synthesis through activation of S6 Ribosomal protein (a component of the ribosome) and other components of the translational machinery.[22] S6K1 can also participate in a positive feedback loop with mTORC1 by phosphorylating mTOR's negative regulatory domain at two sites; phosphorylation at these sites appears to stimulate mTOR activity.[23][24]

mTORC1 has been shown to phosphorylate at least four residues of 4E-BP1 in a hierarchical manner.[6][25][26] Non-phosphorylated 4E-BP1 binds tightly to the translation initiation factor eIF4E, preventing it from binding to 5'-cappedmRNAs and recruiting them to the ribosomal initiation complex.[27] Upon phosphorylation by mTORC1, 4E-BP1 releases eIF4E, allowing it to perform its function.[27] The activity of mTORC1 appears to be regulated through a dynamic interaction between mTOR and Raptor, one which is mediated by GβL.[9][10] Raptor and mTOR share a strong N-terminal interaction and a weaker C-terminal interaction near mTOR's kinase domain.[9] When stimulatory signals are sensed, such as high nutrient/energy levels, the mTOR-Raptor C-terminal interaction is weakened and possibly completely lost, allowing mTOR kinase activity to be turned on. When stimulatory signals are withdrawn, such as low nutrient levels, the mTOR-Raptor C-terminal interaction is strengthened, essentially shutting off kinase function of mTOR

E por ultimo, Proteinuria.

http://en.wikipedia.org/wiki/Proteinuria

mTOR, e proteinuria foram usados como base o wikipedia.

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