Just found another article on increasing ARs, and although you are going to say the same thing, isn't it possible that 2 seperate studies have reached the same conclusion. It is Possible.

Enjoy.........

take the broadest view possible, but at the molecular level. Consider one molecule of an anabolic/androgenic steroid (AAS) in the bloodstream, bound to a molecule of testosterone binding globulin (TeBG). A receptor on the outside of the muscle cell will bring the TeBG/AAS into the cell. Interestingly, this process may itself stimulate the metabolism of the cell by increasing cAMP, but that's a side note.

Next, inside the cell, the molecule of AAS binds to a molecule of androgen receptor (AR).

Think of the AR as being a machine that does nothing unless it is turned on. The AR either has an AAS bound to it, and is thereby switched on, or it does not, and is off. There is no intermediate condition that might cause an AAS to give a weak effect.
Therefore, the AR is just as much activated by say a bound molecule of Methenolone (from Primobolan) as it is by a bound molecule from any other AAS.
You may object to this, 228 mg/week for example, of Parabolan, certainly gives a different effect than 228 mg/week of Primobolan. This is true, but the reasons for the difference in effect lie elsewhere.
The AR now travels to the nucleus of the cell. Actually, it will join together with another activated AR to form a dimer, but this is a detail you may ignore. The AR binds to certain parts of the DNA, and certain genes then start producing more mRNA.
The mRNA is different for each gene, and carries the information the cell needs to make protein.
Ah, protein! At last, something simple. The molecule of AAS ultimately causes the muscle cell to make more of some protein, helping you to get bigger. There were steps needed to get from the mRNA to the protein, but we will skip them.
Does each binding of AAS to an AR result in exactly one extra molecule of protein produced? No, because even though the AR is fully activated by any AAS, that does not mean that it has a 100% chance of binding to DNA. And differing amounts of extra mRNA might be produced by this. Also, an AR remains active only as long as an AAS remains bound to it.
So the amount of extra growth per extra activated AR can vary. Now, having a broad view of the process, let's take a closer look at the AR itself.
The AR is a large protein molecule, produced from one and only gene in DNA. There aren't lots of different kinds of receptors, as some authors claim. And there definitely aren't AR's specific for oral or injectable anabolics!
The first important question to ask is, "How many AR's do you have? Is the number small or large? Can it be changed?" Since these are, in effect, little machines which are either on or off, and their effect is greater as more are activated, we want as many of them switched on as possible.
There are far fewer ARs than most people realize. Some authors who are fearful of AAS doses beyond 200 mg/week say that only this amount will be accepted by the receptors in muscle, and everything past that will "spill over" and go into receptors in the skin and elsewhere.
Research shows that muscle tissue has roughly 3 nanomoles of ARs per kg. Then your body probably has less than 300 nanomoles of ARs, grand total, let's say.
Well, one 2.5 mg tab of Oxandrolone supplies about 8000 nanomoles of AAS. Clearly, that's far more molecules than your body has receptors. A little math shows that all those receptors combined could bind only about 4% of the molecules of AAS in one little 2.5 mg tab! So binding to ARs cannot appreciably reduce the concentration of AAS in the blood.
Therefore, the idea that ARs will bind most of whatever dose some author recommends is entirely wrong. There just aren't that many receptors.
Typical doses of AAS are high enough that almost all the ARs are bound to AAS, whether the dose is say 200 mg/week or 1000 mg/week. If the same percentages of ARs are active (nearly 100%), then why do higher doses give more results? It's a fact that they do.
One popular explanation is that high doses of AAS block cortisol receptors and are thus anti-catabolic. But if this were an adequate explanation, then one could use anti-cortisol drugs together with low doses of AAS and get the same results as with high doses of AAS. This isn't the case.
Three other possibilities come to mind:

high doses of AAS could result in the production of a larger number of ARs. This would stimulate more protein synthesis.
High doses of AAS could stimulate growth by means that don't involve the AR.
High doses of AAS might improve the efficiency of DNA binding, production of mRNA, or conversion of mRNA to protein.

quote:

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Originally posted by Cornellius:
I can feel another fight...

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No Fights on this board, just analysis and discussion

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I'll quit the juice....when Amy Fadhli asks me out.

Thanks.

Primo57 - post it bro, would really like some interesting reading right about now.

F1

See below abstract.

Short-term oxandrolone administration stimulates net muscle protein synthesis in young men.

JOURNAL OF CLINICAL ENDOCRINOLOGY AND METABOLISM. vol. 84, no. 8 (1999 Aug): 2705-11.

Short term administration of testosterone stimulates net protein synthesis in healthy men. We investigated whether oxandrolone [Oxandrin (OX)], a synthetic analog of testosterone, would improve net muscle protein synthesis and transport of amino acids across the leg. Six healthy men [22+/-1 (+/-SE) yr] were studied in the postabsorptive state before and after 5 days of oral OX (15 mg/day). Muscle protein synthesis and breakdown were determined by a three-compartment model using stable isotopic data obtained from femoral arterio-venous sampling and muscle biopsy. The precursor-product method was used to determine muscle protein fractional synthetic rates. Fractional breakdown rates were also directly calculated. Total messenger ribonucleic acid (mRNA) concentrations of skeletal muscle insulin-like growth factor I and androgen receptor (AR) were determined using RT-PCR. Model-derived muscle protein synthesis increased from 53.5+/-3 to 68.3+/-5 (mean+/-SE) nmol/min.100 mL/leg (P < 0.05), whereas protein breakdown was unchanged. Inward transport of amino acids remained unchanged with OX, whereas outward transport decreased (P < 0.05). The fractional synthetic rate increased 44% (P < 0.05) after OX administration, with no change in fractional breakdown rate. Therefore, the net balance between synthesis and breakdown became more positive with both methodologies (P < 0.05) and was not different from zero. Further, RT-PCR showed that OX administration significantly increased mRNA concentrations of skeletal muscle AR without changing insulin-like growth factor I mRNA concentrations. We conclude that short term OX administration stimulated an increase in skeletal muscle protein synthesis and improved intracellular reutilization of amino acids. The mechanism for this stimulation may be related to an OX-induced increase in AR expression in skeletal muscle.