Active Component:

• AMP; Adenosine 5’-Monophosphate; 5’-Adenylic Acid

• Calcium Citrate

• Biotin

 

Form:
Ampical comes as a white powder to be added at 100mg to 500mg per serve of finished product. This performance ingredient is certified and guaranteed in purity using Fourier Transform (Infra-Red) Raman Spectroscopy. It imparts a flavour enhancing taste.

 

Recommended Application:

• 100mg - 500mg per serve of finished product (do not exceed recommendations)

  • Specialised for endurance training (less suited to resistance training)

  • Energy enhancement

  • Weight loss

 

Research Highlights:

• Increased fat metabolism

• Increased skeletal muscle mitochondrial biogenesis, encouraging endurance phenotype

• Increased skeletal muscle energy utilisation 

• General health promoting

 

Permissible Label and Advertising Claims Under FSANZ:

• Contributes to normal energy metabolism

• Contributes to normal fat metabolism and energy production

• Contributes to normal functioning of the nervous system

 

Research Details:

AMP is a product of the resynthesis of ATP from ADP via adenylate kinase, and is the primary signal for activation of AMP-Activated Protein Kinase (AMPK) in response to depleted ATP stores (Hardie, 2004; Adams, Chen, Van Denderen, Morton, Parker, Witters, & Kemp, 2004). This makes AMP the cornerstone of increased ATP production, but its activation of AMPK goes beyond simply upregulating ATP levels, as it is critical in mitochondrial health and cellular response to exercise, and has even been described as an ‘exercise mimetic’ (Herzig, & Shaw, 2018; Chen, Stephens, Murthy, Canny, Hargreaves, Witters, & McConell, 2003; Narkar, Downes, Ruth, Embler, Wang, Banayo, & Kang, 2008). Interestingly, the average human at any one time contains 250g of ATP, but over the course of the day will produce over 60kg of ATP, as a result of the constant use and recycling of the same 250g (Pizzorno, 2014). This suggests that small changes to instantaneous AMP and ATP stores could significantly alter total daily energy availability.

 

AMPK is the primary cellular sensor for energy usage, and behaves as a detector for the AMP/ATP ratio, upregulating its activity in response to increased AMP or decreased ATP (Hardie, Ross, & Hawley, 2012). AMPK also takes cellular glucose concentration as an input, whereby insufficient glucose encourages formation of the active AXIN-AMPK-LKB1 complex (Zhang, Guo, Zhang, Lin, Yin, Peng, & Li, 2013). 

 

AMPK activation exhibits a swathe of beneficial effects, including upregulation of the expression of genes controlling glucose uptake, fatty acid oxidation, and mitochondrial biogenesis. Many of these effects in skeletal muscle are the direct result of AMPK’s induction of PGC-1α, the master regulator for mitochondrial biogenesis and energy homeostasis. This in turn results in increased expression of genes such as GLUT1 and GLUT4, the glucose channels which enable cellular glucose uptake and metabolism (Barnes, Ingram, Porras, Barros, Hudson, Fryer, & Baldwin, 2002; Jäger, Handschin, Pierre, & Spiegelman, 2007). AMPK activation also increases cellular NAD+ levels, in turn upregulating SIRT1, which has been implicated in increased lifespan, lipolysis in fatty tissues, and insulin sensitivity (Cantó, Gerhart-Hines, Feige, Lagouge, Noriega, Milne, & Auwerx, 2009; Imai, & Guarente, 2014; Picard, Kurtev, Chung, Topark-Ngarm, Senawong, de Oliveira, & Guarente, 2004; Sun, Zhang, Ge, Yan, Chen, Shi, & Zhai, 2007).

 

AMPK is also strongly linked to cellular responses to hypoxic conditions, such as upregulation of glycolysis (Emerling, Weinberg, Snyder, Burgess, Mutlu, Viollet, & Chandel, 2009; Marsin, Bertrand, Rider, Deprez, Beauloye, Vincent, & Hue, 2000).

 

Other protective effects of the activation of AMPK by AMP-5 include protection against neurodegeneration (Li, Zeng, Viollet, Ronnett, & McCullough, 2007), against renal cysts (Takiar, Nishio, Seo-Mayer, King, Li, Zhang, & Caplan, 2011) and modulation of reactive oxygen species to protect against diabetes (Dugan, You, Ali, Diamond-Stanic, Miyamoto, DeCleves, & Nguyen, 2013; Hinchy, Gruszczyk, Willows, Navaratnam, Hall, Bates, & Murphy, 2018).

Adams, J., Chen, Z. P., Van Denderen, B. J., Morton, C. J., Parker, M. W., Witters, L. A., & Kemp, B. E. (2004). Intrasteric control of AMPK via the γ1 subunit AMP allosteric regulatory site. Protein science, 13(1), 155-165.

 

References:

Barnes, K., Ingram, J. C., Porras, O. H., Barros, L. F., Hudson, E. R., Fryer, L. G., & Baldwin, S. A. (2002). Activation of GLUT1 by metabolic and osmotic stress: potential involvement of AMP-activated protein kinase (AMPK). Journal of cell science, 115(11), 2433-2442.

 

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., & Auwerx, J. (2009). AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature, 458(7241), 1056-1060.

 

Chen, Z. P., Stephens, T. J., Murthy, S., Canny, B. J., Hargreaves, M., Witters, L. A., & McConell, G. K. (2003). Effect of exercise intensity on skeletal muscle AMPK signaling in humans. Diabetes, 52(9), 2205-2212.

 

Dugan, L. L., You, Y. H., Ali, S. S., Diamond-Stanic, M., Miyamoto, S., DeCleves, A. E., & Nguyen, W. (2013). AMPK dysregulation promotes diabetes-related reduction of superoxide and mitochondrial function. The Journal of clinical investigation, 123(11).

 

Emerling, B. M., Weinberg, F., Snyder, C., Burgess, Z., Mutlu, G. M., Viollet, B., & Chandel, N. S. (2009). Hypoxic activation of AMPK is dependent on mitochondrial ROS but independent of an increase in AMP/ATP ratio. Free Radical Biology and Medicine, 46(10), 1386-1391.

 

Hardie, D. G. (2004). The AMP-activated protein kinase pathway–new players upstream and downstream. Journal of cell science, 117(23), 5479-5487.

 

Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012). AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nature reviews Molecular cell biology, 13(4), 251-262.

 

Herzig, S., & Shaw, R. J. (2018). AMPK: guardian of metabolism and mitochondrial homeostasis. Nature reviews Molecular cell biology, 19(2), 121.

 

Hinchy, E. C., Gruszczyk, A. V., Willows, R., Navaratnam, N., Hall, A. R., Bates, G., & Murphy, M. P. (2018). Mitochondria-derived ROS activate AMP-activated protein kinase (AMPK) indirectly. Journal of Biological Chemistry, 293(44), 17208-17217.

 

Imai, S. I., & Guarente, L. (2014). NAD+ and sirtuins in aging and disease. Trends in cell biology, 24(8), 464-471. 

 

Jäger, S., Handschin, C., Pierre, J. S., & Spiegelman, B. M. (2007). AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α. Proceedings of the National Academy of Sciences, 104(29), 12017-12022.

 

Li, J., Zeng, Z., Viollet, B., Ronnett, G. V., & McCullough, L. D. (2007). Neuroprotective effects of adenosine monophosphate-activated protein kinase inhibition and gene deletion in stroke. Stroke, 38(11), 2992-2999.

 

Marsin, A. S., Bertrand, L., Rider, M. H., Deprez, J., Beauloye, C., Vincent, M. F., & Hue, L. (2000). Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia. Current biology, 10(20), 1247-1255.

 

Narkar, V. A., Downes, M., Ruth, T. Y., Embler, E., Wang, Y. X., Banayo, E., & Kang, H. (2008). AMPK and PPARδ agonists are exercise mimetics. Cell, 134(3), 405-415.

 

Picard, F., Kurtev, M., Chung, N., Topark-Ngarm, A., Senawong, T., de Oliveira, R. M., & Guarente, L. (2004). Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ. Nature, 429(6993), 771-776.

 

Pizzorno, J. (2014). Mitochondria—fundamental to life and health. Integrative Medicine: A Clinician's Journal, 13(2), 8.

 

Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., & Zhai, Q. (2007). SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B. Cell metabolism, 6(4), 307-319.

 

Takiar, V., Nishio, S., Seo-Mayer, P., King, J. D., Li, H., Zhang, L., & Caplan, M. J. (2011). Activating AMP-activated protein kinase (AMPK) slows renal cystogenesis. Proceedings of the National Academy of Sciences, 108(6), 2462-2467.

 

Zhang, Y. L., Guo, H., Zhang, C. S., Lin, S. Y., Yin, Z., Peng, Y., & Li, M. (2013). AMP as a low-energy charge signal autonomously initiates assembly of AXIN-AMPK-LKB1 complex for AMPK activation. Cell metabolism, 18(4), 546-555.