Adrian Burke - www.FUSIONBodybuilding.com
Friday, February 23, 2007
Wednesday, February 21, 2007
2007 SABBA Bodybuilding Championships & Bikini Model Search
COMPETITOR INFORMATION for the
THE 1ST ANNUAL GREENE YAK FITNESS MODEL SEARCH
HOST HOTEL: Ramada Hotel
1818 Victoria Avenue
Regina, SK
Reservations: 1-306-569-1666
(refer to “2007 Novice Champs group # 9859) for discount rate)
Please book by March 17th, 2007 to guarantee your rate
WEIGH-INS: 6 pm sharp
Friday March 30th, 2007
University Theater, located in the Dr. William Riddell Center
at the University of Regina
3737 Wascana Parkway
Regina, SK
FINALS: 5 pm
Saturday March 31st, 2007
University Theater, located in the Dr. William Riddell Center
at the University of Regina
3737 Wascana Parkway
Regina, SK
Fitness Model Search Competition Information
This is the 1st ever Greene Yak model search which is perfect for the female who has an athletic physique with possibly (but not mandatory) a modeling background that yields a marketable look. This event is a terrific opportunity in many regards to the competitor. The bar has been raised for this event in that this event is being used as a National Qualifier. Aside from the prestige of winning the 1st ever Greene Yak model search, the winner of the model search will be given the opportunity to represent Canada at the Miss Caribbean Tan International Finals Pageant! That’s right, the winner will receive an all expense paid trip (air, hotel, food) to Mexico for a week to represent Canada for the first time ever!
In the model search you will not be required to perform a gymnastic routine. The model search competition will consist of two (2) rounds:
Round One – sports attire round
In the sports attire round, the competitor may wear any type of athletic clothing that compliments your particular body type. Fitness or gym wear, aerobic wear, sports skirts, workout “booty” shorts are all good examples. All attire must be tasteful with respect to decency. Bare foot or sport shoes are acceptable, but heels are not permitted. The competitor will be judged on an on overall athletic appearance that is naturally obtainable.
Round Two – two piece bikini with high heels
In the two piece bikini round, the competitor will be judged on an on overall athletic appearance that is naturally obtainable as in round one. High heel shoe style and two piece bikini style and color is up to the competitor, however absolutely no G-string or thong bottoms will be allowed. It is important to note that the judges will be presented a different “total package” while wearing a two piece bikini with high heels as opposed to the sports attire round and therefore will be judging with a fresh perspective.
General Model Search Rules and Regulations
*Competitors must have filled out and signed the Model Search entry form and paid the entry fee.
*Hair may be styled as desired, as well as jewelry is allowed as long as not excessive.
*No posing oils or lotions are allowed in any round.
*All two piece bikinis and sport attire must be brought to the weigh-ins. If you do not have it with you, you will be allowed 15 minutes to get it. If not brought in this time frame, you can be disqualified from the competition.
*Numbers must be worn on the left hip in all rounds.
*Depending on the number of competitors, the competition format (for both rounds) are as follows: The competitors will line up at the back of the stage and be called out of the lineup one at a time in which they will have approximately 30 seconds to move around the stage walking the “catwalk”. You may stop, do a ¼ turn, ½ turn, and/or strike a pose in a manner that a runway model would, and in a way that suits and compliments you best. Remember to make sure the judges see you.
* Back Stage: Due to the size of the backstage and change rooms, no one will be allowed to accompany you back stage; friends, coaches, etc. There will be help for the competitors back stage. Security will be present.
*Competitors should be at the venue approximately ½ hour before show time to familiarize yourself with the stage and backstage area.
Note: There will be no pump up weights supplied backstage at the venue. If you require any pump up weights, or rubber resistance bands, you may bring them.
Adrian Burke - www.FUSIONBodybuilding.com
Monday, February 19, 2007
(((CONTEST))) ***FUSION Bodybuilding's TRAIN INSANE Face***
The new FUBAR formula is about to launch - about damn time! To get things going we want you to send us a snap shot of your best TRAIN INSANE face. We are going to give FUBAR samples to everyone who enters AND to the 10 best TRAIN INSANE face's we are going to send you a FREE bottle.
Be part of the insanity – click below for contest conditions: http://forum.bodybuilding.com/showthread.php?t=1483681
Remember to TRAIN INSANE…cuz if you aren’t - someone else is!!!
Chris Belanger – VP Sales - www.FUSIONBodybuilding.com
Be part of the insanity – click below for contest conditions: http://forum.bodybuilding.com/showthread.php?t=1483681
Remember to TRAIN INSANE…cuz if you aren’t - someone else is!!!
Chris Belanger – VP Sales - www.FUSIONBodybuilding.com
Monday, February 12, 2007
HORMONES
Testosterone
Molecular Structure of Testosterone
Testosterone (T) – perhaps one of the most important hormones for bodybuilding, or at least, one of the most common hormones in the human body. T is a primary sex hormone in men, and also highly anabolic. It is also found in women, but to a much lesser degree than men, men create, on average, twenty to thirty more times T than women.
Since T is highly anabolic, this means that it plays a role in “building of”, usually tissues in the body, ie. muscle mass. T also plays a role in protein synthesis which helps you repair muscle after an intense workout. Other anabolic effects with T is strength gain, this is fairly obvious, the more muscle mass you have, the heavier you can lift.
T is a steroid hormone, and like all other steroid hormones cholesterol is one of the precursors for its production. Most of the T in men is made in the testes, but also in smaller quantities in the adrenal cortex, which is found on top of the kidneys. In women, most of the T is synthesized in the ovaries.
In addition to its large role on muscle tissue synthesis, T indirectly affects muscle fiber’s protein content by promoting growth hormone release, which leads to insulin growth factor (IGF) synthesis and release from the liver. T also influences neural receptors to increase neurotransmitter release and initiate structural protein changes that alter the size of the neuromuscular junction, the gap between the pre-synapse and the cellular membrane of the muscle cell. These neural effects increase the force-production capabilities of skeletal muscle, thus more strength.
Luteinizing Hormone (LH) and Follicle-Stimulating Hormone (FSH)
These two hormones are gonadotropic hormones; a hormone released either from the anterior pituitary gland, which is found in the brain. FSH in males stimulates gernminal epithelium growth in the testes to promote sperm devolvement. LH also stimulates the testes to secrete T.
How exercise affects FSH and LH is still unknown, here are inconsistent reports that describe short-term exercise-association release. However, LH release works like a pulse; it has it peaks and low points, thus making it somewhat difficult to separate any specific exercise related changes from a normal pattern. But generally, LH concentration rises before exercise and peaks during recovery.
Growth Hormone, Exercise, and Tissue Synthesis
Growth hormone is a 191 amino acid, single chain polypeptide hormone, which is synthesized, stored and secreted by the cells within the anterior pituitary gland, which stimulates growth and cell reproduction.
Structure of Human Growth Hormone
Short term physical activity stimulates a sharp rise in GH pulse amplitude and the amount of hormone secreted per pulse. More importantly though, exercise stimulates release of GH isoforms with extended half-lifes as compared to normal GH, this will allow for the effects of GH to last longer on target tissues. Some of the most GH release benefits include muscle, bone, and connective tissue growth and remodeling. It also influences the choice of “fuel” during exercise, principally decreasing glucose uptake, increasing free fatty acid mobilization and enhancing liver gluconeogensis (the creation of glycogen). The net metabolic effect on increased exercise-induced GH production preserves plasma glucose concentration for central nervous system and muscle functions. Many of the growth-promoting effects of GH result from actions of an intermediary chemical messenger on different target tissues, rather than direct effect of GH itself. These peptide messengers, produced in the liver, are termed somataodmeials or insulin-like-growth factors because of there similar structure to insulin. These factors exert potent peripheral effects on the motor units of other tissues.
The mechanism on how exercise stimulates GH release to improve protein synthesis, and thus muscle hypertrophy (muscles growing in size), and it’s other effects is unknown. One hypothesis says that exercise directly stimulates GH release, or release of somatomedians from the liver or kidneys, which then in turn stimulates anabolic processes. Exercise also may indirectly affect GH by stimulating the cholinergic pathways to trigger GH release.
Trained and sedentary individual show similar increases in GH concentration when they exercise to exhaustion. In contrast though, the sedentary person maintains higher levels of GH for several hours into recovery. During a standard bout of sub-maximal exercise, sedentary individuals have a greater GH response. Because this absolute sub-maximal exercise level represents greater stress for the less fit person. GH release generally relates more to the relative strenuousness of physical effort.
Insulin-Like Growth Factors (IGF)
IGF’s mediates many of GH’s effects. In response to GH simulation, liver synthesize IGF-1, a 70-amino acid poly peptide and IGF-II (a 67-amino acid polypeptide, the total time for this process that requires 9 – 30 hours. IGF’s travel in the blood attached to one of five types of binding proteins for release as a free hormone to interact with specific receptors. The factors that influence IGF transport include the binding proteins within muscle, nutrition status and plasma insulin levels.
The time required for IGF synthesis to GH stimulation affects any IGF appearance during or immediately following exercise. This suggest that it’s release results from disruption of cells already containing IGF. Also, GH-mediated release of IGF with exercise may reflect a different time course than the typically observed in non-exercise conditions.
Kurt Kuhn - www.FUSIONBodybuilding.com
Molecular Structure of Testosterone
Testosterone (T) – perhaps one of the most important hormones for bodybuilding, or at least, one of the most common hormones in the human body. T is a primary sex hormone in men, and also highly anabolic. It is also found in women, but to a much lesser degree than men, men create, on average, twenty to thirty more times T than women.
Since T is highly anabolic, this means that it plays a role in “building of”, usually tissues in the body, ie. muscle mass. T also plays a role in protein synthesis which helps you repair muscle after an intense workout. Other anabolic effects with T is strength gain, this is fairly obvious, the more muscle mass you have, the heavier you can lift.
T is a steroid hormone, and like all other steroid hormones cholesterol is one of the precursors for its production. Most of the T in men is made in the testes, but also in smaller quantities in the adrenal cortex, which is found on top of the kidneys. In women, most of the T is synthesized in the ovaries.
In addition to its large role on muscle tissue synthesis, T indirectly affects muscle fiber’s protein content by promoting growth hormone release, which leads to insulin growth factor (IGF) synthesis and release from the liver. T also influences neural receptors to increase neurotransmitter release and initiate structural protein changes that alter the size of the neuromuscular junction, the gap between the pre-synapse and the cellular membrane of the muscle cell. These neural effects increase the force-production capabilities of skeletal muscle, thus more strength.
Luteinizing Hormone (LH) and Follicle-Stimulating Hormone (FSH)
These two hormones are gonadotropic hormones; a hormone released either from the anterior pituitary gland, which is found in the brain. FSH in males stimulates gernminal epithelium growth in the testes to promote sperm devolvement. LH also stimulates the testes to secrete T.
How exercise affects FSH and LH is still unknown, here are inconsistent reports that describe short-term exercise-association release. However, LH release works like a pulse; it has it peaks and low points, thus making it somewhat difficult to separate any specific exercise related changes from a normal pattern. But generally, LH concentration rises before exercise and peaks during recovery.
Growth Hormone, Exercise, and Tissue Synthesis
Growth hormone is a 191 amino acid, single chain polypeptide hormone, which is synthesized, stored and secreted by the cells within the anterior pituitary gland, which stimulates growth and cell reproduction.
Structure of Human Growth Hormone
Short term physical activity stimulates a sharp rise in GH pulse amplitude and the amount of hormone secreted per pulse. More importantly though, exercise stimulates release of GH isoforms with extended half-lifes as compared to normal GH, this will allow for the effects of GH to last longer on target tissues. Some of the most GH release benefits include muscle, bone, and connective tissue growth and remodeling. It also influences the choice of “fuel” during exercise, principally decreasing glucose uptake, increasing free fatty acid mobilization and enhancing liver gluconeogensis (the creation of glycogen). The net metabolic effect on increased exercise-induced GH production preserves plasma glucose concentration for central nervous system and muscle functions. Many of the growth-promoting effects of GH result from actions of an intermediary chemical messenger on different target tissues, rather than direct effect of GH itself. These peptide messengers, produced in the liver, are termed somataodmeials or insulin-like-growth factors because of there similar structure to insulin. These factors exert potent peripheral effects on the motor units of other tissues.
The mechanism on how exercise stimulates GH release to improve protein synthesis, and thus muscle hypertrophy (muscles growing in size), and it’s other effects is unknown. One hypothesis says that exercise directly stimulates GH release, or release of somatomedians from the liver or kidneys, which then in turn stimulates anabolic processes. Exercise also may indirectly affect GH by stimulating the cholinergic pathways to trigger GH release.
Trained and sedentary individual show similar increases in GH concentration when they exercise to exhaustion. In contrast though, the sedentary person maintains higher levels of GH for several hours into recovery. During a standard bout of sub-maximal exercise, sedentary individuals have a greater GH response. Because this absolute sub-maximal exercise level represents greater stress for the less fit person. GH release generally relates more to the relative strenuousness of physical effort.
Insulin-Like Growth Factors (IGF)
IGF’s mediates many of GH’s effects. In response to GH simulation, liver synthesize IGF-1, a 70-amino acid poly peptide and IGF-II (a 67-amino acid polypeptide, the total time for this process that requires 9 – 30 hours. IGF’s travel in the blood attached to one of five types of binding proteins for release as a free hormone to interact with specific receptors. The factors that influence IGF transport include the binding proteins within muscle, nutrition status and plasma insulin levels.
The time required for IGF synthesis to GH stimulation affects any IGF appearance during or immediately following exercise. This suggest that it’s release results from disruption of cells already containing IGF. Also, GH-mediated release of IGF with exercise may reflect a different time course than the typically observed in non-exercise conditions.
Kurt Kuhn - www.FUSIONBodybuilding.com
Friday, February 02, 2007
Thursday, February 01, 2007
Leucine as a Nutritional Signal
Branched-Chain Amino Acids (Leucine, IsoLeucine, and Valine) also known as BCAA’s are the building blocks of the body. They make up 35% of your muscle mass and must be present for molecular growth and development to take place. BCAA's act as nitrogen carriers and assist the muscles in synthesizing other amino acids needed for anabolic muscle action.
Over the next little while I will not be discussing the anabolic effects about the BCAA’s but rather discussing the role of one very important BCAA – Leucine.
Leucine
Systematic Name: (S)-2-amino-4-methyl-pentanoic acid
After doing some research I came across an article put together by Susan M. Hutson (Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC 27157) and Robert A. Harris (Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202-5122)
Leucine as a Nutritional Signal
Although the anabolic effects of amino acids originating from dietary protein on protein synthesis and cell function were first reported over 20 year ago, until recently to molecular basis for many of these observations remained elusive. Now there is convincing evidence that amino acids are actually participants in signal transduction pathways, activating in selected cells some of the same signaling cascades as the anabolic hormone insulin.
Activation of signaling pathways is now recognized to be an important non-protein function of amino acids. This can be and often is studied with amino acid mixtures. In most instances, however, the indispensable branch-chain amino acid Leucine can exert the same effects as amino acid mixtures.
Historically, Leucine has always seemed special and more important that the other two branched-chain amino acids, IsoLeucine and Valine. We have long known that Leucine is ketogenic and is specific among the branched-chain amino acids in its ability to stimulate insulin release from the islet cells of the pancreas (Panten et al. 1974).
A paper was put forth, “Regulation of Branched-Chain α-Keto Acid Dehydrogenase Kinase Expression” by Robert A. Harris, reviews the molecular mechanisms by which Leucine catabolism is controlled at the level of the branched-chain α-keto acid dehydrogenase complex. Evidence is presented for nutrient and hormonal regulation of expression of the branched chain α-keto acid dehydrogenase kinase. The hypothesis is put forth the involvement of thyroid hormone in the regulation of the expression of this gene.
A second paper has been put forth, “Function of Leucine in Excitory Neurotransmitter Metabolism in the Central Nervous System” by Susan M. Hutson, addresses the role of branched-chain amino acids in metabolism in the central nervous system. The hypothesis is advanced that branched-chain amino acids have an important role as donors of nitrogen for dispensable amino acid biosynthesis, analogous to their role in glutamine and alanine synthesis in skeletal muscle developed in the 1970s (Odessey et al. 1974, Chang and Goldberg 1978, Garber et al. 1976). Evidence that BCAA nitrogen is required for formation of the neurotransmitter glutamate has been reviewed (Yudkoff et al. 1996, Bixel et al. 1997, Hutson et al. 1998) and new findings on the special role of branched-chain amino acids in neurotransmitter metabolism in the central nervous system are present.
1. Chang T. W., Goldberg A. L. The metabolic fates of amino acids and the formation of glutamine in skeletal muscle. J. Biol. Chem. 1978;253:3685-3693
2. Fajans S. S., Knopf R. F., Floyd J. C., Power L., Conn J. W. The experimental induction in man of sensitivity to leucine hypoglycemia. J. Clin. Invest. 1963;42:216-229
3. Hutson S. M., Berkich D. A., Drown P., Xu B., LaNoue K. F. Role of branched-chain aminotransferase isoenzymes and gabapentin in neurotransmitter metabolism. J. Neurochem. 1998;71:863-874
4. Odessey R., Khairallah E. A., Goldberg A. L. Origin and possible significance of alanine production by skeletal muscle. J. Biol. Chem. 1974;250:290-298
5. Panten U., Christians J., Kriegstein E., Von Poser W., Hasselblatt A. Studies on the mechanism of L-leucine-and alpha-ketoisocaproic acid-induced insulin release from perifused isolated pancreatic islets. Diabetologia 1974;10:149-154
6. Yudkoff M., Daikhin Y., Grunstein L., Nissim I., Stern J., Pleasure D., Nissim I. Astrocyte leucine metabolism: significance of branched-chain amino acid transamination. J. Neurochem. 1996;66:378-385
In conclusion to this article I believe that there is substantial evidence that BCAA’s and specifically Leucine may have an important role on weight loss. I will continue do my research on the metabolic effects of this incredible amino acid and keep you posted with the findings.
Chris Belanger – VP Sales
Over the next little while I will not be discussing the anabolic effects about the BCAA’s but rather discussing the role of one very important BCAA – Leucine.
Leucine
Systematic Name: (S)-2-amino-4-methyl-pentanoic acid
After doing some research I came across an article put together by Susan M. Hutson (Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC 27157) and Robert A. Harris (Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202-5122)
Leucine as a Nutritional Signal
Although the anabolic effects of amino acids originating from dietary protein on protein synthesis and cell function were first reported over 20 year ago, until recently to molecular basis for many of these observations remained elusive. Now there is convincing evidence that amino acids are actually participants in signal transduction pathways, activating in selected cells some of the same signaling cascades as the anabolic hormone insulin.
Activation of signaling pathways is now recognized to be an important non-protein function of amino acids. This can be and often is studied with amino acid mixtures. In most instances, however, the indispensable branch-chain amino acid Leucine can exert the same effects as amino acid mixtures.
Historically, Leucine has always seemed special and more important that the other two branched-chain amino acids, IsoLeucine and Valine. We have long known that Leucine is ketogenic and is specific among the branched-chain amino acids in its ability to stimulate insulin release from the islet cells of the pancreas (Panten et al. 1974).
A paper was put forth, “Regulation of Branched-Chain α-Keto Acid Dehydrogenase Kinase Expression” by Robert A. Harris, reviews the molecular mechanisms by which Leucine catabolism is controlled at the level of the branched-chain α-keto acid dehydrogenase complex. Evidence is presented for nutrient and hormonal regulation of expression of the branched chain α-keto acid dehydrogenase kinase. The hypothesis is put forth the involvement of thyroid hormone in the regulation of the expression of this gene.
A second paper has been put forth, “Function of Leucine in Excitory Neurotransmitter Metabolism in the Central Nervous System” by Susan M. Hutson, addresses the role of branched-chain amino acids in metabolism in the central nervous system. The hypothesis is advanced that branched-chain amino acids have an important role as donors of nitrogen for dispensable amino acid biosynthesis, analogous to their role in glutamine and alanine synthesis in skeletal muscle developed in the 1970s (Odessey et al. 1974, Chang and Goldberg 1978, Garber et al. 1976). Evidence that BCAA nitrogen is required for formation of the neurotransmitter glutamate has been reviewed (Yudkoff et al. 1996, Bixel et al. 1997, Hutson et al. 1998) and new findings on the special role of branched-chain amino acids in neurotransmitter metabolism in the central nervous system are present.
1. Chang T. W., Goldberg A. L. The metabolic fates of amino acids and the formation of glutamine in skeletal muscle. J. Biol. Chem. 1978;253:3685-3693
2. Fajans S. S., Knopf R. F., Floyd J. C., Power L., Conn J. W. The experimental induction in man of sensitivity to leucine hypoglycemia. J. Clin. Invest. 1963;42:216-229
3. Hutson S. M., Berkich D. A., Drown P., Xu B., LaNoue K. F. Role of branched-chain aminotransferase isoenzymes and gabapentin in neurotransmitter metabolism. J. Neurochem. 1998;71:863-874
4. Odessey R., Khairallah E. A., Goldberg A. L. Origin and possible significance of alanine production by skeletal muscle. J. Biol. Chem. 1974;250:290-298
5. Panten U., Christians J., Kriegstein E., Von Poser W., Hasselblatt A. Studies on the mechanism of L-leucine-and alpha-ketoisocaproic acid-induced insulin release from perifused isolated pancreatic islets. Diabetologia 1974;10:149-154
6. Yudkoff M., Daikhin Y., Grunstein L., Nissim I., Stern J., Pleasure D., Nissim I. Astrocyte leucine metabolism: significance of branched-chain amino acid transamination. J. Neurochem. 1996;66:378-385
In conclusion to this article I believe that there is substantial evidence that BCAA’s and specifically Leucine may have an important role on weight loss. I will continue do my research on the metabolic effects of this incredible amino acid and keep you posted with the findings.
Chris Belanger – VP Sales
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