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BiPro--Muscle Mass, Strength & Function

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Transcript of BiPro--Muscle Mass, Strength & Function

Muscle Mass, Strength & Function
Healthy Muscle is Central to Metabolic Stability & Mobility1
Whole-Body Metabolism
Mobility/Physical Activities
Healthy Aging
Managing Body Weight & Composition
Protein Quantity
Protein Quality
Digestion and Absorption Kinetics
Starvation
Chronic Disease
Loss of Lean Leg Mass During Bed Rest
Nutrition for Muscle Health: Dietary Protein & Muscle Synthesis
Muscle's Role in Catabolism
Time of Consumption
Leucine Content in Common Foods
References
Sarcopenia
Muscle Protein Synthesis
Whole Body Protein
Net muscle protein balance
Dietary protein need for healthy older adults
BiPRO and Alpha-lactalbumin for Whole-Body Protein Metabolism
The human body needs to synthesize approximately 250 grams of new proteins every day in order to replace old proteins and repair tissue damage. Nearly every protein in the body is replaced over the course of one year. Optimizing dietary protein intake is important because dietary protein together with the existing protein in our body provide the essential amino acids to build new proteins. Most new proteins are not used for growth, but to repair and remodel existing protein structures.

Muscle protein synthesis versus whole body protein synthesis
When considering whole-body protein metabolism, the difference between whole body protein synthesis (WBPS) and skeletal muscle protein synthesis (MPS) must be considered. Skeletal muscle only contributes 25–30% to WBPS1 and has a protein turnover rate that is approximately 20 times lower than other parts of the body, including the gut2,3 and plasma proteins.4 The regulation of protein synthesis is different in skeletal muscle versus other tissues (e.g., liver and the intestinal epithelium).
Importance of Skeletal Muscle
Skeletal muscle plays a vital role in maintaining adult health and response to critical illness. Healthy muscle is critical for metabolic stability and mobility. Thus, the maintenance of adequate muscle mass, strength, and metabolic function should be a primary focus when considering recommendations for dietary intake. The following are key functions of skeletal muscle and its impact on adult health.

Central role of whole-body protein metabolism
Essential tissues and organs, including the liver, brain, and heart etc., rely on adequate maintenance of protein turnover for health and survival. A steady supply of amino acids is necessary for protein synthesis to occur at rates that compensate for persistent protein breakdown in all tissues and organs. These amino acids are supplied to tissues and organs via the bloodstream. In the absence of adequate dietary protein, or in a state of impaired gastrointestinal absorption, muscle protein is the primary reservoir for these amino acids and the maintenance of protein synthesis in critical organs such as the liver, kidney, heart and immune cells. In a state of food deprivation, hepatic gluconeogenesis (the generation of glucose from non-carbohydrate sources in the liver) is essential to maintain blood glucose for the brain and nervous system. Glucose is produced from amino acids in an effort to regulate blood glucose levels, 4 and these amino acids come from muscle protein. When adequate muscle mass is available, plasma amino acid concentrations can be maintained via net muscle protein breakdown, resulting in adequate substrate to maintain essential body protein metabolism for both synthesis of essential proteins and gluconeogenesis, even in the absence of dietary protein.
Muscle protein synthesis is sensitive to amino acid lucine concentrations (figure 1A).
Figure 2. Leucine is a nutrient signal that activates the mTOR pathway for muscle protein synthesis.
Leucine
Leucine plays a unique role among amino acids as a dietary trigger required to initiate muscle protein synthesis (figure 2).11-13 The trigger for MPS is activation of the signal protein complex known as mTORC1 (mammalian target of rapamycin complex), which is critical in the regulation of translation initiation in skeletal muscle, but not in the liver. Only leucine among the essential amino acids has significant effects on mTORC1. If leucine is absent, the other amino acids have no potential to stimulate MPS.
Net muscle protein balance
The development of a healthy skeletal muscle mass, whether in children, healthy adults, adults with clinical conditions or the elderly, is determined from the net balance between the processes of muscle protein synthesis (MPS) and breakdown (MPB). These opposing processes are collectively called protein turnover, and allow muscles to undergo continuous repair, remodeling and development to adapt to physical demands. Net muscle protein balance (NMP) is constantly in flux: NMP = MPS – MPB (figure 3).
Physical activity accelerates protein turnover in skeletal muscle, increasing both MPS and MPB.18-20 During intense muscle activity (i.e., resistance or endurance exercise), MPS is inhibited while MPB remains high, resulting in net catabolism. Muscle protein breakdown contributes to intracellular amino acid levels, and likely plays a role in maintaining the balance of EAA for synthesis of stress response proteins.4 When damaged proteins are removed and degraded, their constituent amino acids can be recycled for synthesis of new proteins. Subsequent repair of damaged muscle and development of new muscle occurs under the process known as anabolism, where MPS is greater than MPB and accelerated by consuming adequate quantities of high quality protein soon after exercise.
Muscle protein synthesis is a highly regulated and responsive process, representing the primary driver of protein turnover, and ultimately changes in NMP balance. Particularly relevant for athletes, there is a well-documented synergistic effect on MPS when resistance exercise is followed by consumption of dietary amino acids.21,22 This stimulated increase in MPS can dramatically shift NMP balance from negative to positive, resulting in net muscle protein gain.23
On the other hand, growth and repair of other tissue is sensitive to energy status (figure 1B). This differential regulation allows the liver to maintain essential protein synthesis as long as energy is available, while skeletal muscle will only produce an anabolic response when dietary protein is adequate.

Muscle mass, strength, and metabolic function are central characteristics for exercise performance, as well as activities of daily living (ADL). Aging is accompanied by a progressive loss of muscle mass and function, known as sarcopenia (figure 1). This common phenomenon has a dramatic impact on life quality and survival. Sarcopenia commonly leads to frailty, an increased incidence of falls and hindrance to performing ADL. Maintaining muscle mass and preventing or slowing the development of sarcopenia can prolong quality of life during the aging process.



As life expectancy moves older, the most serious health risks are the loss of functional mobility
and a decline in capacity to maintain activities of daily living (ADL). Loss of muscle mass,
strength, and metabolic flexibility lead to an array of health risks including falls, bone fractures,
obesity, insulin insensitivity, and diabetes. Maintaining the health of skeletal muscle is central
to adult health and dietary protein is critical for muscle health.

Renal Function
Potential stress of high-protein diets on renal function in older adults is a frequent concern. However, research studies have shown little or no evidence that high-protein diets cause kidney damage in healthy individuals.

Benefits of Increased Dietary Protein Intake for Older Adults Increased dietary protein ingestion in older adults helps maintain functionality, enhance recovery from illness, and support overall good health.

Increased protein intake is associated with:

-Increased muscle mass and strength12
-Higher bone mass density13-15
-Slower rate of bone loss4
-Reduced general health problems in older women
Physical Activities & Healthy Aging
Nutrition needs for athletes depend on the unique demands of their sport. Although specific nutrition needs differ among athletes, all athletes must optimize muscle strength and performance. Dietary protein intake has a significant impact on athletic performance and recovery. Athletes seek to maintain energy for optimal performance, achieve rapid muscle recovery and avoid injuries. Whey protein isolate is used by athletes to build and repair muscles, to improve body composition with increased lean muscle mass and reduced fat, and to enhance performance with greater strength and endurance.

Muscle Catabolism and Anabolism
Physical activity accelerates protein turnover in skeletal muscle, increasing both protein synthesis and breakdown. During intense muscle activity, muscle protein breakdown (MPB) exceeds muscle protein synthesis (MPS), creating a catabolic period of tissue breakdown.
Subsequent recovery and repair of damaged muscle proteins is critical for maximum benefit of exercise training, and is dependent on consuming adequate quantities of high quality protein soon after exercise.
Particularly relevant for athletes, there is a synergistic effect on MPS when resistance exercise is followed by consumption of dietary amino acids.
Protein stimulation of MPS can dramatically shift net muscle protein (NMP) balance from negative to positive, resulting in net muscle protein gain.
Sports Nutrition
Mobility
Metabolism and weight management
Total energy expenditure (TEE) is the sum of resting energy expenditure (REE), the thermic
effect of food (TEF), and energy expenditure related to physical activity (AEE).

TEE = REE + TEF + AEE

REE is the amount of energy required by the body during a 24-hour period to function under resting conditions and has the largest impact on TEE (~60-70%). Energy expenditure of muscle during resting conditions is primarily due to synthesis and breakdown of muscle protein. When physical activity is performed, muscle solely contributes to energy expenditure which accounts for 15-30% of TEE. Overall, muscle accounts for ~ 35% of daily energy expenditure for sedentary individuals and over 50% for active adults. More muscle mass translates to higher rates of REE, which are directly related to a higher metabolism, known as a key regulator of weight management (figure 2).


Muscle Mass & Metabolism
Preserving a good ratio of lean muscle mass to adipose tissue and appetite control are two major elements involved in maintaining a healthy body weight. Research has shown that higher protein intake during a reduced-calorie diet can improve total weight loss and increase the percentage of fat loss while maintaining lean tissue.
PRESERVE LEAN MUSCLE
• Muscle mass and function are keys to long-term
weight management and adult health.6
• Diets containing 25-30g of high quality protein (2.5g
leucine) per meal and reduced carbohydrate protect
metabolically active lean muscle mass during weight
loss/maintenance and increase loss of body fat.7
• Leucine* serves as a nutrient signal to trigger
initiation of muscle protein synthesis to repair and
replace body proteins.
• Muscle protein synthesis is a major factor in energy
expenditure accounting for up to 40% of calorie
burning after a high quality protein meal.
• BiPRO is one of the best sources of leucine.
THERMOGENESIS
• The thermic effect of a food (TEF) is defined as
the increase in energy expenditure above the resting
metabolic rate due to processing ingested nutrients.
• The composition of a meal influences the thermic
effect. TEF of protein is ~20%–35% of energy
consumed while the TEF of carbohydrates and fat is
only ~5%–15%. 12-14
• The high thermic effect of proteins arises from the
initiation of protein synthesis in muscle after each
meal. This metabolic process stimulates energy use
in muscles and results in boosted fat burning.
SATIETY
• The extent of fullness, both in degree and time
span, deters snacking between meals. Diets higher in
protein have been shown to increase satiety more than
carbohydrates or fats.8
• Satiety involves a complex and integrated response
of hormonal, neurological and physical responses. 9,10
These responses appear to relate to the dietary levels
of leucine and aromatic amino acids (tryptophan and
phenylalanine) regulating hormones in the blood and
neurological signals in the brain.
• Neurological outcomes relate to brain responses to
tryptophan and serotonin or to leucine and signals to
the hypothalamus.11
• BiPRO is a rich source of leucine and aromatic amino
acids.
GLYCEMIC CONTROL
• Improved glycemic control is of critical importance
for weight management, type 2 diabetes, and Metabolic
Syndrome. Replacement of dietary carbohydrates with
protein improves glycemic control by:
• Improving postprandial insulin response
• Minimizing postprandial glucose spikes
• Enhancing gluconeogenesis to stabilize blood
glucose between meals
• Gluconeogenesis is a metabolic pathway that
generates glucose mostly from amino acids to
keep blood glucose levels from dropping too low
(hypoglycemia).
• Branched chained amino acids (BCAAs), specifically
leucine, have unique roles in metabolic regulation:
• Maintenance of glucose homeostasis by enhancing
recycling of glucose
• Regulation of insulin signaling cascade
Appetite Control
Dietary Protein Needs for Healthy Older Adults
Recent studies suggest that older populations benefit from a higher dietary protein intake than
currently recommended.
Current dietary protein intake recommendation for all adults: 0.8 g/kg BW/d
Suggested dietary protein intake for older adults (> 65 years): at least 1.0-1.2 g/kg BW/d

Elderly adults have increased dietary protein needs due to several factors:

Reduced ability to use available protein
Anabolic resistance to muscle protein synthesis
High splanchnic extraction
Insulin resistance
Immobility
Inadequate intake of protein
Appetite loss/anorexia
Gastrointestinal irregularities
Increased need for protein
Inflammatory disease
Increased oxidative protein modification
Chronic and acute diseases common to normal aging

Whey proteins are known to be a good source of
branched chain amino acids, including the essential
amino acid leucine. The leucine contained in individual
proteins is a critical factor in determining the amount
of protein required at a meal. In addition to being used
as a substrate, leucine performs the key role as a dietary
trigger for skeletal muscle to begin the synthesis
process.1,2,3 This is of critical importance because if
the meal has less than 2.0 grams of leucine, muscle
synthesis will not initiate and the protein is used as
calories.1,4
Importance of Leucine

Whey proteins are known to be a good source of
branched chain amino acids, including the essential amino acid leucine. The leucine contained in individual proteins is a critical factor in determining the amount of protein required at a meal. In addition to being used
as a substrate, leucine performs the key role as a dietary trigger for skeletal muscle to begin the synthesis process.1,2,3 This is of critical importance because if the meal has less than 2.0 grams of leucine, muscle synthesis will not initiate and the protein is used as calories.
IMPORTANCE OF LEUCINE
Dietary Protein Needs for Healthy Older Adults
Recent studies suggest that older populations benefit from a higher dietary protein intake than currently recommended.

Current dietary protein intake recommendation for all adults: 0.8 g/kg BW/d

Suggested dietary protein intake for older adults (> 65 years): at least 1.0-1.2 g/kg BW/d

Elderly adults have increased dietary protein needs due to several factors:

Reduced ability to use available protein
-Anabolic resistance to muscle protein synthesis
-High splanchnic extraction
-Insulin resistance
-Immobility
 Inadequate intake of protein
-Appetite loss/anorexia
-Gastrointestinal irregularities

 Increased need for protein
-Inflammatory disease
-Increased oxidative protein modification
-Chronic and acute diseases common to normal aging
Nutritionally, not all proteins are created equally;
different proteins have different amino acid profiles. Depending on the leucine content of the particular
protein, 2.5 grams of leucine corresponds to about
20-40 grams of total protein. Thus, on average,
30 grams of protein is recommended per meal to
supply adequate leucine to start protein synthesis.6
BiPRO, whey protein isolate produced from an ion
exchange method, has a leucine concentration of
13.1g leucine/100g protein. Our ion-exchange process allows us to select for native protein and minimal nonprotein nitrogen.

• BiPRO from Ion Exchange contains the
highest concentration of leucine compared
to other whey proteins and other protein
sources
PROTEIN QUALITY

Specific timing of dietary protein intake is crucial to maximizing its effects. Intense resistance exercise has been shown to increase rates of MPS for up to 48 hours after an acute bout of exercise for young individuals. However, exercise-induced increases in MPS are greatest immediately after exercise. Consumption of dietary protein after exercise has a synergistic effect with exercise on MPS and the anabolic effects may to last up to 48 hours post-exercise.
 Athletes should consume 15 g whey protein isolate (a less than optimally effective dose to stimulate MPS at a fasted meal) within 24 hours after resistance exercise. This effect of enhanced MPS response to protein ingestion has also been reported after low intensity endurance exercise if the activity is performed to exhaustion.
 It’s important for athletes to consume sufficient protein containing 2.5 g of leucine at each meal because MPS only occur during the 3-hour period after a meal.
Timing of Protein Intake: Window of Anabolic Potential after Resistance Exercise
Dietary proteins differ in protein quality based on their amino acid profile and digestion/absorption kinetics. The quality of the protein directly impacts the postprandial (after a meal) MPS response and in turn, net muscle protein balance.9,10 Whey proteins are a rich source of branched chain amino acids, including the essential amino acid leucine. Ingestion of whey protein results in a higher magnitude and more rapid postprandial peak plasma leucine and EAA concentration (figure 2). This results in significantly increased MPS compared to ingestion of casein, casein hydrolysate, minced beef, or steak (figure 3) where postprandial plasma leucine appears at a slower rate and lower magnitude
Whey Protein Isolate – The Ideal Protein for Skeletal Muscle Health
Digestion & Absorption
Differences in digestion and absorption kinetics between whey protein and casein have established these proteins as “fast” and “slow” digestible proteins, respectively.14-16 The slow digesting casein has a bigger impact on visceral protein synthesis,17,18 while whey protein has a significant effect on skeletal muscle health. Hydrolyzing casein (CASH) can alter its digestion and absorption kinetics to be similar to a fast protein, although a greater concentration of plasma EAA and leucine are still observed for WPI compared to CASH.9,16 The high leucine concentration in whey protein (table 1) is one of the main attributes contributing to its superior anabolic properties.
Davisco’s BiPRO® and Alpha-lactalbumin are rich in leucine and as whey protein isolates, exhibit fast digestion and absorption kinetics making them ideal protein sources for development and protection of lean muscle mass and metabolic function.
Response to critical illness and chronic diseases:
During times of stress or critical illness, maintenance of protein synthesis in tissues and organs is vital to preventing rapid degeneration and encouraging recovery. Muscle protein is a primary source of amino acids necessary for whole-body protein synthesis, especially when adequate amino acids are absent from the diet, or when absorption from the gastrointestinal tract is impaired. The stressed state, associated with illnesses such as sepsis, cancer and traumatic injury, requires even greater demands for amino acids from muscle protein breakdown than during periods of nutrient deprivation.7 The demand for precursor amino acids for the synthesis of proteins during recovery from illness is significant. Physiologic responses may include synthesis of proteins involved in immune function or wound healing, as well as accelerated synthesis of acute phase proteins in the liver. Cachexia, a syndrome including rapid loss of weight, wasting of muscle mass, strength, and metabolic function, is often associated with critical illness (e.g., cancer, chronic obstructive pulmonary diseases, and chronic heart failure), and survival of these patient populations is highly dependent upon the extent of muscle mass loss.
Mechanism of Muscle Loss
Hospitalization, bed rest or periods of prolonged inactivity are common occurrences following physical injury or illness. The absence of physical activity results in loss in muscle mass and function which are strong predictors of future health including mobility and mortality.
• Consume 20-30 g of high quality protein containing at
least 2.5 g leucine at each meal.7,11-14
• The key amino acid for triggering MPS and
overcoming anabolic resistance is the essential amino
acid leucine.

• High quality whey protein isolate is exceptionally
high in leucine making it an ideal protein source.
BiPRO has the highest leucine concentration among
protein sources.

• Elderly inpatients typically do not consume enough
protein, despite being presented with adequate
quantities. BiPRO is an ideal source because it
produces the maximum anabolic effects with the least
amount of total protein.
• Young healthy adults subject to bed rest experience
loss of lower body lean muscle mass at a rate of 100-
200 g/week6-8, while older adults approach 600 g/
week.9 (Figure 1)
• Older adults are at an increased risk for loss of
muscle function during bed rest compared to younger
adults, as they start out with less lean muscle mass
and strength and have reduced potential for
recovery.10
• Prolonged loss of muscle mass and function in older
adults is called sarcopenia.
• Aging produces “anabolic resistance” reducing the
response of muscle protein synthesis (MPS) to dietary
protein and combined with a decrease in physical
activity are believed to be the causes of sarcopenia.
• Age-related anabolic resistance combined with
bed rest produces an acute loss of muscle mass and
strength often leading to a permanent loss in the
ability to perform activities of daily living postrecovery
and to early-onset morbidity.
Muscle loss can affect everyone but ricks are greater for older adults
In the absence of an aggressive countermeasure, muscle loss is an almost certain outcome of bed rest. Appropriate countermeasures include nutrition support and resistance exercise therapy.
Prevention of muscle loss during bed rest
Nutritional support – high quality protein
Bed Rest

• When possible, exercise should be incorporated in
close proximity to consumption of dietary protein.
• A synergistic effect on MPS is observed when
resistance exercise is followed by protein intake.15
• If resistance exercise is performed without adequate
protein intake, the benefits of the exercise therapy are
diminished.
Exercise
During periods of prolonged inactivity or bed rest, aggressive treatment is required to combat accelerated loss of muscle mass and strength. Incorporation of adequate quantities of high leucine containing proteins including BiPRO whey protein isolate into each meal are required to prevent permanent loss of muscle function.
Muscle mass maintenance is achieved through balancing
muscle protein synthesis (MPS) and muscle protein breakdown
(MPB). When the rate of MPB exceeds that of MPS the balance
is negative and muscle mass is lost. (Figure 3)












• Prolonged bed rest reduces MPS - the primary driver for
muscle loss.9,17,18
• Prolonged bed rest results in hormonal dysregulation and
an inflammatory response - accelerating muscle loss.3,19
Loss of lean leg mass during bed rest
Protein and Musculoskeletal Health
Low intake of dietary protein leads to a negative protein balance and the loss of lean body mass. Increasing dietary protein can minimize common musculoskeletal health problems observed in older adults, including sarcopenia and osteoporosis.
Sarcopenia
Sarcopenia is the loss of skeletal muscle mass and function as a natural part of the aging process, often coinciding with increased fat mass. Sarcopenia is a complex process, with a combination of factors responsible for its onset, including changes in anabolic hormones, sedentary lifestyle, insulin resistance, inadequate dietary protein or caloric intake, chronic disease and inflammation.2
Nutritional intervention with increased protein consumption can help maintain muscle mass and functional capacity throughout the health span of aging adults, by promoting muscle protein synthesis.

Osteoporosis
Osteoporosis is characterized by a decrease in bone mass and density, causing bones to become fragile and more likely to fracture. Dietary protein interacts synergistically with calcium to significantly and positively impact bone health.
 Adequate protein intake has been shown to be an essential factor to maintaining bone or minimizing bone loss in older adults.
 Strong muscles have a positive impact on bone density.
Healthly aging
The digestive loss of scelital musclue and streght assocoated with aging is referred to as sarcopenia.
Approxmatley 45% of older adults in the United States are affected by sarcopenia, a total number that will continue to increase as the population ages.
Consumption of an adequate amount of high quality protein throught the day can slow down sarcopenia with aging.
Sarcopenia
Time of Concumption
Managing Body Weight & Compostion
8. Kotler DP et al. 1989. Am J Clin Nutr 50:444 –7.
19. Kadar L et al. 2000. Ann N Y Acad Sci 904:584 –91.
20. Anker SD et al 2005. Ann Med 36:518 –29.
21. Paddon-Jones DP et al. 2004. JCEM 89(9):4351–8.
22. Kortebein P et al. 2007. JAMA 297:1772–1774.
23. Short KR et al. 2000. Curr Opin Clin Nutr Metab Car 39–44.
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