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Scientific Studies About Protein Balance

Extra Information for FAQ on Amino Acid Balance

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Discussion
Part Three: Proteins

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1.  Protein (PRO) is the third "energy nutrient" discussed in this lesson. Like carbohydrate and lipid, it is made up of hydrogen, oxygen, and carbon atoms. What makes the structure of protein different is that in addition to those three atoms, protein also contains nitrogen atoms. These nitrogen atoms give the name amino (nitrogen containing) to the amino acids which make up protein. While there are only 20 known amino acids, they can be combined in an infinite number of sequences. Think about the size of the dictionary. All the words in the dictionary are made from just 26 different letters. Now think of how many different kinds of proteins could be made from 20 amino acids if there were no restrictions on size, or on the way the amino acids could be combined. Amazing, isn't it? In fact, there may be as many as 10,000 different proteins in a single human cell!

Proteins perform many important functions in the body, including growth and maintenance; formation of enzymes, hormones, and antibodies; fluid and electrolyte balance; acid-base balance; and providing energy. All of these functions are essential to life, and without protein, we could not exist. Use the outline I have included to help you as you read Chapter 5. I have tried to highlight important information to help you in your understanding of this important nutrient.

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1. Classification
   1. Amino Acids--building blocks of proteins
      1. Essential amino acids--phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, histidine, lysine, and leucine

         Memory Aid: Pvt. Tim Hall (the "a" in hall stands for amino acid--not a specific one)

      2. Semiessential amino acids (conditionally indispensable)--cysteine and tyrosine can spare the need for two essential amino acids methionine and phenylalanine, respectively
      3. Nonessential amino acids--the body can make these amino acids when provided with nitrogen and other chemical fragments (C,H)
   2. Dipeptide--two amino acids bonded together
   3. Tripeptide--three amino acids bonded together
   4. Oligopeptide--more than three amino acids but less than 50
   5. Polypeptide--50-100 amino acids
   6. Protein--at least 100 amino acids (most foods contain just the large protein form)
2. Functions of Protein
   1. Body building--necessary for muscles, framework for mineral deposition, hair and nails, for immunity protection, etc.
   2. Growth and maintenance--cells are constantly dying and must be replaced; protein also is necessary to build new tissue
   3. Construction of enzymes, hormones, and antibodies
   4. Regulation of body processes, fluid movement, osmotic pressure, and control of acid-base balance
   5. Providing energy--if the diet does not contain enough carbohydrate, amino acids may be used for this purpose; gluconeogenesis is the process of turning amino acids into glucose.
3. Sources
   1. Complete Proteins--meat, fish, poultry, cheese, eggs, and milk; the proteins of these foods contain all the essential amino acids
   2. Incomplete Proteins--foods from plants; these foods are low in or lacking one or more of the essential amino acids
   3. Complementary (supplementary) Proteins--two protein foods, usually plants, each of which supply the amino acids missing in the other
4. Dietary Recommendations

   For healthy adults, the RDA (Recommended Dietary Allowance) for protein has been set at 0.8 grams for each kilogram (2.2 pounds) body weight. To determine your protein RDA:

   1. Find your ideal body weight.
   2. Convert pounds to kilograms (pounds divided by 2.2 1b/kg equals kilograms).
   3. Multiply by 0.8 g/kg to get your protein RDA in grams per day.

   Athletes need slightly more, but the increased need is well covered by a regular diet. For children who are growing, the RDA is higher per unit of body weight, and for infants it is the highest of all.

5. Protein-Energy Malnutrition (PEM)
   1. Kwashiorkor--protein deficiency
   2. Marasmus--protein and kcalorie deficiency

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Complete the following Self-Help Activities. Write your answers on your own paper. When you have completed the exercise, check your answers using the key provided in the Appendix of this course guide. Do not submit these exercises for grading.

1. Calculate the RDA for protein for Charlie, a 200-pound male. Charlie's desired weight is 180 pounds.
2. Calculate the grams of protein in the following meal, using the Exchange System (Appendix G, page A-78).

   3-oz. hamburger patty
   1 hamburger bun
   1/2 cup green beans
   1 small apple
   1 cup skim milk

HealthGate Document

Record 1 from database: MEDLINE

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Title

PROFORCE--a new, high-biologic-value protein product for athletes.

Author

Boyadzhiev N; Popov I; Hristov H

Address

University of Medicine, Department of Physiology, Plovdiv, Bulgaria.

Source

Folia Med (Plovdiv), 1992, 34:2, 35-8

Abstract

The protein product PROFORCE has been developed from a base of egg, milk and cereal using linear optimization. Its balanced composition has been specially designed to meet the physiological needs of athletes practicing endurance-demanding sports. A medicobiologic evaluation using a routine technique was performed using three concentration levels of protein feeding. This enhanced the range of the investigated parameters. The following results were obtained: Protein Efficiency Ratio (PER) = 2.64 +/- 0.22 (p < 0.001); Net Protein Ratio (NPR) = 3.27 +/- 0.22 (p < 0.001). Comparison with the control group shows that the protein product is of high quality. Albumin, cholesterol, triglycerides and total protein were determined for the three protein-feeding concentrations. The most favorable influence on the protein parameters and cholesterol levels were observed when feeding experimental rats on the nine-percent protein concentration. Amino acid content of the product was compared to a number of proteins of proven high quality. The comparison suggests that the product is suitable for athletes practicing endurance-demanding sports. The conclusion is that PROFORCE has a wide range of applications which would include use by athletes practicing aerobic sports.

Language of Publication

English

Unique Identifier

94010570

MeSH Heading (Major)

Dietary Proteins|*AD/IP

MeSH Heading

Animal; Food, Formulated; Human; Physical Endurance; Rats; Rats, Wistar; Sports; Weight Gain

Publication Type

JOURNAL ARTICLE

ISSN

0204-8043

Country of Publication

BULGARIA

CAS Registry/EC Number

0 (Dietary Proteins)

  Title

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Protein quality, amino acid balance, utilization, and evaluation of diets containing amino acids as therapeutic agents.

Author

Harper AE; Yoshimura NN

Address

Research Department, McGaw, Inc., Irvine, California 92713-9791.

Source

Nutrition, 1993 Sep-Oct, 9:5, 460-9

Abstract

Basic concepts of amino acid nutrition are summarized and quantitative amino acid requirements of different age-groups based on current knowledge are presented. The newer concepts of "conditionally indispensable" amino acids and organ-specific requirements for amino acids are discussed. The concepts of nitrogen balance, limiting amino acid, protein utilization, protein efficiency ratio, and amino acid score for determining protein quality are reviewed, and examples of low-, intermediate-, and high-quality proteins are provided. Problems in assessing efficiency of nitrogen utilization when single amino acids or amino acids in combination with balanced diets are used as therapeutic agents are discussed in relation to the potential roles of the branched-chain amino acids, arginine, and glutamine in trauma and as immunostimulators.

Language of Publication

English

Unique Identifier

94115115

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---

HealthGate Document

Record 1 from database: MEDLINE
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Title

Essential amino acid reference profile affects the evaluation of enteral feeding products [see comments]

Author

Dubin S; McKee K; Battish S

Address

Biomedical Engineering and Science Institute, Drexel University, Philadelphia, PA 19104.

Source

J Am Diet Assoc, 1994 Aug, 94:8, 884-7

Abstract

The chemical score is a measure of the predicted metabolic usefulness of a protein in a food based on the comparison (ratio or percentage) of the concentrations of the essential amino acids (EAAs) to a "profile" assumed to reflect the true needs of the body. The score for the limiting EAA is taken to represent the value of the food. Such a chemical score is particularly useful for therapeutic diets where bioassay (such as nitrogen-balance studies) in a large number of patients may be unethical or impractical. Although a major limitation to the chemical-score method previously was scarcity and/or imprecision of data about EAA concentrations in foods, this situation has been mitigated by modern analytic methods. The validity of a chemical score is also exquisitely sensitive to the EAA profile used for comparison. Chemical scores published for a variety of enteral and parenteral feeding products implied a low (approximately 50%) protein value. These computations were based on the EAA profile of egg protein. This pattern is sufficient, in most cases, for body needs, but it may be far more than is necessary. Recently published profiles, based on measurements in human beings of actual protein and EAA requirements, point to a more realistic chemical-score computation. These profiles accommodate age and lifestyle factors and provide greater flexibility in the formulation of therapeutic diets.

Language of Publication

English

Unique Identifier

94321709

MeSH Heading (Major)

Amino Acids, Essential|*AN; Dietary Proteins|*AN; Enteral Nutrition|*; Food, Formulated|*AN; Nutritional Requirements|*

MeSH Heading

Adolescence; Animal; Child; Human; Infant

Publication Type

JOURNAL ARTICLE

ISSN

0002-8223

Country of Publication

UNITED STATES

Record 2 from database: MEDLINE
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Title

The nutrition management of the patient with acute renal failure.

Author

Kopple JD

Address

Division of Nephrology and Hypertension, Harbor-UCLA Medical Center, Torrance 90509, USA.

Source

JPEN J Parenter Enteral Nutr, 1996 Jan, 20:1, 3-12

Abstract

The clinical status of patients with acute renal failure (ARF) varies greatly. Some individuals have only mild or moderate ARF or may have only mild perturbations of their metabolic status. Other patients exhibit a severe reduction in renal function with oliguria or anuria. Depending upon their comorbid conditions, ARF patients may be among the most hypercatabolic patients in the hospital. Clinical trials have not clearly shown a beneficial effect of nutrition support on morbidity or mortality in patients with ARF, although limitations in sample size and experimental design and inclusion of patients with widely disparate clinical conditions may have contributed to the difficulty in demonstrating benefits. Several recent therapeutic approaches that have been studied either in experimental animals with ARF or in small numbers of humans with ARF hold promise for improving clinical outcome. Continuous arteriovenous or venovenous hemofiltration with or without dialysis is such a therapy. In comparison to intermittent hemodialysis this former treatment more safely removes large quantities of water and solutes from critically ill patients with unstable hemodynamics and allows them to receive rather large quantities of nutrients, including amino acids. Also promising are studies in experimental animals with ARF which indicate that several growth factors may accelerate the recovery of renal function. In rats with ARF, insulin-like growth factor 1 both enhances recovery of renal function and suppresses their enhanced catabolism. For most patients with ARF requiring nutrition support, evidence suggests that both essential and nonessential amino acids should be employed. However, there appears to be a therapeutic role for small quantities of essential amino acids, without nonessential amino acids, in selected patients. Data support the importance of proactive measures to prevent fluid and electrolyte imbalances in patients with ARF.

Language of Publication

English

Unique Identifier

96380244

MeSH Heading (Major)

Kidney Failure, Acute|*TH; Nutritional Support|*

MeSH Heading

Amino Acids|AD; Animal; Growth Substances|TU; Hemodialysis; Hemofiltration; Human

Publication Type

JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL

ISSN

0148-6071

Country of Publication

UNITED STATES

Record 3 from database: MEDLINE
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Title

Plasma tryptophan to large neutral amino acids ratio and therapeutic response to a selective serotonin uptake inhibitor.

Author

Lucca A; Lucini V; Catalano M; Alfano M; Smeraldi E

Address

Istituto di Ricovero e Cura a Carattere Scientifico H. San Raffaele, Italia.

Source

Neuropsychobiology, 1994, 29:3, 108-11

Abstract

The molar ratio of total plasma tryptophan (Trp) to the sum of the other large neutral amino acids (LNAAs), thought to reflect brain serotonin (5-HT) formation, was estimated in 47 patients with major depression (unipolar and bipolar) before and after 6 weeks of treatment with a serotonin uptake inhibitor, fluvoxamine. We found a significant difference between responders (n = 39) and nonresponders (n = 8) for the pre- and in-treatment plasma Trp to LNAAs ratios. In contrast, there were no differences between the two groups for the mean plasma steady-state fluvoxamine levels. These findings suggest that a specific plasma amino acid profile may be a useful indicator of good clinical response to a selective 5-HT uptake inhibitor.

Language of Publication

English

Unique Identifier

94294069

MeSH Heading (Major)

Amino Acids|*BL; Bipolar Disorder|BL/*DT/PX; Depressive Disorder|BL/*DT/PX; Fluvoxamine|AE/*TU; Tryptophan|*BL

MeSH Heading

Adult; Aged; Dose-Response Relationship, Drug; Drug Administration Schedule; Female; Human; Male; Middle Age; Personality Inventory

Publication Type

CLINICAL TRIAL; JOURNAL ARTICLE

ISSN

0302-282X

Country of Publication

SWITZERLAND

HealthGate Document

Record 1 from database: MEDLINE
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Title

Controlled trial of oligopeptide versus amino acid diet in treatment of active Crohn's disease.

Author

Mansfield JC; Giaffer MH; Holdsworth CD

Address

Gastroenterology Unit, Royal Hallamshire Hospital, Sheffield.

Source

Gut, 1995 Jan, 36:1, 60-6

Abstract

Elemental diets are effective in inducing remission in active Crohn's disease, but how they exert this therapeutic effect is unclear. In a previous study a whole protein containing diet proved less effective than one in which food antigens were excluded, suggesting that exclusion of food antigens from the gut was a possible mechanism. This study was designed to test whether an oligopeptide diet of hydrolysed proteins was as effective as an amino acid based diet. These diets were equally antigen free but with different nitrogen sources. Forty four patients with active Crohn's disease were randomised in a controlled trial of amino acid versus oligopeptide diet. The feeds were given by nasogastric tube in equicaloric quantities and were the sole form of nutrition. Treatment was continued for four weeks although failure to improve by day 10 resulted in withdrawal. Quantitative leucocyte scintigraphy was used to investigate the effect of diet treatment on gut inflammation. Clinical and nutritional responses to treatment were also measured. Sixteen patients entered remission (including withdrawal of corticosteroids), six patients could not tolerate the nasogastric tube, and 22 patients failed to respond. The two diets were equally effective. Patients who responded had a rapid drop in clinical index of disease activity and a major reduction in the bowel uptake of leucocytes on scintigraphy. The oligopeptide and amino acid based enteral feeds were equally effective at inducing remission in active Crohn's disease. With both diets clinical improvement was accompanied by a reduction in intestinal inflammation.

Language of Publication

English

Unique Identifier

95197081

MeSH Heading (Major)

Amino Acids|*TU; Crohn Disease|RI/*TH; Enteral Nutrition|*MT; Food, Formulated|*; Oligopeptides|*TU

MeSH Heading

Comparative Study; Female; Human; Intestines|RI; Leukocytes|RI; Male; Organotechnetium Compounds|DU; Oximes|DU; Support, Non-U.S. Gov't; Treatment Outcome

Publication Type

CLINICAL TRIAL; JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL

ISSN

0017-5749

Country of Publication

ENGLAND

Record 2 from database: MEDLINE
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Title

Determinants of protein turnover in health and disease.

Author

Newby FD; Price SR

Address

Renal Division, Emory University, Atlanta, Ga. 30322, USA.

Source

Miner Electrolyte Metab, 1998, 24:1, 6-12

Abstract

Protein synthesis, protein degradation, and amino acid oxidation are tightly regulated to preserve lean body mass in healthy individuals. An adaptative response to a reduction in dietary protein in normal adults is decreased branched-chain amino acid oxidation which increases the availability of amino acids. In nephrosis, reduced branched-chain amino acid oxidation decreases amino acid requirements and helps to compensate for urinary protein loss. Conversely, uremia and other catabolic diseases are associated with muscle wasting resulting from activation of the ubiquitin-proteasome proteolytic pathway and branched-chain ketoacid dehydrogenase, the rate-limiting enzyme for branched-chain amino acid catabolism. By understanding the processes responsible for muscle wasting in catabolic states, therapeutic interventions may be designed to improve protein balance.

Language of Publication

English

Unique Identifier

98059800

MeSH Heading (Major)

Health Status|*; Proteins|BI/*ME

MeSH Heading

Adult; Amino Acids, Branched-Chain|ME; Dietary Proteins|AD; Human; Muscle Proteins|ME; Nephrotic Syndrome|ME; Oxidation-Reduction; Support, U.S. Gov't, P.H.S.; Uremia|ME

Publication Type

JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL

ISSN

0378-0392

Country of Publication

SWITZERLAND

Record 3 from database: MEDLINE
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Title

Oxidative stress: free radical production in neural degeneration.

Author

Götz ME; Künig G; Riederer P; Youdim MB

Address

Department of Psychiatry, University of WÂurzburg, Germany.

Source

Pharmacol Ther, 1994, 63:1, 37-122

Abstract

It is not yet established whether oxidative stress is a major cause of cell death or simply a consequence of an unknown pathogenetic factor. Concerning chronic diseases, as Parkinson's and Alzheimer's disease are assumed to be, it is possible that a gradual impairment of cellular defense mechanisms leads to cell damage because of toxic substances being increasingly formed during normal cellular metabolism. This point of view brings into consideration the possibility that, besides exogenous factors, the pathogenetic process of neurodegeration is triggered by endogenous mechanisms, either by an endogenous toxin or by inherited metabolic disorders, which become progressively more evident with aging. In the following review, we focus on the oxidative stress theory of neurodegeneration, on excitotoxin-induced cell damage and on impairment of mitochondrial function as three major noxae being the most likely causes of cell death either independently or in connection with each other. First, having discussed clinical, pathophysiological, pathological and biochemical features of movement and cognitive disorders, we discuss the common features of these biochemical theories of neurodegeneration separately. Second, we attempt to evaluate possible biochemical links between them and third, we discuss experimental findings that confirm or rule out the involvement of any of these theories in neurodegeneration. Finally, we report some therapeutic strategies evolved from each of these theories.

Language of Publication

English

Unique Identifier

95062559

MeSH Heading (Major)

Alzheimer Disease|DT/*ME/PP; Nerve Degeneration|*; Oxidative Stress|*

MeSH Heading

Animal; Antioxidants|TU; Cell Death; Cognition|PH; Energy Metabolism; Excitatory Amino Acids|PH; Free Radicals; Human; Mitochondria|DE/PH; Movement Disorders|DT/ME/PP; Reactive Oxygen Species|AE; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC

ISSN

0163-7258

Country of Publication

ENGLAND

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