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Centro di Studio per la Fisiopatologia dello Shock CNR, Catholic University, Rome, Italy and * Department of Surgery, UMDNJ, Newark, NJ
1To whom correspondence should be addressed.
 |
ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONSUBJECTS AND METHODSRESULTSDISCUSSIONREFERENCES |
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KEY WORDS: • taurine • humans • sepsis • parenteral nutrition • plasma amino acids
|
INTRODUCTION |
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TOPABSTRACTINTRODUCTIONSUBJECTS AND METHODSRESULTSDISCUSSIONREFERENCES |
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, Hayes 1988a
and 1988b
,
Huxtable and Barbeau 1976
, Huxtable 1992
,
Kendler 1989
, Neary et al. 1997
,
Redmond et al. 1998
, Stapleton et al. 1998
, Watson et al. 1995
, Wright et al. 1986
). The available knowledge is limited to reports of
decreased plasma Tau in trauma, sepsis and critical illnesses
(Askanazi et al. 1980
, Gray et al. 1994
,
Jeevanandam et al. 1990
and 1995
, Neary et al. 1997
, Paauw and Davis 1990
, Vente et al. 1989
). In particular, little is known about the relationship
between changes in plasma Tau and in other AA levels. This is important
due to specific properties that render Tau unique with respect to the
other AA. Tau is not incorporated into proteins, which may dissociate
Tau levels from changes in protein synthetic and catabolic rates, and
from the consequent changes in the plasma AA pool. In addition, Tau
differs from the more familiar AA not only for being a sulfonic rather
than a carboxylic AA, but also for being a ß-AA rather than an
-AA. This latter feature involves dependency of Tau on a distinct
intracellular AA transport system, system ß, and supports the
independence of Tau from well-known alterations in other transport
systems (such as system A), which are major determinants of changes in
the plasma AA pool in sepsis.
Moreover, there is a specific need to characterize the relationship
between plasma Tau and other AA levels not only in septic patients
under standard total parenteral nutrition (TPN) but also in patients
undergoing modified TPN with high doses of branched-chain amino
acids (BCAA). In fact, the latter regimen is at present a customary
practice in many countries; it has been shown to significantly affect
protein synthetic and catabolic rates and plasma AA interactions
(Bower et al. 1986
, Cerra et al. 1982
,
Chiarla et al. 1988
, Freund et al. 1978
,
Skeie et al. 1990
), and there is evidence of a modified
response of Tau, compared with most of the other AA, to leucine
infusion in normal subjects (Hagenfeldt et al. 1980
,
Sherwin 1978
). Our study was performed to assess the
relationships among plasma Tau, levels of the other AA, doses of BCAA
and variables quantifying severity of metabolic and cardiorespiratory
impairment in two groups of septic patients randomly selected to
undergo standard or modified (high BCAA) TPN support.
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SUBJECTS AND METHODS |
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TOPABSTRACTINTRODUCTIONSUBJECTS AND METHODSRESULTSDISCUSSIONREFERENCES |
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). Neither solution contained Tau, Glu or Asp. Doses of nonprotein
energy sources and of total AA did not differ among groups. Group
Sep-A and Sep-B also did not differ in body weight (72.9
± 9.9 vs. 75.9 ± 12.8 kg), height (174 ± 8 vs. 175
± 6 cm), body surface area (1.87 ± 0.16 vs. 1.91 ± 0.16 m2) (Du Bois and Du Bois 1916
), ratio of actual to ideal body weight (1.11 ± 0.09
vs. 1.14 ± 0.18) (Metropolitan Life Insurance Company 1984
), estimated lean body mass (52.6 ± 6.6 vs. 54.4
± 5.1 kg) (Hume 1966
), mortality rate (12.5 vs.
25%), age (25 ± 6 vs. 32 ± 19 y) and sex
distribution, injury severity score (a widely used anatomic trauma
severity index: medians 31 vs. 30, ranges from 14 to 48 and from 11 to
54, respectively) (Greenspan et al. 1985
) and sepsis
severity score (medians 30 vs. 28, ranges from 9 to 54 and from 11 to
51, respectively) (Skau et al. 1985
, Stevens 1983
). Group Sep-A included eight patients (3 women, 5 men)
after motor vehicle accidents (n = 6) or gunshot wounds
(n = 2), with combinations of severe abdominal, chest
and head injuries. The source of sepsis was intra-abdominal
(n = 3), pulmonary (n = 4) or extensive
infection of a lower limb (n = 1). One patient died of
multiple organ dysfunction syndrome (MODS). Group Sep-B included 8
patients (2 women, 6 men) after motor vehicle accidents (n
= 7) or gunshot wounds (n = 1), also with
combinations of severe abdominal, chest and head injuries. The source
of sepsis was intra-abdominal (n = 3),
retroperitoneal (n = 1), pulmonary (n = 1) or extensive infection of upper or lower limbs (n = 3). One patient died of MODS, one of acute myocardial failure. Sepsis
was diagnosed on the basis of the simultaneous presence of a
temperature >38.3°C, a white blood cell count >12,000 or <3000
cell/mm3 and clear evidence of a source of
infection, confirmed by positive blood cultures, positive cultures from
the surgical drainage of infected areas (or positive sputum cultures in
the case of pulmonary infections) (Chiarla et al. 1988
).
Cases without undoubtedly proven diagnosis of sepsis were excluded. No
patient had oliguric renal failure. The duration of study for each
patient was determined by onset and duration of sepsis. The
prerandomization period (up to onset of sepsis) lasted 4 ± 2 d in Group Sep-A and 5 ± 2 d in Group Sep-B.
Measurements performed during this period were separated into the
following groups: measurements performed in presepsis patients
receiving a standard mixed AA solution, before randomization to Group
Sep-A (Group Pre-Sep-A) (n = 33) and measurements
performed in presepsis patients receiving the same AA solution, before
randomization to Group Sep-B (Group Pre-Sep-B) (n = 38). Thereafter, the study was carried out until criteria for
persistent sepsis were fully met, or until death in a septic state
occurred, i.e., for 10 ± 5 d in Group Sep-A and 8
± 4 d in Group Sep-B. Plasma samples for AA
determinations, which were obtained daily before randomization and then
every 8 h during sepsis to account for diurnal variation, were
analyzed in a Beckman AA analyzer (Beckman Instruments, Palo Alto, CA).
Samples for AA analysis were prepared according to the standard
procedures indicated for use of the Beckman 6300 AA analyzer.
Measurements also included the determination of plasma cholesterol and
lactate, and cardiorespiratory variables such as cardiac index (CI) by
the thermodilution method
(L·min-1·m-2)
(Oximetrix 3, Abbott Laboratories, Critical Care Products, Morgan Hill,
CA), arteriovenous O2 concentration difference
(a-vDO2, mL/100 mL) and respiratory index (RI,
units) to assess the severity of metabolic and cardiorespiratory
impairment (Giovannini et al. 1999
, Siegel et al. 1979
).
|
). The protocol complied with the Helsinki
Declaration as revised in 1983, and was approved by the Institutional
Ethical Committee. |
RESULTS |
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TOPABSTRACTINTRODUCTIONSUBJECTS AND METHODSRESULTSDISCUSSIONREFERENCES |
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), were significantly higher in Group Sep-B compared with Sep-A
(Table 3
). In both Groups Sep-A and Sep-B, Tau had strong direct
relationships with Asp, Glu, ß-alanine (ß-Ala) and
phosphoethanolamine (Pea) (r2 > 0.36,
P < 0.001) and was unrelated or weakly related
(r2 < 0.05) to the other AA.
Covariance analysis showed a significantly greater slope in Group
Sep-B than in Sep-A for the relationships of Tau with Asp, Glu
and Pea, whereas covariance for ß-Ala was not significant
(P = 0.08) (Table 4
). Group Sep-B had higher concentrations of Tau, Asp, Glu, ß-Ala
and Pea, and lower concentrations of the other AA than Group Sep-A.
Differences in leucine, isoleucine and valine could be related to the
higher dose of these three amino acids administered in Group Sep-B.
These differences provided further evidence of associations among
plasma Tau, Asp, Glu, ß-Ala and Pea. Because these AA were not being
administered (Table 1)
, differences in levels in Group Sep-B
compared with Sep-A might be an indirect consequence of the
modified TPN support. Regression analysis was performed on substrate
doses for Groups Sep-A and Sep-B combined. Tau levels were
unrelated to doses of glucose, fat and non-BCAA, whereas a
significant direct relationship was found with the BCAA dose
(r2 = 0.20, P < 0.001, Table 4
). Weaker direct correlations with the BCAA dose were
found for Asp, Glu and Pea (r2 <
0.08, P < 0.05 for all).
|
|
|
and Fig. 1
). Thus, decreasing Tau was associated with signs of worsening of
metabolic and cardiorespiratory function, without differences between
Group Sep-B and Group Sep-A.
|
|
|
DISCUSSION |
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TOPABSTRACTINTRODUCTIONSUBJECTS AND METHODSRESULTSDISCUSSIONREFERENCES |
|---|
, Redmond et al. 1998
, Stapleton et al. 1998
, Watson et al. 1995
). Indeed, the
post-traumatic fall in plasma Tau is thought to reflect an abrupt
increase in requirements for host-defense and reparative processes,
whereas partial recovery toward less abnormal Tau levels when sepsis
develops should reflect enhanced supply from endogenous sources to
balance requirements (Askanazi et al. 1980
, Gray et al. 1994
, Hashiguchi et al. 1997
,
Hofford et al. 1996
, Jeevanandam et al. 1990
and 1995
, Neary et al. 1997
, Paauw and Davis 1990
, Redmond et al. 1998
, Stapleton et al. 1998
, Vente et al. 1989
, Watson et al. 1995
). Although modifications of Tau levels under these
conditions are not fully characterized, this trend was reproduced in
the measurements in our study. An important role of Tau in
host-defense and anti-inflammatory protection is suggested by
the maintenance of high Tau concentrations in neutrophils and
lymphocytes, even in the presence of reduced Tau availability
(Gaull 1986
, Kopple et al. 1990
,
Neary et al. 1997
, Redmond et al. 1998
,
Soupart 1962
, Stapleton et al. 1998
,
Vinton et al. 1986
and 1987
), with the observation of a
progressive fall in plasma Tau when sepsis worsens and evolves toward
MODS and death. This tendency of plasma Tau to decrease with the
worsening of metabolic and cardiorespiratory patterns was observed also
in our study (Table 5
, Fig. 1
). In addition, low Tau was part of the
preterminal pattern in both patients who died of MODS, although the
value of a similar observation in only two patients is limited.
Sepsis is characterized by dramatic changes in protein and AA
metabolism and turnover. The assessment of changes in plasma Tau levels
with respect to levels of other AA seem relevant, given its unusual
role; however, this aspect has remained unexplored. The results in our
study showed that plasma Tau varies independently of changes in most
other AA levels. Exceptions were Glu, Asp, ß-Ala and Pea, whose
changes were related directly to those of Tau (moreover, with
increasing leucine, isoleucine and valine doses, levels of these AA
increased with those of Tau, whereas levels of the other AA were
generally decreased). These relationships were not totally unexpected,
given the structural similarities and the physicochemical properties
that may involve a balance in levels of these AA. These include, for
example, competition for intracellular AA transport system and binding
to membrane enzymes and receptors, metabolic relationships linking
ß-Ala and Tau precursors, and other mechanisms involving covariation
of plasma and tissue levels of these AA (e.g., simultaneous involvement
in osmoregulation) (Griffith 1983
and 1986
,
Hofford et al. 1996
, Lehmann et al. 1985
,
Lehmann 1989
, Milakofsky et al. 1985
,
Schaffer et al. 1995
, Shotwell et al. 1983
, Wu 1976
). However, the relationships found
among Tau, Glu and Asp are particularly interesting, especially when
their parallel increases at high leucine, isoleucine and valine doses
(Group Sep-B) are considered. Although the increases in Glu and Asp in
Group Sep-B may depend on increased substrate availability and
transformation (the BCAA are precursors of both Glu and Asp, and there
is an equilibrium between Glu and Asp interconversion) (Skeie et al. 1990
), the correlations with Tau may support an effect of
increased BCAA dose on Tau synthesis. This is because Glu and Asp are
also interrelated metabolically with cysteinesulfinic acid, which is a
precursor of Tau (it is an intermediate in the synthesis of Tau from
cysteine) (Hayes 1988a
and 1988b
,
Stipanuk 1986
). To our knowledge, the outcomes of these
interactions have not been explored previously in clinical studies.
Their importance should be assessed also because the higher plasma Tau
in Group Sep-B occurred with an AA solution containing a lower dose
of other precursors of Tau (although serine was an exception, the total
sum of moles of methionine, serine, threonine and glycine was lower).
There is another relevant aspect of these interactions. Both Tau and
glutathione have antioxidative roles, and both rely on similar
substrates for synthesis. Actually, Glu and cysteine are precursors of
glutathione and of Tau (cysteinesulfinate is a by-product of
cysteine). This may lead to competition for substrate when demand for
antioxidant protection increases; in effect, decreased plasma levels of
sulfur AA in sepsis have been considered to be a consequence of AA
utilization to enhance glutathione synthesis, and this same mechanism
has been suggested to explain the fall in Tau (Grimble 1993
and 1994
, Hashiguchi et al. 1997
, Malmezat et al. 1998
). On the basis of these considerations, high dose BCAA
might potentiate antioxidant protection by supporting the synthesis of
both Tau and glutathione, a possibility that should be investigated in
further studies.
In conclusion, our results provide an insight into features of Tau that
remain incompletely understood, characterizing the relationships with
plasma levels of other AA, with TPN substrate doses, and with metabolic
and cardiorespiratory variables in septic patients. More study is
required to characterize fully Tau metabolism and interactions in
sepsis. Beyond an improvement in understanding of pathophysiology,
there are also therapeutic implications. These relate to evidence that
Tau availability is associated with better preservation of effector
cell function in host defense, decreased susceptibility to host tissue
damage after activation of inflammatory cells and protection against
proinflammatory mediator-induced lung and liver dysfunction
(Banks et al. 1992
, Cantin 1994
,
Gordon et al. 1992
, Grimble 1993
and
1994
, Guertin et al. 1993
,
Malmezat et al. 1998
, Pathirana and Grimble 1992
, Redmond et al. 1996
, Schuller-Levis et al. 1994
, Stapleton et al. 1998
).
|
FOOTNOTES |
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Manuscript received January 7, 2000. Initial review completed February 14, 2000. Revision accepted May 16, 2000.
|
REFERENCES |
|---|
|
TOPABSTRACTINTRODUCTIONSUBJECTS AND METHODSRESULTSDISCUSSIONREFERENCES |
|---|
1. Askanazi J., Carpentier Y. A., Michelsen C. B., Elwyn D. H., Fürst P., Kantrowitz L. R., Gump F. E., Kinney J. M. Muscle and plasma amino acids following injury: influence of intercurrent infection. Ann. Surg. 1980;192:78-95[Medline]
2. Banks M. A., Porter D. W., Martin W. G., Castranova V. Taurine protects against oxidant injury to rat alveolar pneumocytes. Lombardini J. B. Schaffer S. W. Azuma J. eds. Taurine: Nutritional Value and Mechanism of Action 1992:341-354 Plenum Press New York, NY. (Adv. Exp. Med. Biol. 315 341–354)
3. Belli D. C. Taurine and TPN solutions?. Nutrition 1994;10:82-84[Medline]
4. Bower R. H., Muggia Sullam M., Vallgren S., Hurst J. M., Kern K. A., LaFrance R., Fischer J. E. Branched chain amino acid-enriched solutions in the septic patient. A randomized, prospective trial. Ann. Surg. 1986;203:13-20[Medline]
5. Cantin A. M. Taurine modulation of hypochlorous acid-induced lung epithelial cell injury in vitro. J. Clin. Investig. 1994;93:606-614
6. Cerra F. B., Upson D., Angelico R., Wiles C., III, Lyons L., Faulkenbach L., Paysinger J. Branched chains support postoperative protein synthesis. Surgery 1982;92:192-199[Medline]
7. Chiarla C., Siegel J. H., Kidd S., Coleman B., Mora R., Tacchino R., Placko R., Gum M., Wiles C. E., III, Belzberg H. Inhibition of post-traumatic septic proteolysis and ureagenesis and stimulation of acute-phase protein production by branched-chain amino acid TPN. J. Trauma 1988;28:1145-1172[Medline]
8. Du Bois D., Du Bois E. F. A formula to estimate the approximate surface area if height and weight be known. Arch. Intern. Med. 1916;17:863-871
9. Freund H. R., Ryan J. A., Fisher J. E. Amino acid derangements in patients with sepsis: treatment with branched-chain amino acid rich infusion. Ann. Surg. 1978;188:423-430[Medline]
10. Gaull G. E. Taurine as a conditionally essential nutrient in man. J. Am. Coll. Nutr. 1986;5:121-125[Medline]
11. Giovannini I., Boldrini G., Chiarla C., Giuliante F., Vellone M., Nuzzo G. Pathophysiologic correlates of hypocholesterolemia in critically ill surgical patients. Intensive Care Med 1999;25:748-751[Medline]
12. Gordon R. E., Heller R. F., Heller R. F. Taurine protection of lungs in hamster models of oxidant injury: a morphologic time study of paraquat and bleomycin treatment. Lombardini J. B. Schaffer S.W. Azuma J. eds. Taurine: Nutritional Value and Mechanism of Action 1992:319-328 Plenum Press New York, NY. (Adv. Exp. Med. Biol. 315 319–328)
13. Gray G. E., Landel A. M., Meguid M. M. Taurine-supplemented total parenteral nutrition and taurine status of malnourished cancer patients. Nutrition 1994;10:11-15[Medline]
14. Greenspan L., McLellan B. A., Greig H. Abbreviated Injury Scale and Injury Severity Score: a scoring chart. J. Trauma 1985;25:60-64[Medline]
15.
Griffith O. W. Cysteinesulfinate metabolism. Altered partitioning between transamination and decarboxylation following administration of ß-methyleneaspartate. J. Biol. Chem. 1983;258:1591-1598
16.
Griffith O. W. ß-Amino acids: mammalian metabolism and utility as -amino acid analogues. Annu. Rev. Biochem. 1986;55:855-878[Medline]
17. Grimble R. F. The maintenance of antioxidant defenses during inflammation. Wilmore D. W. Carpentier Y. A. eds. Metabolic Support of the Critically Ill Patient 1993:347-363 Springer Verlag Berlin, Germany.
18. Grimble R. F. Nutritional antioxidants and the modulation of inflammation: theory and practice. New Horizons 1994;2:175-185[Medline]
19. Guertin F., Roy C. C., Lepage G., Yousef I., Tuchweber B. Liver membrane composition after short term parenteral nutrition with and without taurine in guinea pigs: the effect of taurine. Proc. Soc. Exp. Biol. Med. 1993;203:418-423[Medline]
20. Hagenfeldt L., Eriksson S., Wahren J. Influence of leucine on arterial concentrations and regional exchange of amino acids in healthy subjects. Clin. Sci. (Lond.) 1980;59:173-181[Medline]
21. Hashiguchi Y., Fukushima R., Saito H., Naka S., Inaba T., Lin M. T., Muto T. Interleukin-1 and tumor necrosis factor alter plasma concentration and interorgan fluxes of taurine in dogs. Shock 1997;7:147-153[Medline]
22. Hayes K. C. "Vitamin-like" molecules: taurine. Shils M. E. Young V. R. eds. Modern Nutrition in Health and Disease 7th ed. 1988a Lea & Febiger Philadelphia, PA.
23. Hayes K. C. Taurine nutrition. Nutr. Res. Rev. 1988b;1:99-113
24. Hofford J. M., Milakofsky L., Pell S., Vogel W. A profile of amino acid and catecholamine levels during endotoxin-induces acute lung injury in sheep: searching for potential markers of the acute respiratory distress syndrome. J. Lab. Clin. Med. 1996;128:545-551[Medline]
25.
Hume R. Prediction of lean body mass from height and weight. J. Clin. Pathol. 1966;19:389-391
26.
Huxtable R. J. Physiological actions of taurine. Physiol. Rev. 1992;72:101-163
27. Huxtable R. Barbeau A. eds. Taurine 1976 Raven Press New York, NY.
28.
Jeevanandam M., Ali M. R., Holaday N. J., Petersen S. R. Adjuvant recombinant human growth hormone normalizes plasma amino acids in parenterally fed trauma patients. J. Parent. Enteral Nutr. 1995;19:137-144
29.
Jeevanandam M., Young D. H., Ramias L., Schiller W. R. Effect of major trauma on plasma free amino acid concentration in geriatric patients. Am. J. Clin. Nutr. 1990;51:1040-1045
30. Kendler B. S. Taurine: an overview of its role in preventive medicine. Prev. Med. 1989;18:79-100[Medline]
31.
Kopple J. D., Vinton N. E., Laidlaw S. A., Ament M. E. Effect of intravenous taurine supplementation on plasma, blood cell, and urine taurine concentrations in adults undergoing long-term parenteral nutrition. Am. J. Clin. Nutr. 1990;52:846-853
32. Lehmann A. Effects of microdialysis-perfusion with anisoosmotic media on extracellular amino acids in the rat hippocampus and skeletal muscle. J. Neurochem. 1989;53:525-535[Medline]
33. Lehmann A., Lazarewicz J. W., Zeise M. N-Methylaspartate-evoked liberation of taurine and phosphoethanolamine in vivo: site of release. J. Neurochem. 1985;45:1172-1177[Medline]
34.
Malmezat T., Breuillé D., Pouyet C., Patureau Mirand P., Obled C. Metabolism of cysteine is modified during the acute phase of sepsis in rats. J. Nutr. 1998;128:97-105
35. Metropolitan Life Insurance Company 1983 Metropolitan height and weight tables. Stat. Bull. 1984;64:2-9
36. Milakofsky L., Hare T. A., Miller J. M., Vogel W. H. Rat plasma levels of amino acids and related compounds during stress. Life Sci 1985;36:753-761[Medline]
37. Neary P., Stapleton P. P., Condron C., Redmond H. P., Bouchier-Hayes D. J. Surgical stress induces neutrophil plasma taurine sequestration indicating its essential role in the maintenance of proinflammatory cell homeostasis. Faist E. eds. The Immune Consequences of Trauma, Sepsis and Shock. Mechanisms and Therapeutic Approaches 1997:407-411 Monduzzi Bologna, Italy.
38.
Paauw J. D., Davis A. T. Taurine concentrations in serum of critically injured patients and age- and sex-matched healthy control subjects. Am. J. Clin. Nutr. 1990;52:657-660
39.
Pathirana C., Grimble R. F. Taurine and serine supplementation modulates the metabolic response to tumor necrosis factor in rat feds a low protein diet. J. Nutr. 1992;122:1369-1375
40. Redmond H. P., Stapleton P. P., Neary P., Bouchier-Hayes D. Immunonutrition: the role of taurine. Nutrition 1998;14:599-604[Medline]
41.
Redmond H. P., Wang J. H., Bouchier-Hayes D. Taurine attenuates nitric oxide- and reactive oxygen intermediate-dependent hepatocyte injury. Arch. Surg. 1996;131:1280-1288
42. Schaffer S. W., Azuma J., Madura J. D. Mechanisms underlying taurine-mediated alterations in membrane function. Amino Acids 1995;8:231-246
43. Schuller-Levis G., Quinn M. R., Wright C., Park E. Taurine protects against oxidant-induced lung injury: possible mechanism(s) of action. Huxtable R. eds. Taurine in Health and Disease 1994:31-39 Plenum Press New York, NY.
44. Seber G.A.F. Linear Regressions Analysis 1977 Wiley New York, NY.
45. Sherwin R. S. Effect of starvation on the turnover and metabolic response to leucine. J. Clin. Investig. 1978;61:1471-1481
46. Shotwell M. A., Kilberg M. S., Oxender D. L. The regulation of neutral amino acid transport in mammalian cells. Biochim. Biophys. Acta 1983;737:267-284[Medline]
47. Siegel J. H., Cerra F. B., Coleman B., Giovannini I., Shetye M., Border J. R., McMenamy R. R. Physiological and metabolic correlations in human sepsis. Surgery 1979;86:163-193[Medline]
48.
Skau T., Nyström P. O., Carlsson C. Severity of illness in intraabdominal infection. A comparison of two indexes. Arch. Surg. 1985;120:152-158
49. Skeie B., Kvetan V., Gil K. M., Rothkopf M. M., Newsholme E. A., Askanazi J. Branch-chain amino acids: their metabolism and clinical utility. Crit. Care Med. 1990;18:549-571[Medline]
50. Soupart P. Free amino acids of blood and urine in the human. Holden J. T. eds. Amino Acid Pools: Distribution, Formation and Function of Free Amino Acids 1962:220-262 Elsevier Amsterdam, The Netherlands.
51.
Stapleton P. P., O’Flaherty L., Redmond P., Bouchier-Hayes D. J. Host defense—a role for the amino acid taurine?. J. Parent. Enteral Nutr. 1998;22:42-48
52.
Stevens L. E. Gauging the severity of surgical sepsis. Arch. Surg. 1983;118:1190-1192
53. Stipanuk M. H. Metabolism of sulfur-containing amino acids. Annu. Rev. Nutr. 1986;6:179-209[Medline]
54. Vente J. P., Von Meyenfeldt M. F., Eijk H. M. Plasma amino acid profiles in sepsis and stress. Ann. Surg. 1989;209:57-62[Medline]
55.
Vinton N. E., Laidlaw S. A., Ament M. E., Kopple J. D. Taurine concentrations in plasma and blood cells of patients undergoing long-term parenteral nutrition. Am. J. Clin. Nutr. 1986;44:398-404
56. Vinton N. E., Laidlaw S. A., Ament M. E., Kopple J. D. Taurine concentrations in plasma, blood cells, and urine of children undergoing long-term total parenteral nutrition. Pediatr. Res. 1987;21:399-403[Medline]
57. Watson R.W.G., Redmond H. P., McCarthy J., Bouchier-Hayes D. Taurolidine, an antilipopolysaccharide agent, has immunoregulatory properties that are mediated by the amino acid taurine. J. Leukoc. Biol. 1995;58:299-306[Abstract]
58. Wright C. E., Tallan H. H., Lin Y. Y. Taurine: biological update. Annu. Rev. Biochem. 1986;55:427-453[Medline]
59. Wu J. Y. Purification, characterization, and kinetic studies of GAD and GABA-T from mouse brain. Roberts E. Chase T. N. Tower D.B. eds. GABA in Nervous System Function 1976:7-55 Raven Press New York, NY.
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