Rivista Italiana di Nutrizione Parenterale ed Enterale / Anno 22 n. 4, pp.

193-200 Wichtig Editore, 2004

Rassegna - Review

The role of whey protein in antioxidant defense

S.G. SUKKAR1, G. BOUNOUS2

1
Clinical Nutrition Unit, Azienda San Martino University Hospital Genova - Italy
2
Research and Development Department, Immunotec Research Ltd, Vaudreuil-Dorion, Quebec - Canada

ABSTRACT: Whey protein concentrates (WPC) are a heterogeneous group of proteins (β-lac-
toglobulin, α-lactalbumin, serum albumin and immunoglobulins) obtained in milk after casein
(CAS) precipitation. WPC also contains bioactive substances, such as hormones, growth fac-
tors (insulin-like growth factors (IGFs), transforming growth factor-β (TGF-β) platelet derived
growth factor) and cytokines, which can have an important physiological role. In in vitro stud-
ies, WPC demonstrate anticancer actions such as the inhibition of cancer cell growth and anti-
mutagenic effects while, in experimental tumor animal models, tumor burden reduction. Fur-
thermore, WPC present immuno-enhancing properties due to glutathione (GSH) synthesis of
lymphocytes, which can represent a possible tool in oxidative stress related diseases. Finally,
WPC consumption in adults is associated with a significant increase in protein synthesis, with
no change in protein catabolism when compared with CAS, according to their different enteric
absorption. The physiological mechanisms by which WPC interact with the antioxidant system,
cancer prevention and metabolism, as well as the possible role of WPC in immunonutrition are
discussed. In conclusion, WPC could be an interesting integrative protein source in clinical nu-
trition. Human clinical trials are required to verify the efficacy of WPC in counteracting oxida-
tive stress and in favoring protein anabolism in protein-energy malnutrition syndromes. (RINPE
2004; 22: 193-200)
KEY WORDS: Antioxidants, Whey protein, Cancer, Immune system, Immunonutrition, Oxida-
tive stress, ROS

PAROLE CHIAVE: Antiossidanti, Proteine del siero di latte, Cancro, Sistema immunitario, Immu-
nonutrizione, Stress ossidativo, Radicali liberi

INTRODUCTION flammatory cascade (Fig. 1). The majority of free radicals

The current interest in complementary medicine has
led to the increasing use and misuse of terms such as
“free radicals” and “antioxidants”. A free radical can be
defined as any species that contains one or more unpaired
electrons, an unpaired electron being one that is alone in
originate in the final stage of cell respiration, in which
electrons flow from organic substrates to oxygen, yield-
ing energy. When mitochondria are functioning, an elec-
tron passing through the respiratory chain can leak direct-
ly onto the oxygen molecule resulting in superoxide radi-
cal formation: O2 + e- O.-2.
▼

an orbital. Most biological molecules contain only paired
electrons. A radical either can donate its unpaired electron
to another molecule or can acquire an electron from an-
other molecule in order to pair. The characteristic of
events involving free radicals is the development of a
chain reaction with subsequent damage to adjacent bio-
logical structures, which could be involved in the pro-in-
Figure 2 demonstrates the sequence of biochemical
events following the appearance of O.-2.
Overall, antioxidants include endogenous and ex-
ogenous elements such as antioxidant enzymes (super-
oxide dismutase catalase), vitamins (vitamin C and vita-
min E), the glutathione (GSH) system and non-vitamin
substances such as catechins and β-carotene (1). More-

© SINPE-GASAPE 193
Oxidative stress and whey protein

Fig. 1 - Possible role of nutri-

tional intervention as comple-
mentary therapy in chronic oxi-
dative stress and chronic in-
flammation: signal transduction
and gene expression can be
down-regulated by antioxidant
natural systems and their pre-
cursor (cysteine, glutamate,
whey protein concentrates and
antioxidant vitamins), by diet
derived antioxidants substan-
ces, by diet derived inhibitors of
NF-kB or by n-3 fatty acids
(from: Sukkar & Rossi Autoim-
munity Rev 2004; 3: 199-206)
(35).

ROS: reactive oxygen species;

EGCG: epigallocatechin 3-gal-
late; SL: sesquiterpene lacto-
nes; AP-1: activator protein-1;
NF-kB: nuclear factor-kB; AA:
arachidonic acid; ECA: eicosa-
pentaenoic acid; COX: cycloxy-
genase; LOX: lipoxygenase;
PG: prostaglandines; TX: trom-
boxans; LT: leucotriens.

over, the term “antioxidant” was used initially to define
the cell’s own protective mechanisms. It is noteworthy
that the two major barriers against released free radicals
are located close to the mitochondria, in proximity to
the oxidant formation source. GSH (L-gamma-glu-
tamyl-L-cysteinylglycine) can spontaneously, or with
the help of peroxidase, easily deliver the H necessary for
the reduction in the radicals (Fig. 2). The redox system
is represented by GSH in the cells and by albumin and
cysteine in plasma. In both cases, the active element is
the SH (thiol) cysteine group which, when performing
its antioxidant activity, is oxidized to cystine or cysteine
disulfide (Fig. 3). Therefore, the cysteine/cystine ratio
defines the redox state that represents the major deter-
minant of optimal cell function.
The tripeptide GSH is largely distributed inside the
cells where it is a substrate for two classes of enzymes,
the selenium-dependent GSH peroxidase and a family of
GSH transferases, which are considered to catalyze
detoxification by two different reactions: spontaneous or
enzyme-associated. The involvement of GSH in cancer
protection (in particular of cancer-induced DNA dam-
age) includes a reduction in 9Y GSH peroxidase of hy-
drogen peroxide, free radicals and reactive oxygen

194
Sukkar and Bounous
Fig. 2 - Interactions between ROS and GSH.
species (ROS). GSH transferases catalyze the GSH con-
jugation of electrophilic compounds biotransformed
from xenobiotics (mutagens and carcinogens), which are
eliminated easily from the body (2-4).
Dietary GSH sources are few (1, 5, 6) and excess di-
etary protein or sulphur amino acids do not enhance the
maximum hepatic GSH amount beyond the normal
physiological maximum level obtained with adequate
dietary components.
The liver, the key organ for xenobiotic detoxification
and elimination, is the major site of GSH synthesis. This
organ has the unique and particular ability to convert the
sulphur amino acid methionine to cysteine required for
GSH synthesis (2, 7).
Almost 95% of GSH synthesized in the liver is re-
leased in the blood stream, which supplies the extra-he-
patic tissues (2), and bile. The latter is the main GSH
source for the intestinal mucosa, where its concentration
is relatively high (50-60% of liver content), but its distri-
bution is not uniform.
The colorectal mucosa seems to have lower GSH
transferase activity in comparison to other parts of the in-
testinal mucosa, and this could partially explain the sus-
ceptibility to cancerogenesis of this anatomic district (8).
GSH biosynthesis is strictly dependent on precursor
Fig. 3 - Cellular and plasma redox system.
amino acid concentrations (glutamate, glycine and cys-
teine) and competes with albumin synthesis for the
available cysteine (1, 9). The kinetic characteristics ex-
pressed by the km rate for amino acid activating en-
zymes (the rate limiting enzymes for protein synthesis)
is 0.003 mmol/L, whereas that for gamma glutamyl cys-
teine synthetase (the rate limiting enzymes for GSH
synthesis) is 0.35 mmol/L. This means that the biosyn-
thetic pathway for proteins works maximally at a con-
centration approximately 166-fold lower than for GSH
synthesis, whose production is subsequently impaired in
greater amounts than that of proteins at low cysteine
availability (1).
Grimble and Grimble demonstrated that rats nour-
ished with different amounts of sulphur amino acids, un-
dergoing inflammatory stimuli, show differences in net
responses to protein and GSH synthesis by the liver (10).
Therefore, a redox mechanism that links receptor-
mediated signals to low intracellular GSH levels favors
those cells that are engaged in high protein synthesis
(11). The albumin concentration reflects a measure of
the degree of stress rather than the nutritional status.
Several studies have demonstrated that the fractional
synthesis rate is increased rather than decreased in both
traumatized patients and in cachectic stressed patients
195
Oxidative stress and whey protein
(12). This effect can be due to the presence of the cys-
teinil radical in albumin. A possible suggestion claims
that albumin enters tissues to repair damage inflicted by
the stress conditions, and here it is oxidized.
Therefore, in many catabolic clinical conditions the
increased turnover and breakdown of albumin could be
associated with cysteine consumption. It is noteworthy
that nutritional intervention is often ineffective in raising
the albumin content of plasma, whereas N-acetylcysteine
(NAC), a cysteine analog, can raise plasmatic albumin
levels (9). Another possible cysteine source is whey pro-
tein, which has been proved to increase the lymphocyte
concentration of GSH in animal fed models (13).
Immune system and antioxidant systems
If Figure 3 represents part of the lymphocyte ma-
chinery, we can understand why in vitro studies have
demonstrated that the oxygen-requiring antigen driven
clonal expansion and antibody synthesis in immune
cells depends on their capacity to reconstitute GSH to
neutralize the increased production of oxygen-derived
radicals; therefore, facilitating a sustained immune re-
sponse (14, 15). This principle was verified by in vivo
experiments where animals fed cysteine rich whey pro-
tein concentrate (WPC) showed enhanced immune re-
sponses to a T-dependent antigen (13, 17) (Fig. 4). This
effect was abolished by the administration of buthionine
sulfoximine, which inhibited the GSH synthesis; there-
fore, demonstrating that the role of these proteins on the
immune system depends on the GSH system (18).
Dietary whey protein concentrates
Biological characteristics
WPC are a heterogeneous group obtained in milk af-
ter casein (CAS) precipitation at pH 4.6 (19). The con-
centrations in milk vary from approximately 5-7 g/L.
The major components in decreasing amounts are β-lac-
toglobulin (2-4 g/L), α-lactalbumin (0.6-1.7 g/L),
bovine serum albumin (0.2-0.4 g/L) and immunoglobu-
lins (0.5-1.8 g/L). Commercial WPC (approximately
75% protein) is prepared in the diary industry as a by-
product of cheese and CAS manufacture. WPC contains
carbohydrate (4% lactose) and 5% lipids (approximately
25% fatty acids and 25% phospholipids) (19), it also
contains bioactive substances such as hormones, growth
factors (insulin-like growth factors, transforming growth
factor-β (TGF-β) and platelet growth factor) and cy-
tokines, which can have an important physiological role.
For example, TGF-β is able to regulate cell growth in
both normal cells and tumor cells by suppressing prolif-
196
Fig. 4 - Reports of studies showing the immunoenhancing role of
specially prepared dietary WPCs.
eration or enhancing apoptosis (19). Given that TGF-β is
unaffected by acidic stomach pH, it can reach intestinal
cells where, after receptor binding, it can act through an
antiproliferative fashion, and subsequently be absorbed
and exert its action on other cellular compartments.
Anticancer actions of WPC
A preliminary study (20) and a more detailed ver-
sion (21) reported the effects of formula diets containing
20 g/100 g diet of WPC, CAS or Purina mouse chow on
dimethylhydrazine-dihydrochloride (DMH)-induced
colon tumors in A/J mice. At 28 weeks, tumor incidence
and tumor area were substantially reduced in WPC-fed
mice, and in lower amounts, but always significant in
CAS-fed mice. At the end of the experiment, the mice
continuously fed WPC were alive, whereas 33% of the
CAS- or Purina-fed mice had died. The Purina/WPC-fed
mice were afforded greater protection from colon tu-
mors than the Purina/CAS-fed mice.
McIntosh et al (22) also demonstrated that dairy
protein-based diets restricted DMH-induced tumor gen-
esis, and soybean protein-fed at 20 g/100 g in AIN-76A
diets resulted in a tumor incidence rate of 30, 45, 55 and
60% respectively, although the results did not reach sta-
tistical significance. Moreover, tumor burdens (i.e. the
total number of tumors within each group) in WPC and
CAS-fed groups were significantly (p<0.02) lower than
for red meat or soybean protein-fed groups (Tab. I).
The discovered immunoenhancing WPC activity
inspired the first study of WPC feeding on the devel-
opment of experimental colon carcinoma in mice (20).
The positive results of this study (i.e. a reduction in
tumor burden with WPC administration) were con-
firmed in rats (22) (Fig. 5, Tab. I) and extended to oth-
er types of malignancies such as mammary tumors in
female rats (23).
Sukkar and Bounous
TABLE I - AMOUNTS OF SULPHUR AMINO ACIDS, LIVER GLUTATHIONE AND TUMOUR DATA FOR RATS FED VARIOUS DIETS1
Source of Cysteine Methionine
protein
Soybean 0.70 1.30
Meat 0.50 2.20
Whey 2.30 2.10
1
Adapted from McIntosh (1995).*p<0.02 vs. a, b
WPC effects on cell cultures
Cell culture studies showed that whey protein or
whey protein components were able selectively to inhib-
it cancer cell growth. The addition of whey protein to
the medium of estrogen-responsive human breast cancer
cell line MCF-7 and of a prostate cancer cell line signif-
icantly reduced cell growth (24). The growth in the
breast cancer line MCF-7 was also demonstrated to be
inhibited by bovine serum (25). Bovine serum albumin,
but not total whey protein, β-lactoglobulin or soybean
protein exhibited a strong anti-mutagenic effect against
the mutagen 4-nitroquinoline-L-oxide in a Chinese ham-
ster epithelial cell line (26). Finally, WPC stimulated the
proliferation and GSH synthesis of normal lymphocytes
whereas it inhibited the proliferation of rat mammary tu-
mor or Jurkat T tumor cells (27).
Anabolic effects
Boirie et al (28) claimed recently, by analogy with
carbohydrates, that slow and fast proteins exist, accord-
ing to the speed at which they are digested and absorbed
Fig. 5 - Results of Studies Demonstra-
ting the Role of Specially Prepared
Dietary wpc s in Cancer Prevention.
Carcinogen was dimethylhydrazine-
dihydrochloride (DMH), which indu-
ces colon tumors similar to those
found in humans (with regard to type
of lesions1 and response to chemothe-
rapy2). The diets were fed before and
throughout the 24 weeks DMH-treat-
ment period. No differential effect of
diet on body weight was seen.
Total cysteine Liver glutathione Tumor Tumor
+ methionine mmol/g incidence burden
(wet tissue) (%) (tumors/group)
2.00 2.45 60 26a
2.70 4.16 55 21b
4.40 5.21 30 7*
as amino acids from the gut. In this report, the authors
studied the effect of two milk proteins, CAS and WPC,
on postprandial whole-body protein metabolism in hu-
mans. In order to achieve this, they combined oral and
intravenous administration of 13C-leucine labeled and
unlabeled specific proteins using a dual tracer methodol-
ogy. The most exciting result of this study was that
when they administered WPC to adult patients, a high,
rapid and transient peak in plasmatic amino acids was
observed. This event was associated with a significant
increase (>68%) in protein synthesis, with no change in
protein catabolism. On the contrary, after CAS adminis-
tration, the plasma amino acid surge proved lower, slow-
er but more prolonged. Therefore, protein synthesis was
only moderately increased (>31%), whereas a marked
inhibition in protein break down (i.e. leucine oxidation)
was evidenced; notably, leucine intake was identical in
both meals. Overall, the different behavior of these two
proteins possibly reflects the different exit rate from the
stomach into the duodenum, which is much faster for
WPC, causing a rapid influx of amino acids analogous
to the stimulation of protein synthesis observed after in-
travenous amino acid infusion. In addition, it must be
197
Oxidative stress and whey protein
NATURAL
WHEY PROTEIN CONCENTRATE
1. Bounous G et al. Clin Invest Med 1988; 11: 213-7 – The incidence
and size of DMH induced colon tumors was lower in dietary-trea-
ted mice.
2. Papenburg R et al. Tumour Biol 1990; 11: 129-36 – Similar re-
sults as in 1, in addition, dietary treatment was effective also on
established malignancy. Improved survival.
3. McIntosh G et al. J Nutr 1995; 125: 809-16 – Almost identical re-
sults as in 1 were obtained in rats.
4. Hakkar R et al. Cancer Epidemiol Biomarkers Prev 2000; 9: 113-
7 - In rats, the incidence of chemically induced mammary tumors
was lower.
5. Bounous G et al. Anticancer Res 2000; 20: 4785-92 [1]
- Cancer of the prostate. All patients had elevated PSA levels with
biopsy confirmed cancer of the prostate. 13 out of 15 patients
showed a progressive decline of PSA values during 3-12 months
observation period.
- Metastasis of renal carcinoma. In a 50-year-old woman: following
3 yrs, a significant decrease of metastatic disease in liver, resolu-
tion in lung and bone was seen.
- Bladder cancer. During 1 yr observation, no recurrence of papil-
lary transitional cell carcinoma.
[1] The whey protein concentrate, specifically an isolate defined by protein gra-
de, in non-instantized native form, marketed as Immunocal/HMS90, was obtai-
ned from Immunotec Research Ltd.
Fig. 6 - Anticancer effect of cyst(e)ine in natural and pharmaceutical compositions, cysteine delivery systems.
borne in mind that albeit the percentage of amino acids
able to stimulate insulin secretion is similar in both pro-
teins, WPC possess a higher proportion of branched-
chain amino acids, which permits a synergistic effect
with insulin on protein metabolism (i.e. anabolism). On
the contrary, the percentage of amino acids that stimu-
late glucagone secretion is lower in WPC and, subse-
quently, the catabolic effect of this hormone is reduced
after the ingestion of this protein (29).
The same group (30) has recently extended previous
data by analyzing the effects of dietary carbohydrates
and lipids added to WPC and CAS. To verify this two
test meals, which differed only in their protein composi-
tion (CAS vs. WPC) but not in leucine amount, were ad-
ministered to healthy adult males. Each test meal was
otherwise composed of identical amounts of carbohy-
drates and fat. Although preliminary, the results of the
study suggested that (1) WPC was still more rapidly ab-
sorbed than CAS, as previously shown (28); (2) post-
prandial leucine balance was still lower with WPC-con-
taining meals than with those containing CAS, i.e. pro-
teolysis was more markedly inhibited by the latter
“slow” protein, although the differences in digestion rate
and leucine balance were less marked than when the pro-
198
PHARMACEUTICAL
NAC (N-ACETYLCYSTEINE)
1. De Flora S et al. Cancer Lett 1986; 32: 235-41 – Inhibition of
urethan induced lung tumors in mice.
2. De Flora S et al. Am J Med 1991; 91: 1225-305 – Prevention of
mutation and cancer by thiols is particularly useful in condition of
GSH depletion.
3. De Flora S et al. J Cell Biochem 1995; (suppl 22): S33-41 – A
study of the mechanisms contributing to NAC anticarcinogenesis.
4. De Flora S et al. Int J Cancer 1996; 67: 842-8 – Synergism
between NAC and doxorubicin in the prevention of tumors and
metastases in mice.
5. Delneste Y et al. Blood 1997; 90: 1124-32 – NAC exhibited potent
anti lymphoma activity in mice.
6. D’Agostini F et al. Int J Oncol 1998; 13: 217-24 – In mice, NAC
interact with a cytotoxic agent in inhibiting melanoma cell inva-
sion and metastases.
7. Dröge W. Current Opin Clin Nutr Metab Care 1999; 2: 227-33 –
Plasma albumin level and body cell mass in cancer patients are
increased by NAC.
8. Estensen RD et al. Cancer Lett 1999; 147: 109-14 – In patients at
risk of colon cancer, NAC produces a decrease of proliferation in-
dex in the crysts.
9. Morini M et al. Int J Biol Markers 1999; 14: 268-71 - Inhibition
of neo angiogenesis and tumor progression in murine melanomas.
teins were administered alone. These results demonstrat-
ed that added non-protein energy sources to CAS and
WPC reduced the differences in both the protein diges-
tion rate and protein gain. Finally, this preliminary study
showed that in contrast to the young, in elderly people a
fast protein (i.e. WPC) induces a better postprandial
leucine balance than that obtained with a slow protein
(i.e. CAS). This latter finding suggests that in healthy el-
derly people, the optimization of protein retention could
be achieved by changing the pattern of protein feeding
and/or the rate of protein absorption (28-30).
The potential to enhance protein synthesis and to re-
duce/inhibit protein breakdown improves the therapeutic
possibilities for patients with wasting syndromes such as
those with sepsis, burns, acquired immunodeficiency syn-
drome, skeletal trauma and multiple organ failure (29, 30).
Mechanisms of cysteine delivering drugs/systems
The effect of a cysteine pro-drug such as NAC on
tumor development and carcinogenesis (Fig. 6) strongly
suggests that WPC can act as a cysteine delivery system
in inhibiting tumor growth. In discussing the effects of
WPC on tumors, it is important to distinguish between
Sukkar and Bounous
the anti-carcinogenesis effect and the anti-tumoral ef-
fect. Our suggestion is that WPC can possess both; in
particular the former effect could be obtained by the
ability of WPC to provide high substrate levels for GSH
synthesis in relevant tissues; therefore, enhancing the
detoxification of potential carcinogens or free radicals in
spontaneous carcinogenesis. The second property (i.e
the anti-tumoral effect) could rely on the GSH-depen-
dent stimulation of the immune system by WPC. Table I
(22) illustrates the relationship between cysteine, GSH
and the development of experimental tumors (19). The
causative role of cysteine deficiency in immunological
dysfunction developments in oncological patients is sup-
ported by the observation that additional cysteine
sources can restore natural killer cell activity (31). It is
interesting to note that oncological patients show an ac-
celerated shift to more oxidized conditions, which could
contribute to the loss of body cell mass (32). These data
suggest that during cancer progression, the antioxidant
buffer activity could progressively decline due to the de-
pletion of the thiol (SH) group in the redox equation.
Therefore, a natural cysteine donor such as WPC could
inhibit/delay tumor growth by directly increasing intra-
cellular thiol levels (33).
Finally, cysteine itself could exert a direct anti-tu-
mor effect in two different ways unrelated to GSH syn-
thesis. Concerning the former, it was recently demon-
strated that several sulfur-containing antioxidants such
as NAC and dimercaptopropanol selectively induced a
5-10 fold increase in p53-dependent apoptosis in a
transformed cell line and primary cultures, but not in
normal cells. In particular, NAC elevated p53 expression
post-transcriptionally by increasing the p53 mRNA
translation rate rather than by altering protein stability.
In contrast, antioxidants whose action is limited to scav-
enging radicals do not seem to possess this important
property (33).
The second feature of a cysteine delivery system is
related to its inhibitory effect on neoangiogenesis and
tumor progression and recurrence both in vitro and in vi-
vo (rodents) (34).
The promising anticancer effect of NAC is, unfortu-
nately, hampered by its adverse effects at pharmacologi-
cal doses. Therefore, long-term use of a natural cysteine
donor such as WPC could be a promising option in the
long-term nutritional support of oncological patients.
In conclusion, WPC could be an interesting and al-
ternative protein source with immunomodulating prop-
erties in clinical nutrition. Clinical trials are mandatory
to verify the efficacy of whey protein to counteract the
oxidative stress by the increase in GSH synthesis, and to
verify the anabolic role as alternative protein substrates
in malnutrition-inflammation syndromes.
RIASSUNTO
Le proteine del siero del latte (WPC)rappresentano
un gruppo eterogeneo di proteine (β-lattoglobuline,
α-lattoalbumine, albumine seriche e immunoglobuline)
derivate dal latte previa precipitazione delle caseine. Le
WPC contengono anche sostanze bioattive quali ormoni,
fattori di crescita (insulin-like growth factors (IGFs),
transforming growth factor-β (TGF-β), platelet derived
growth factor) e citochine, che presentano importanti
ruoli fisiologici.
Studi in vitro hanno dimostrato che le WPC presen-
tano potere antimutageno e anticarcinogenetico mentre,
in modelli sperimentali animali, sono in grado di inibire
la crescita neoplastica.
Le WPC mostrano inoltre proprietà immunosti-
molanti, associate ad un incremento della sintesi di glu-
tatione linfocitario, potrebbe rappresentare un interes-
sante strumento terapeutico nelle patologie correlate con
lo stress ossidativo.
Infine il consumo di WPC nell’uomo si riflette in un
migliore effetto anabolico proteico rispetto al consumo
di caseina in relazione al differente meccanismo di as-
sorbimento enterico.
I meccanismi fisiologici attraverso i quali le WPC
interagiscono con il sistema antiossidante, con la car-
cinogenesi e con il metabolismo proteico, nonché il loro
possibile ruolo immunonutrizionale sono discussi in
questo articolo.
In conclusione le WPC possono rappresentare una in-
teressante fonte proteica integrativa in nutrizione clinica.
È auspicabile che studi clinici controllati vengano
condotti nell’uomo, al fine di definire l’efficacia clinica
delle WPC nel contrastare lo stress ossidativo e nel fa-
vorire l’anabolismo proteico in corso di malnutrizione
proteico-calorica.
Address for correspondence:
Dr. S.G. Sukkar
Clinical Nutrition Unit
S. Martino University Hospital
Largo R. Benzi, 10
16132 Genova, Italy
e-mail: samir.sukkar@hsanmartino.liguria.it
199
Oxidative stress and whey protein
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Ricevuto il 18/8/2004
Accettato dopo Revisione il 4/11/2004