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A possible association between cholesterol levels and inflammatory markers, such as oxidized low-density lipoprotein, highly sensitive C-reactive protein and oxidized low-density lipoprot

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with hypercholesterolemia and inflammatory processes Marta Medeiros Frescura Duarte1, Vaˆnia L Loro1, Joa˜o B T Rocha1, Daniela B R Leal2,

Andreza F de Bem1, Arace´li Dorneles1, Vera M Morsch1 and Maria R C Schetinger1

1 Departamento de Quı´mica, Centro de Cieˆncias Naturais e Exatas, Programa de Pos-Graduac¸a˜o em Bioquı´mica Toxicolo´gica, Universidade Federal de Santa Maria, Brazil

2 Hospital Universita´rio de Santa Maria, Santa Maria, RS, Brazil

Hypercholesterolemia is widely accepted as one of the

major risk factors for the development of ischemic heart

disease, angina, and myocardial infarction Although

the risks imposed by hypercholesterolemia seem to be

manifold, most attention has been devoted to its role in

atherosclerosis [1] Atherosclerosis is an inflammatory

disease that is associated with endothelial cell activation,

oxidative stress, and the accumulation of leukocytes in

the walls of arteries [2] The inflammatory process

induced by hypercholesterolemia is not limited to large arteries Endothelial cell adhesion molecule expression, enhanced oxidant production and leukocyte–endothelial cell adhesion have been demonstrated in postcapillary venules of different tissues of hypercholesterolemic animals [3–6]

Low-density lipoprotein is a major carrier of cholesterol in the circulation, and can play an impor-tant role in atherogenesis if it undergoes oxidative

Keywords

cholesterol; highly sensitive C-reactive

protein; NTPDase; oxidized low-density

lipoprotein; oxidized low-density lipoprotein

autoantibodies

Correspondence

M R C Schetinger, Departamento de

Quı´mica, Centro de Cieˆncias Naturais e

Exatas, Universidade Federal de Santa

Maria, Av Roraima 1000, 97105-900, Santa

Maria, RS, Brazil

Fax: +55 5532 208978

Tel: +55 5532 208665

E-mail: mariaschetinger@gmail.com

(Received 18 August 2006, revised 29

January 2007, accepted 19 March 2007)

doi:10.1111/j.1742-4658.2007.05805.x

The activity of NTPDase (EC 3.6.1.5, apyrase, CD39) was verified in plate-lets from patients with increasing cholesterol levels A possible association between cholesterol levels and inflammatory markers, such as oxidized low-density lipoprotein, highly sensitive C-reactive protein and oxidized low-density lipoprotein autoantibodies, was also investigated Lipid per-oxidation was estimated by measurement of thiobarbituric acid reactive substances in serum The following groups were studied: group I,

< 150 mgÆdL)1cholesterol; group II, 151–200 mgÆdL)1 cholesterol; group -III, 201–250 mgÆdL)1 cholesterol; and group IV, > 251 mgÆdL)1 choles-terol The results demonstrated that both ATP hydrolysis and ADP hydrolysis were enhanced as a function of cholesterol level Low-density lipoprotein levels increased concomitantly with total cholesterol levels Tri-glyceride levels were increased in the groups with total cholesterol above

251 mgÆdL)1 Oxidized low-density lipoprotein levels were elevated in groups II, III, and IV Highly sensitive C-reactive protein was elevated in the group with cholesterol levels higher than 251 mgÆdL)1 Oxidized low-density lipoprotein autoantibodies were elevated in groups III and IV Thiobarbituric acid reactive substance content was enhanced as a function

of cholesterol level In summary, hypercholesterolemia is associated with enhancement of inflammatory response, oxidative stress, and ATP and ADP hydrolysis The increased ATP and ADP hydrolysis in group IV was confirmed by an increase in CD39 expression on its surface The increase

in CD39 activity is possibly related to a compensatory response to the inflammatory and pro-oxidative state associated with hypercholesterolemia

Abbreviations

hsCRP, highly sensitive C-reactive protein; OxLDL, oxidized low-density lipoprotein; PRP, platelet-rich plasma.

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modification by endothelial cells, vascular smooth

muscle, or macrophages within the arterial wall [7]

Oxidized low-density lipoprotein (OxLDL) as well as

OxLDL autoantibodies have been found in several

studies in atherosclerotic lesions [8] The highly

sensitive C-reactive protein (hsCRP) enhances the

binding of OxLDL to monocytic⁄ macrophage-like

cells through Fcc receptors [9]

Platelets also accumulate within atherosclerotic

lesions, and can recruit additional platelets to form a

thrombus, indicating that the arterial wall can assume

both an inflammatory and prothrombogenic phenotype

when blood cholesterol levels are elevated [10,11]

Platelets are one of the most important blood

compo-nents that participate in and regulate thrombus

forma-tion by releasing active substances, such as ADP [12]

Micromolar concentrations of ADP are sufficient to

induce human platelet aggregation, and in the

coagula-tion cascade, AMP is hydrolyzed to adenosine, which

has an important function in the regulation of platelet

aggregation [13–15] Furthermore, the roles of

nuc-leotides and nucleosides as extracellular signaling

molecules have been well established Extracellular

nu-cleotides have become recognized for the significant

role that they play in modulating a variety of processes

related to vascular inflammation and thrombosis

[16–19] In this vein, recent data from our laboratory

have indicated changes in nucleotide hydrolysis by

platelets from patients carrying diseases generally

asso-ciated with changes in coagulation⁄ homeostasis

[13–15] More recently, there has been growing interest

in the long-term effects of extracellular nucleotides and

nucleosides on cell growth, proliferation, and death

[16–19]

NTPDase (CD39, ecto-apyrase, ATP

diphospho-hydrolase) is a glycosylated, membrane-bound enzyme

that hydrolyzes ATP and ADP to AMP, which is

sub-sequently converted to adenosine by 5¢-nucleotidase

(EC 3.1.3.5, CD73) NTPDases are located in various tissues, including the platelet membrane [20,21] NTP-Dase and CD73 play an important role in the regula-tion of blood flow and thrombogenesis by regulating ADP catabolism [22] Another aspect that must be emphasized here is the fact that NTPDase1 rapidly metabolizes ADP released during platelet activation This event is very important, because ADP is the final mediator of platelet recruitment and thrombus forma-tion [23] In fact, NTPDase1 has been recognized to play an important role in thromboregulation by hydro-lyzing and lowering extracellular ADP, which inhibits platelet aggregation In a recent study, Papanikolaou

et al [24] have shown that depletion of membrane cho-lesterol results in strong inhibition of NTPDase, and that this is reversed by purified cholesterol

Thus, one question that could be asked is whether the different cholesterol levels observed in human blood could affect NTPDase1 activity This study was performed in an attempt to answer this question The activity of NTPDase1 was measured on platelets of human donors with cholesterol levels ranging from less than 150 to more than 251 mgÆdL)1 Furthermore,

we studied whether cholesterol levels were associated with inflammatory markers, e.g hsCRP, and with lipid peroxidation

Results Patient characteristics are shown in Table 1 Glucose levels were in the normal range in all the groups studied, and ranged from 88 to 99 mgÆdL)1 No signi-ficant differences were observed in the high-density lipoprotein cholesterol levels among the groups Conversely, low-density lipoprotein levels increased concomitantly with the increase in total cholesterol levels, and were significantly higher in groups III and

IV Triglyceride levels were increased in group IV (the

Table 1 Characteristics of the four groups: age (years), sex (male ⁄ female), smoking, hypolipemic medication, and anti-inflammatory treat-ment Age is represented by mean ± SE.

Patients

Cholesterol groups

I (< 150 mgÆdL)1) II (151–200 mgÆdL)1) III (201–250 mgÆdL)1) IV (> 251 mgÆdL)1)

Sex

Hypolipemic

medication

Anti-inflammatory

treatment

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group with total cholesterol above 251 mgÆdL)1;

Table 2)

OxLDL was elevated in groups II, III, and IV

(Table 3), whereas hsCRP was elevated only in

group IV (cholesterol higher than 251 mgÆdL)1)

Ox-LDL autoantibodies were elevated in groups III and

IV (Table 3)

A statistically significant positive correlation was

found between the cholesterol levels and thiobarbituric

acid reactive substance production (r¼ 0.7438,

P< 0.01), which indicates an association between

plasma⁄ serum ⁄ blood and oxidative stress (Fig 1)

ATP hydrolysis was modified by cholesterol levels

above 151 mgÆL)1, and post hoc comparisons by

Duncan’s test revealed that it was significantly higher

in patients from groups II, III, and IV Furthermore,

these groups were significantly different from each

other (Fig 2A) Similar results were observed for

ADP hydrolysis Post hoc comparisons by Duncan’s

multiple range test revealed that patients from

groups II, III and IV presented higher levels of ADP

hydrolysis and that these groups were significantly

different from each other (Fig 2B) Correlation

ana-lysis indicated a positive correlation between

increased cholesterol levels and platelet ATP and

ADP hydrolysis (Fig 3A,3B)

Statistical analysis of the content of CD39-positive

cells by flow cytometry using labeled antibody against

NTPDase1 revealed that group IV (cholesterol higher

than 251 mgÆdL)1) had a significant increase in the

expression of NTPDase1, when compared to the other groups (P < 0.05, post hoc comparisons by Duncan multiple test; Fig 4)

There was a statistically significant correlation between ATP and ADP hydrolysis with OxLDL (r¼ 0.82, P < 0.01; r ¼ 0.91, P < 0.001), hsCRP (r¼ 0.82, P< 0.01; r¼ 0.91, P < 0.001), and OxLDL autoantibodies (r¼ 0.85, P < 0.01; r ¼ 0.96,

P < 0.001) ATP and ADP hydrolysis were also corre-lated with tryglyceride levels (r¼ 0.819, P < 0.001;

r ¼ 0.92, P < 0.001; Table 4)

Table 2 High-density lipoprotein (HDL), low-density lipoprotein (LDL), triglyceride and glucose (mg⁄ dL) levels of patients with different cho-lesterol levels Results are expressed as the mean ± SE (n ¼ 40 for each group).

Blood parameters

Cholesterol groups

I (< 150 mgÆdL)1) II (151–200 mgÆdL)1) III (201–250 mgÆdL)1) IV (> 251 mgÆdL)1)

* Indicates significant difference at P < 0.05 between groups.

Table 3 OxLDL (mg ⁄ dL), hsCRP (mg ⁄ L) and OxLDL autoantibodies (mg ⁄ L) in patients with different cholesterol levels Results are expressed as the mean ± SE (n ¼ 40 for each group).

Parameters

Cholesterol levels

I (< 150 mgÆdL)1) II (151–200 mgÆdL)1) III (201–250 mgÆdL)1) IV (> 251 mgÆdL)1)

* Indicates significant difference at P < 0.05 between groups.

35 30 25 20 15 10

Cholesterol (mg/dl)

5 0

0 50 100 150 200 250 300 350 400 450

Fig 1 Correlation between cholesterol levels and thiobarbituric acid reactive substances (n ¼ 40) (r ¼ 0.74, P < 0.01) y ¼ 4.37 + 0.077x, where y ¼ malondialdehyde production (nmolÆmL)1) and x ¼ cholesterol levels.

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The present study clearly indicated that cholesterol

lev-els are associated with increased OxLDL, OxLDL

autoantibody formation, and inflammatory markers

The results of this study reveal that patients with high

cholesterol may have a predisposition to atheroma

pla-que development The results of the present study also

show a positive correlation between cholesterol levels

and OxLDL and hsCRP production, which is in

accordance with the literature data [7] Our study

con-firmed the hypothesis that increased levels of

choles-terol may be associated with hsCRP and OxLDL

autoantibodies, which are good indicators of increased

risk for atherosclerosis development

The present results show for the first time that

nucleo-tide hydrolysis is enhanced in platelets of patients

with hypercholesterolemia Probably, high cholesterol

levels induce an increase in platelet ATP and ADP

hydrolysis as a compensatory mechanism to inhibit

platelet aggregation and limit thrombus formation in

patients with a predisposition to atheroma development

30

A

B

< 150

> 251

*

*

*

*

*

*

201-250 151-200

< 150

> 251 201-250 151-200

20

10

0

10.0

7.5

5.0

2.5

0.0

< 150

151-200 Cholesterol (mg/dl)

201-250 > 251

< 150 151-200

Cholesterol (mg/dl)

201-250 > 251

Fig 2 ATP (A) and ADP (B) hydrolysis in platelets from patients

with hypercholesterolemia (n ¼ 40) Results are expressed as

nmol P i Æmin)1Æmg)1of protein Different letters indicate a significant

difference at P < 0.05 between groups.

A 40

30

20

10

0

0 50 100 150 200

Cholesterol (mg/dl)

250 300 350 400

80

10

8

6

4

2

0

120 160 200 240 280 320 360 400

450

B

Fig 3 Correlation analysis between cholesterol levels and ATP (A) and ADP (B) hydrolysis (n ¼ 40) (r ¼ 0.75, P < 0.01) y ¼ 2.06 + 0.078x, where y ¼ ATP hydrolysis and x ¼ cholesterol levels.

< 150

> 251

*

201-250 151-200

0 5 10 15 20 25 30 35

< 150

151-200 Cholesterol (mg/dl)

201-250 > 251

Fig 4 CD39 expression on platelets The analysis was done by flow cytometry (see Experimental procedures) Data represent the mean ± SE of 10 individuals Data were analyzed statistically

by Duncan’s multiple range test *Significantly different from the others (P < 0.05).

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Data from nucleotide hydrolysis and NTPDase1

(CD39) expression in platelet membranes indicated that

the mechanisms involved in ATP and ADP hydrolysis

vary with the cholesterol level In fact, up to

250 mgÆdL)1, there was no increase in CD39 expression

in platelets, but patients with cholesterol higher than

251 mgÆdL)1 exhibited a significant increase in the

expression of this complement This may indicate that

cholesterol up to 250 mgÆdL)1 causes an increase in

ATP and ADP hydrolysis by changing the plasma

mem-brane properties of platelets

In a previous study, our laboratory demonstrated

that diabetic, hypertensive and diabetic⁄ hypertensive

patients presented elevated nucleotide hydrolysis by

platelets [13,15] Taken together, we can suppose that

these associated pathologic conditions may change

the rate of platelet nucleotide hydrolysis Platelets

comprise one of the components of the thrombus

microenvironment and of the process of

thrombo-regulation It is known that the rate of platelet

nuc-leotide hydrolysis is lower in platelets than in

endothelium However, considering the function and

the mobility of platelets, we can understand their

active role in this process and the importance of

such hydrolysis In line with this, literature data

indi-cate that adenine nucleotides and adenosine are

important modulators of atherosclerosis [18], and

that upregulation of CD39⁄ NTPDase1 on platelets

has beneficial effects on endothelial cell activation;

this may be observed in vascular inflammation [19]

It is of importance that Papanikolaou et al [24]

showed that the reduction of cholesterol levels by

drugs results in strong inhibition of the enzymatic

and antiplatelet activities of NTPDase The results

presented here are in agreement with this, and we

have shown that circulating cholesterol positively

modulates platelet NTPDase1 activity Papanikolaou

et al [24] suggested that cholesterol may affect the

ability of this enzyme to undergo conformational

changes required for nucleotide hydrolysis Probably,

it enhances the interaction between the enzyme and

its substrates

In the literature, there are some studies showing that the levels of cholesterol or its oxidation status can affect ATPase activities [25,26] However, a direct role

of plasma cholesterol levels on platelet ecto-CD39 has never been established Lijnen et al [27] suggested that cholesterol lowering in hypercholesterolemic patients may result in a significant decrease in erythrocyte and platelet membrane cholesterol content Perhaps this occurred in our study When the cholesterol level is increased, the platelet membrane cholesterol content is enhanced, increasing the conformational stability of the transmembrane NTPDase1 protein, promoting activation

Taking together the importance of the physiologic (lipid bilayer component) or pathologic (factor related

to atherogenesis) functions of cholesterol, as well as the importance of the platelets and NTPDase, we con-cluded that cholesterol levels can modulate platelet NTPDase activity in vivo

In conclusion, our study demonstrated that the hydrolysis of adenine nucleotides is modified in plate-lets from hypercholesterolemic patients, and we suggest that this may play a beneficial role by preventing thrombus formation However, the modulation of nuc-leotide hydrolysis is possibly not sufficient to inhibit thrombus formation Indeed, clinical evidence indicates with clarity that the hypercholesterolemia is a risk fac-tor for future fatal events (unstable angina and myo-cardial infarction)

Experimental procedures

Chemicals Nucleotides, sodium azide, Hepes and Trizma base were pur-chased from Sigma (St Louis, MO, USA) Antibodies for flow cytometry analysis [R-phycoerythrin-conjugated mouse monoclonal antibody against human CD39, and fluorescein isothiocyanate-conjugated mouse monoclonal antibody against human CD61] were purchased from Serotec Ltd (Kidlington, Oxford, UK) and BD PharMingen (San Jose,

CA, USA), respectively All other reagents used in the experi-ments were of analytical grade and of the highest purity

Patients The sample consisted of patients with different cholesterol levels and ages ranging from 40 to 70 years, from LABI-MED (Santa Maria, RS, Brazil) We chose nonsmoking patients not undergoing hypolipemic or anti-inflammatory treatment, with glucose levels ranging from 70 to

95 mgÆdL)1 The sample was divided into four groups cons-siting of 50% female and 50% male, as follows: group 1,

Table 4 Correlation between ATP and ADP hydrolysis and

inflam-matory markers (OxLDL, hsCRP and OxLDL autoantibodies, and

triglycerides.

OxLDL autoantibodies Triglycerides

P < 0.01 P < 0.01 P < 0.01 P < 0.001

P < 0.001 P < 0.001 P < 0.001 P < 0.001

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cholesterol levels < 150 mgÆdL)1(n¼ 40); group 2,

choles-terol levels ranging from 151 to 200 mgÆdL)1 (n¼ 40);

group 3, cholesterol levels ranging from 201 to 250 mgÆdL)1

(n¼ 40); and group 4, cholesterol levels > 251 mgÆdL)1

(n¼ 40) These variations in the cholesterol values (50–

50 mg) were selected to correspond approximately to the

actual clinical interval criterion used to evaluate risk

factors The separation of the subjects into the groups was

based on clinical considerations We consider that a

cholesterol level below 150 mgÆdL)1 is low, and a level

between 151 and 200 mgÆdL)1 is clinically acceptable, but

close to the limit of 200 mgÆdL)1 A level between 201 and

250 mgÆdL)1is just above the limit, and a level higher than

251 mgÆdL)1is well above the safe limit for risk of

cardio-vascular disease All subjects gave written informed consent

to participate in the study The protocol was approved by

the Human Ethics Committee of the Health Science Center,

Federal University of Santa Maria (Protocol number:

015⁄ 2004) Eight milliliters of blood was obtained from

each participant and used for biochemical and hematologic

determinations and platelet-rich plasma (PRP) preparation

Biochemical determinations

Serum total cholesterol and triglyceride concentrations were

measured using standard enzymatic methods with the use of

Ortho-Clinical Diagnostics reagents, and a fully automated

analyzer (Vitros 950, dry chemistry; Johnson & Johnson,

Rochester, NY, USA) High-density lipoprotein cholesterol

was measured in the supernatant plasma after precipitation

of apolipoprotein B-containing lipoproteins with dextran

sulfate and magnesium chloride according to Bachorik &

Albers [28] Low-density lipoprotein cholesterol was

estima-ted with the Friedewald equation [29] hsCRP was measured

by immunoluminometry (IMMULITE 2000; Diagnostic

Products Corporation, Los Angeles, CA, USA) OxLDL was

determined by a capture ELISA according to the

manufac-turer’s instructions (Mercodia AB, Uppsala, Sweden), as

described by Holvoet et al [30] OxLDL autoantibodies were

determined using ELISA as described by Wu & Lefvert [31]

PRP preparation

PRP was prepared from human donors by the methods of

Pilla et al [21] and Lunkes et al [13] Briefly, blood was

collected into 0.129 m citrate and centrifuged at 160 g for

10 min The PRP was centrifuged at 1400 g for 15 min

and washed twice with 3.5 mm Hepes isosmolar buffer

containing 142 mm NaCl, 2.5 mm KCl, and 5.5 mm

glu-cose The washed platelets were resuspended in Hepes

buf-fer, and protein was adjusted to 0.3–0.5 mgÆmL)1, where

6–10 lg of protein was used per tube to ensure linearity

in the enzyme assay NTPDase is an ectoenzyme, and

thus platelet viability and integrity were confirmed by the

measurement of lactate dehydrogenase activity using the

enzymatic Vitros 950 (Ortho-Clinical Diagnostics; Johnson

& Johnson)

NTPDase activity Twenty microliters of the PRP preparation (10–15 lg protein) was added to the reaction mixture of NTPDase and preincubated for 10 min at 37C in a final volume

of 200 lL NTPDase activity was determined by the method of Pilla et al [21], in a reaction medium contain-ing 5.0 mm CaCl2, 100 mm NaCl, 4.0 mm KCl, 6 mm glucose, and 50 mm Tris⁄ HCl buffer (pH 7.4) The reac-tion was started by the addireac-tion of ATP or ADP as sub-strate at a final concentration of 1.0 mm The reaction was stopped by the addition of 200 lL of 10% trichloro-acetic acid to provide a final concentration of 5% The inorganic phosphate (Pi) released by ATP and ADP hydrolysis was measured by the method of Chan et al [32], using KH2PO4 as a standard Controls were pre-pared to correct for nonenzymatic hydrolysis by adding PRP after trichloroacetic acid addition All samples were run in triplicate Enzyme activities are reported as nmol

Pi releasedÆmin)1Æmg)1 protein

Flow cytometry analysis Peripheral blood cells were incubated with anti-CD39 and anti-CD61 (20 lL per 106 cells) for 25 min, lysed with fluorescence activated cell sorter (FACS) reagent, and incu-bated again for 15 min in the dark Cells were washed twice

in NaCl⁄ Pibuffer (pH 7.4) containing 0.02% (w⁄ v) sodium azide and 0.2% (w⁄ v) BSA The cells were then

resuspend-ed in NaCl⁄ Pi buffer (pH 7.4) and immediately analyzed with a FACScalibur flow cytometer using cellquest software (Becton Dickinson, San Jose, CA, USA), without fixation

Hematologic determinations Quantitative determinations of platelets obtained by veni-puncture were performed using a Pentra 120 analyzer (ABX, Montpellier, France) Platelet aggregation was per-formed by the technique of Biggs [33], consisting of the

in vitro macroscopic visualization of aggregates at intervals

of 15–50 s by the addition of ADP to PRP

Determination of lipid peroxidation Lipid peroxidation was estimated by the measurement of thiobarbituric acid reactive substances in serum samples by modifications of the method of Jentzsch et al [34] Briefly, 0.2 mL of serum was added to the reaction mixture con-taining 1 mL of 1% orthophosphoric acid, and 0.25 mL of

an alkaline solution of thiobarbituric acid (final volume

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2.0 mL), and this was followed by 45 min of heating at

95C After cooling, samples and standards of

malondial-dehyde were read at 532 nm against the blank of the

stand-ard curve The results were expressed as nmol

malondialdehydeÆmL)1

Protein determination

Protein was determined by the Coomassie blue method

using BSA as standard [35]

Statistical analysis

Data were analyzed statistically by one-way anova

fol-lowed by the Duncan test Differences between groups were

considered to be significant when P < 0.05 Linear

correla-tion between variables was also carried out

References

1 Tailor A & Granger DN (2003) Hypercholesterolemia

promotes P-selectin-dependent platelet–endothelial cell

adhesion in postcapillary venules Arterioscler Thromb

Vasc Biol 23, 675–680

2 Libby P (2000) Changing concepts of atherogenesis

J Int Med 247, 349–358

3 Scalia R & Appel JZ 3rd & Lefer AM (1998)

Leuko-cyte–endothelium interaction during the early stages of

hypercholesterolemia in the rabbit: role of P-selectin,

ICAM-1, and VCAM-1 Arterioscler Thromb Vasc Biol

18, 1093–1100

4 Stokes KY, Clanton EC, Russell JM, Ross CR &

Granger DN (2001) NAD(P)H oxidase-derived

superoxide mediates hypercholesterolemia-induced

leukocyte–endothelial cell adhesion Circ Res 88,

499–505

5 Song L, Leung C & Schindler C (2001) Lymphocytes

are important in early atherosclerosis J Clin Invest 108,

251–259

6 Zhao Z, Beer MC, Cai L, Asmis R, Beer FC, Villiers

WJS & Westhuyzen DRV (2005) Low-density

lipopro-tein from apolipoprolipopro-tein E-deficient mice induces

macrophage lipid accumulation in a CD36 and

scaven-ger receptor class A-dependent manner Arterioscler

Thromb Vasc Biol 25, 168–173

7 Hulthe J & Fagerberg B (2002) Circulating oxidized

LDL is associated with subclinical atherosclerosis

devel-opment and inflammatory cytokines (AIR Study)

Arter-ioscler Thromb Vasc Biol 22, 62–167

8 Yla-Herttuala S, Palinski W, Butler S, Picard S,

Steinberg D & Witztum J (1994) Rabbit and human

atherosclerotic lesions contain IgG that recognizes

epitopes of oxidized LDL Arterioscler Thromb 14,

32–40

9 Ridker PM & Haughie P (1998) Prospective studies of C-reactive protein as a risk factor for cardiovascular disease J Invest Med 46, 391–395

10 Massberg S, Brand K, Gruner S, Page S, Muller E, Muller I, Bergmeier W, Richter T, Loren M, Konrad I

et al.(2002) A critical role of platelet adhesion in the initiation of atherosclerotic lesion formation J Exp Med 196, 887–896

11 Wagner DD & Burger PC (2003) Platelets in inflamma-tion and thrombosis Arterioscler Thromb Vasc Biol 23, 2131–2137

12 Marcus AJ, Broekman MJ, Drosopoulos JFH, Islam N, Pisnky DJ, Sesti C & Levi R (2003) Heterologous cell– cell interactions: thromboregulation, cerebroprotection and cardioprotection by CD39 (NTPDase-1) J Thromb Haemost 1, 2497–2509

13 Lunkes GI, Lunkes D, Stefanello F, Morsch A, Morsch VM, Mazzantti CM & Schetinger MRC (2003) Enzymes that hydrolyze adenine nucleotides in diabetes and associated pathologies Thromb Res 109, 189–194

14 Arau´jo MC, Rocha JBT, Morsch A, Zanin R, Bauchspiess R, Morsch VM & Schetinger MRC (2004) Enzymes that hydrolyze adenine nucleotides in platelets from breast cancer patients Biochem Biophys Acta

1740, 421–426

15 Lunkes GI, Lunkes D, Morsch VM, Mazzantti CM, Morsch A, Miron VR & Schetinger MRC (2004) NTPDase and 5¢-nucleotidase activities in rats with all-oxan-induced diabetes Diabetes Res Clin Pract 65, 1–6

16 Burnstock G (2002) Purinergic signaling and vascular cell proliferation and death Arterioscler Thromb Vasc Biol 22, 364–373

17 Atkinson B, Dwyer K, Enjyoji K & Robson SC (2006) Ecto-nucleotidases of the CD39⁄ NTPDase family modulate platelet activation and thrombus formation: potential as therapeutic targets Blood Cells Mol Dis 36, 217–222

18 Seye CI, Kong Q, Erb L, Garrad RC, Krugh B, Wang M, Turner JT, Sturek M, Gonza´lez FA & Weisman GA (2002) Functional P2y2 nucleotide recep-tors mediate uridine 5¢-triphosphate-induced intimal hyperplasia in collared rabbit carotid arteries Circula-tion 106, 2720–2726

19 Seye CI, Yu N, Jain R, Kong Q, Minor T, Newton J, Erb L, Gonza´lez FA & Weisman GA (2003) The P2Y2 nucleotide receptor mediates UTP-induced vascular cell adhesion molecule-1 expression in coronary artery endothelial cells J Biol Chem 278(27), 24960–24965

20 Zimmermann H (2001) Ectonucleotidases: some recent developments and note on nomenclature Drug Dev Res

52, 44–56

21 Pilla C, Emanuelli T, Frassetto SS, Battastini AMO, Dias RD & Sarkis JJF (1996) ATP diphosphohydrolase

Trang 8

activity (Apyrase, EC 3.6.1.5.) in human blood platelets.

Platelets 7, 225–230

22 Kawashina Y, Nagasawa T & Ninomiya H (2000)

Con-tribution of ecto-5¢ nucleotidase to the inhibition of

platelet aggregation by human endothelial cells Blood

96, 2157–2162

23 Marcus AJ, Broekman MJ, Drosopoulos JHF, Pinsky

DJ, Islam N, Gayle RB III & Maliszewski CR (2001)

Thromboregulation by endothelial cells: significance for

occlusive vascular diseases Arterioscler Thromb Vasc

Biol 21, 178–182

24 Papanikolaou A, Papafotika A, Murphy C,

Papamarc-aki T, Tsolas O, Drab M, Kurzchalia TV, Kasper M &

Christoforidis S (2005) Cholesterol-dependent lipid

assemblies regulate the activity of the ecto-nucleotidase

CD39 J Biol Chem 280, 26404–26414

25 Wood WG, Igbavboa U, Rao AM, Schroeder F &

Avdulov NA (1995) Cholesterol oxidation reduces

Ca2++Mg2+-ATPase activity, interdigitation, and

increase fluidity of brain synaptic plasma membranes

Brain Res 683, 36–42

26 Ortega A, Santiago-Garcı´a J, Mas-Oliva J & Lepock JR

(1996) Cholesterol increases the thermal stability of the

Ca2+⁄ Mg2+-ATPase of cardiac microsomes Biochim

Biophys Acta 1283, 45–50

27 Lijnen P, Echevaria-Vazquez D & Petrov V (1996)

Influence of cholesterol-lowering on plasma membrane

lipids and function Methods Find Exp Clin Pharmacol

18, 123–126

28 Bachorik PS & Albers JJ (1986) Precipitation methods for quantification of lipoproteins Methods Enzymol Pharmacogenetics Genomics 129, 78–100

29 Friedewald WT & Levy RI, Fredrickson DS (1972) Esti-mation of the concentration of low-density lipoprotein cholesterol in plasma, without the use of preparative ultracentrifuge Clin Chem 18, 499–502

30 Holvoet P, Stassen JM, Van Cleemput J, Collen D & Vanhaecke J (1998) Oxidized low density lipoproteins in patients with transplant-associated coronary artery dis-ease Arterioscler Thromb Vasc Biol 18, 100–107

31 Wu R & Lefvert AK (1995) Autoantibodies against oxi-dized low density lipoprotein (OxLDL): characterization

of antibody isotype, subclass, affinity and effect on the macrophage uptake of oxLDL Clin Exp Immunol 102, 174–180

32 Chan K, Delfret D & Junges K (1986) A direct colori-metric assay for Ca2+ATPase activity Anal Biochem

157, 375–380

33 Biggs R (1975) In Coagulacio´n Sanguı´nea, hemostasia y trombosis(Millan L, ed.), p 606 Editorial JIMS S95, Barcelona

34 Jentzsch AM, Bachmann H, Furst P & Biesalski H (1996) Improved analysis of malondialdehyde in human body fluids Free Radic Biol Med 2, 251–256

35 Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal Bio-chem 72, 218–254

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