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Tiêu đề Mitochondria Regulate Platelet Metamorphosis Induced By Opsonized Zymosan A – Activation And Long-Term Commitment To Cell Death
Tác giả Paola Matarrese, Elisabetta Straface, Giuseppe Palumbo, Maurizio Anselmi, Lucrezia Gambardella, Barbara Ascione, Domenico Del Principe, Walter Malorni
Trường học Istituto Superiore di Sanità
Chuyên ngành Therapeutic Research and Medicines Evaluation
Thể loại báo cáo khoa học
Năm xuất bản 2009
Thành phố Rome
Định dạng
Số trang 12
Dung lượng 711,72 KB

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At a later time point 24 h, opsonized zymosan was found to induce increased expression of CD47 adhesion molecule, platelet aggregation, mitochondrial membrane depolarization and phosphat

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by opsonized zymosan A – activation and long-term

commitment to cell death

Paola Matarrese1, Elisabetta Straface1, Giuseppe Palumbo2, Maurizio Anselmi2, Lucrezia

Gambardella1, Barbara Ascione1, Domenico Del Principe2and Walter Malorni1

1 Department of Therapeutic Research and Medicines Evaluation, Istituto Superiore di Sanita’, Rome, Italy

2 Department of Pediatrics, University of Rome Tor Vergata, Italy

Several mechanisms are brought into play in order

to control the balance between platelet production

and destruction Among these, recent studies have

identified a form of apoptosis Platelets have been

shown to be able to undergo apoptosis in response

to various stimuli [1,2] It has been reported that platelet differentiation recapitulates morpho-func-tional events that are typical of apoptosis, such as trans-bilayer migration of phosphatidylserine (PS) to the outer membrane leaflet [3] Platelets also express

Keywords

aggregation; apoptosis; mitochondrial

membrane potential; platelets; zymosan

Correspondence

P Matarrese, Department of Therapeutic

Research and Medicines Evaluation, Section

of Cell Aging and Degeneration, Istituto

Superiore di Sanita’, viale Regina Elena 299,

00161 Rome, Italy

Fax: +39 6 49903691

Tel: +39 6 49902010

E-mail: paola.matarrese@iss.it

(Received 1 November 2008, revised 25

November 2008, accepted 3 December

2008)

doi:10.1111/j.1742-4658.2008.06829.x

Changes in the mitochondrial membrane potential play a key role in deter-mining cell fate Mitochondria membrane hyperpolarization has been found to occur after cell activation, e.g in lymphocytes, whereas depolar-ization is associated with apoptosis The aim of this study was to investi-gate the effects of an immunological stimulus, i.e opsonized zymosan A,

on human platelet mitochondria by means of flow and static cytometry analyses as well as biochemical methods We found that opsonized zymo-san induced significant changes of platelet morphology at early time points (90 min) This was associated with increased production of reactive oxygen species, and, intriguingly, mitochondrial membrane hyperpolarization At a later time point (24 h), opsonized zymosan was found to induce increased expression of CD47 adhesion molecule, platelet aggregation, mitochondrial membrane depolarization and phosphatidylserine externalization Although these late events usually represent signs of apoptosis in nucleated cells, in opsonized zymosan-treated platelets they were not associated with mem-brane integrity loss, changes in Bcl-2 family protein expression or caspase activation In addition, pre-treatment with low doses of the ‘mitochon-driotropic’ protonophore carbonyl cyanide p-(trifluoro-methoxy)phenyl-hydrazone counteracted mitochondrial membrane potential alterations, production of reactive oxygen species and phosphatidylserine externaliza-tion induced by opsonized zymosan Our data suggest that mitochondrial hyperpolarization represents a key event in platelet activation and remo-deling under opsonized zymosan immunological stimulation, and opsonized zymosan immunological stimulation may represent a useful tool for under-standing of the pathogenetic role of platelet alterations associated with vascular complications occurring in metabolic and autoimmune diseases

Abbreviations

AM, acetoxymethyl ester; DHR123, dihydrorhodamine 123; DIC, differential interference contrast; FCCP, carbonyl cyanide p-(trifluoro-methoxy) phenylhydrazone; IVM, intensified video microscopy; JC-1, 5-5¢,6-6¢-tetrachloro-1,1¢,3,3¢-tetraethylbenzimidazol-carbocyanine iodide; MMP, mitochondrial membrane potential; OPZ, opsonized zymosan; PRP, platelet-rich plasma; PS, phosphatidylserine; ROS, reactive oxygen species.

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many components of nucleated-cell apoptosis such as

caspases [1,4]

Mitochondria are generally considered to be key

players in cell life and death In addition to energy

supply, they have also been demonstrated to be

involved in execution of apoptosis via the release of

apoptogenic factors such as cytochrome c [5] Human

blood platelet mitochondria play a critical role as they

work efficiently as energy factories for both resting

and stimulated cells Mitochondria are also involved in

non-ATP-related functions such as oxygen radical

generation and apoptotic-like events In fact,

mito-chondrial damage has been reported to be a key step

in platelet apoptosis, and mitochondrial membrane

potential (MMP) is lost during storage and under

other conditions [4,6,7] Changes in the mitochondrial

permeability transition pore have been hypothesized to

play a role in production of so-called coated platelets,

a sub-population of platelets observed upon

dual-agonist activation, e.g thrombin plus collagen, that

express surface PS and can be induced by activation of

the pro-apoptotic Bcl-2 family member Bax [3] Hence,

mitochondria integrity and function appear to act as

general regulators of platelet fate in terms of both

acti-vation and apoptosis, two processes that, in platelets,

appear to share some common features, e.g PS

exter-nalization

Zymosan A, a complex polysaccharide obtained

from Saccharomyces cerevisiae, is a complement

activa-tor that can be used as a tool to investigate the role of

activated platelets in several diseases, including

immune complex-mediated inflammation and its

vascu-lar complications [8] Once opsonized, zymosan A has

been suggested to activate platelets in a

complement-and fibrinogen-dependent way In particular,

comple-ment components, such as C5, C6 and C7, are

necessary, and IgG binding is also required for

zymo-san opsonization [9,10] Hence, opsonized zymozymo-san

(OPZ) could represent a suitable model for the study

of platelets as ‘inflammatory’ cells In view of this, we

decided to investigate whether this immunological stimulus may induce mitochondria dysfunction and influence platelet fate We found that mitochondria modifications have a dual role, controlling both plate-let activation and death

Results Characterization of morphological modifications induced by OPZ

Treatment with OPZ induced two main modifications

of platelet morphology: (a) cell remodeling typical of activation at early time points (after 30 and, more markedly, 90 min), and (b) platelet aggregation after

24 h With regard to cell remodeling, we decided to analyze the actin cytoskeleton organization This appeared to be significantly modified by OPZ (Fig 1A): redistribution of actin filaments, forming long actin-positive protrusions (arrows), was detected

in platelets exposed for 90 min to zymosan (central panel), and, more especially, to OPZ (right panel) Scanning electron microscopy analysis indicated that exposure to OPZ for 30 (not shown) and 90 min (Fig 1B) appeared to activate platelets: the typical round morphology of platelets was altered to an activated morphology characterized by emission of thin protrusions A series of analyses were also per-formed using CD47, the thrombospondin receptor, a surface molecule involved in cell adhesion [11] Flow cytometry analyses revealed no changes at early time points, but platelet alterations were observed 24 h after OPZ administration A platelet sub-population overexpressing CD47 was detected in zymosan-trea-ted, and especially OPZ-treazymosan-trea-ted, platelets (a represen-tative flow cytometry analysis is shown in Fig 1C) This increased expression was also detected by immunofluorescence analysis, and platelet aggre-gates were detectable after both zymosan and OPZ treatments (Fig 1D) The number of aggregates was

Fig 1 Characterization of platelet modifications induced by OPZ (A, B) Morphological alterations (A) IVM analysis of actin microfilaments Actin-positive protrusions (arrows) are visible in treated platelets (90 min) Insets in the middle and right panels show bright-field micrographs that have been electronically inverted to highlight these thin protrusions (arrows) Magnification ·1500 (B) Scanning electron microscopy Exposure to zymosan A (opsonized and non-opsonized) for 90 min changed round-shaped resting platelets (control, left panel) into activated platelets characterized by the emission of long thin protrusions Magnification ·4000 (C–F) CD47 expression and cell-aggregation analyses (C) Histograms representing flow cytometry evaluation of surface expression of the adhesion molecule CD47 are shown in the upper panels Numbers represent the percentage of highly positive platelets In the lower panels, dot plots of the physical parameters of the platelet popu-lation (one representative experiment) are shown (D) IVM analysis showing the intracellular distribution of CD47 molecule in zymosan-trea-ted cells (central panel) and OPZ-treazymosan-trea-ted cells (right panel) (E) DIC (Nomarski) micrographs showing cell aggregates in zymosan-treazymosan-trea-ted platelets (central panel) and OPZ-treated platelets (right panel) in comparison with untreated platelets (left panel) In (D) and (E), arrows indi-cate platelet aggregates (F) Quantification of cell aggregation by morphometric analysis performed using DIC Values are means and SD of the results obtained in three independent experiments *P < 0.01 versus control platelets; P < 0.01 versus zymosan-treated platelets.

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Opsonized zymosan Zymosan

Untreated 5

10

20

1000

10 0 10 1 10 2 10 3 10 4 10 0 10 1 10 2 10 3 10 4 10 0 10 1 10 2 10 3 10 4

Untreated

Untreated A

B

C

D

E

F

5 µm

5 µm

Zymosan 24 h

Zymosan 90 min

Opsonized zymosan 24 h Opsonized zymosan 90 min

Fluorescence

0

FSC-Height

1000

0

FSC-Height

1000

0

FSC-Height

10 µm

5 µm

*

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evaluated The results of morphometric analysis by

fluorescence microscopy (CD47-stained samples) and

differential interference contrast (DIC, i.e Nomarski

microscopy, Fig 1E,F) clearly indicated that the

number of aggregates, which was negligible in

con-trol samples, was significantly increased in

OPZ-trea-ted samples in comparison with non-opsonized

zymosan-treated cells (Fig 1F)

OPZ-induced MMP alterations

On the basis of previous studies, which reported

increased MMP (hyperpolarization) in conjunction

with cell activation, e.g in lymphocytes [12,13], and

MMP loss (depolarization) in conjunction with

apop-tosis [5], we analyzed this parameter in platelets treated

with opsonized and non-opsonized zymosan A at

vari-ous time points Quantitative flow cytometry analysis,

performed using a JC-1 probe (a representative

experi-ment is shown in Fig 2A), clearly indicated the

pres-ence of a significantly higher percentage of cells with

hyperpolarized mitochondria (see boxed areas) after

treatment with OPZ (third row) in comparison with

either untreated platelets (first row) or platelets treated

with non-opsonized zymosan (second row)

Impor-tantly, this hyperpolarization of mitochondrial

mem-brane started early after OPZ addition (second

column) and peaked after 90 min (third column)

Interestingly, 24 h after OPZ addition (third row,

fourth column), flow cytometry analysis clearly

revealed a significant percentage of cells

(approxi-mately 35%) displaying mitochondrial membrane

depolarization These effects were also evident by

pool-ing together data obtained from four independent

experiments: Fig 2B,C shows the percentage of cells

with hyperpolarized or depolarized mitochondria,

respectively Altogether, these results indicate that

mitochondria of platelets treated with OPZ underwent

a marked increase in MMP at early time points (until

90 min), followed by a significant MMP loss at later

time points (starting from 24 h) Importantly, in our

experimental system, the decrease in MMP was not

paralleled by an alteration of Bax (Fig 2D) or Bak

(Fig 2E) expression levels

OPZ-induced ROS production Mitochondrial hyperpolarization has been related to hyperproduction of reactive oxygen species (ROS) [13,14] A quantitative time-course analysis of ROS generation during zymosan A treatment was thus per-formed using flow cytometry In accordance with the MMP data, increased ROS production was detected in OPZ-treated platelets using dihydrorhodamine 123 (DHR123) A representative experiment is shown in Fig 3A [compare control platelets (left) and non-ops-onized zymosan-treated platelets (middle panel) with OPZ-treated platelets (right)] The results obtained from four independent experiments are reported in Fig 3B In OPZ-treated cells, increased ROS produc-tion was detectable at earlier time points (30 and

90 min), but the values detected after 24 h were similar

to those found in control samples

OPZ induces PS externalization (but not caspase activation)

We analyzed PS externalization in platelets under vari-ous experimental conditions Flow cytometry evalua-tion of cell-surface expression of PS was performed using annexin V⁄ trypan blue double staining Fig-ure 4A shows the results of a representative experi-ment, and Fig 4B shows mean values obtained from four independent experiments These analyses clearly indicated that, in the absence of any stimulus, platelets displayed very low levels of PS at their surface up to

24 h after isolation (first row, bottom right quadrant), and non-opsonized zymosan treatment induced a small increase of the percentage of annexin V-positive cells (second row), whereas a time-dependent increase in PS externalization was observed in OPZ-treated cells (third row, bottom right quadrant) Interestingly, neither non-opsonized nor OPZ-treated platelets were positive for trypan blue dye (see percentages in the upper right quadrant), indicating that the plasma membrane of most cells was undamaged at least up to 24 h (Fig 4A, third row, fourth column) and 48 h (not shown) after OPZ administration These results were clearer when data obtained from four independent experiments were

Fig 2 OPZ induces MMP alterations (A) Biparametric flow cytometry analysis of MMP after staining with JC-1 in untreated platelets (first row), platelets treated with zymosan A (second row) and platelets treated with OPZ (third row) at various time points The numbers in the boxed areas represent the percentages of cells with hyperpolarized mitochondria The percentages of cells with depolarized mitochondria are shown below the dashed line The results obtained in a representative experiment are shown (B, C) Mean percentage (and SD) of plate-lets with hyperpolarized (B) or depolarized (C) mitochondria obtained from four cytofluorimetric experiments Statistical analyses indicate a significant (P < 0.01) increase in cells with hyperpolarized or depolarized mitochondria at early (up to 90 min) and late (24 h) time points, respectively, only in platelets challenged with OPZ (D, E) Bax (D) and Bak (E) expression levels as evaluated by FACS analysis The y axis shows the median values of fluorescence as the mean and SD from four independent experiments.

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pooled (Fig 4B) Data on cell viability obtained by the

trypan blue exclusion test were confirmed using

calcein-acetoxymethyl ester (AM) (Fig 4C)

On the basis of these results, analysis of the activa-tion state of the main execuactiva-tioners of apoptosis, i.e caspases, was required We found that neither zymosan

Untreated

Zymosan

Opsonized zymosan

40 75

60

45

30

15

0

30 20 10 0

5 4 3 2 1 0

5

D

B

A

C

E 4

3

2

1

0

T 90 min T 24 h

7.1

11.1

11.5

25.1

15.2

16.7

12.2 11.2

14.9 12.2

30.4 7.3

6.9

10.6

7.1 5.6

J-monomers

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(Fig 5A) nor OPZ (Fig 5B) induced activation of

caspases 3 and 9 at any time point considered In

par-ticular, 90 min after zymosan A administration, when

we observed the maximum OPZ-induced MMP

hyper-polarization (Fig 2) and ROS production (Fig 3),

activation of caspase 9 (which depends on the release

of mitochondrial apoptogenic factors) [5] and

cas-pase 3 (the main enzyme involved in cascas-pase-depen-

caspase-depen-dent apoptosis) was negligible Even if the zymosan A

exposure time was prolonged to 24 h, at which time

PS externalization and mitochondrial membrane

depo-larization were observed (see Fig 4), no significant

activation of these caspases was detected As a positive

control, platelets treated with 1 UÆmL)1 of thrombin

for 1 h (in the presence or absence of the specific cas-pase inhibitors) were studied (Fig 5C) Data obtained

in positive controls or in platelets treated for 24 h with opsonized and non-opsonized zymosan A were confirmed by western blot analysis (Fig 5D)

MMP plays a key role in OPZ-mediated effects

We examined the effects of an agent that is capable of specifically influencing MMP homeostasis and cell fate [12,14]: the protonophore uncoupler carbonyl cyanide fluorophenyl-hydrazone (FCCP), which is known to hinder the mitochondria hyperpolarization pheno-menon at low doses [15] In particular, the ability of

T0

T 30 min

T 90 min

T 24 h

Untreated

A

B

10 0 10 1 10 2 10 3 10 4 10 0 10 1 10 2 10 3 10 4 10 0 10 1 10 2 10 3

M = 32.2

M = 44.2

M = 58.6

M = 22.5

M = 17.3

M = 21.4

M = 19.1

M = 22.7

M = 18.4

M = 20.3

M = 17.1

M = 31.6

10 4

Zymosan Opsonized zymosan

Untreated

*

*

70 60 50 40 30 20 10 0

Green fluorescence intensity

Fig 3 OPZ induces production of reactive oxygen species Quantitative cytofluorimetric analysis of ROS production was performed using DHR123 (A) Results obtained in a representative experiment The values represent the median fluorescence (B) Mean values (and SD) obtained from four independent experiments *P < 0.01 versus control and zymosan-treated cells.

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FCCP to counteract the OPZ-induced effects in terms

of ROS production, MMP alterations and PS

external-ization was studied (Fig 6) In our experiments, a very

low dose (20 nm) of FCCP was able to hinder both the early and late events induced by OPZ In platelets pre-treated with FCCP, the increase in ROS

T0 T 30 T 90

Minutes

T 24 h

Minutes

T 24 h

T0 T 30 T 90

Minutes 0

10

20

30

40

0 10 20 30 40

0 10 20 30 40

T 24 h

Untreated

Untreated

5.3 1.4

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A

B

C

2.1

0.4 1.9

0.6 5.9

0.8 6.1

1.3 6.5

2.1 6.7

4.4 34.9

1.3 17.3

0.6 14.3

0.5 7.4

Zymosan

Zymosan

Exposure time

Opsonized zymosan

Opsonized zymosan

Untreated 24 h

Calcein-AM (green fluorescence)

Zymosan 24 h Opsonized zymosan 24 h

Annexin V

Annexin V positive Trypan blue positive

10 0 10 1 10 2 10 3 10 4 10 0 10 1 10 2 10 3 10 4 10 0 10 1 10 2 10 3 10 4

Fig 4 OPZ induces PS externalization (A) FACS analysis after double staining with annexin V ⁄ trypan blue Dot plots from a representative FACS experiment are shown Numbers represent the percentages of annexin V-positive cells (bottom right quadrant) or annexin V ⁄ trypan blue double positive cells (upper quadrant) Note the very low percentage of cells that are positive for trypan blue (B) Results obtained from four independent experiments, reported as means and SD (C) FACS analysis after staining with calcein-AM (which is retained in the cytoplasm of live cells) of platelets treated with zymosan (central panel) or OPZ (right panel) for 24 h Untreated platelets incubated for 24 h at 37 C (left panel) were used as the control Numbers represent the percentage of calcein-negative cells One representative experiment is shown.

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production induced by OPZ administration for 90 min

was significantly reduced (Fig 6A, compare shaded

gray histograms with black histograms) Fittingly, the

mitochondrial membrane hyperpolarization state

observed 90 min after treatment with OPZ was

signifi-cantly inhibited by low doses of FCCP (compare

boxed areas in Fig 6B, first and third panels, with

Fig 2B) The same protective effect of FCCP was

observed with respect to mitochondrial membrane

depolarization induced by 24 h treatment of OPZ

(compare areas under the dashed line in Fig 6B,

sec-ond and fourth panels, with Fig 2C) Similarly, the PS

externalization observed in platelets treated for 24 h with OPZ (see Fig 4) was negligible when platelets were pre-exposed to FCCP (Fig 6C)

Discussion Serum opsonized zymosan (from yeast cell walls) is known as a model phagocytic stimulus that interacts with both immunoglobulin and complement recep-tors, is ingested, and activates oxidative mechanisms Because OPZ engages at least two types of receptor, the signaling pathways triggered by this stimulus are

Caspase 9

Caspase 3

Caspase 3

Caspase 9 activation control

Caspase 3 activation control

Caspase 9

Caspase 3

LEHD-fmk

DEVD-fmk

Positive control

Green fluorescence

Green fluorescence

T 90 min

T 90 min

T 24 h

T 24 h

Zymosan

Opsonized zymosan

T0

T0

A

B

10 0 10 4

10 0 10 4 10 0 10 4

74.6

69.3 13.4

2 32

20

32 20

10 0 10 4

Fig 5 OPZ does not induce caspase activa-tion Analysis of the activation state of casp-ases 3 and 9 in intact living platelets treated with zymosan (A) or opsonized zymosan (B)

at various time points (C) Activation state

of caspases 3 and 9 in a positive control represented by platelets treated for 1 h with thrombin (1 UÆmL)1) in medium containing

1 m M Ca 2+ Values are the percentage of cells containing these caspases in their active form Results obtained in a represen-tative experiment are reported (D) Western blot analysis of caspase 3 in thrombin-trea-ted platelet (lane 2; compare with control in lane 1); untreated platelets (lane 3); platelets treated for 24 h with zymosan (lane 4) or with OPZ (lane 5).

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complex The stimulus may be considered as an

immunological stimulus, which is also able to affect

human platelets by inducing an oxidative burst [10]

Here we show that OPZ can trigger platelet

meta-morphosis [10], consisting of morphological and

bio-chemical changes, that is typical of activation In

fact, platelets rapidly changed from a discoid form

to an activated shape characterized by emission of

long actin-positive protrusions At the last time point

(24 h), OPZ treatment was found to lead to CD47

overexpression and platelet aggregation It has been

suggested that platelet activation and adhesion are

associated with morphological modifications, CD47

overexpression and platelet aggregation [10,11]

How-ever, these changes were accompanied by an early

and transient production of ROS, which probably

serve, as in other cell systems, as signaling molecules

of biological significance Activation of platelets by

OPZ was associated with a transient burst in ROS,

which was possibly due, at least in part, to the

energy metabolism [16] Indeed, zymosan A, an

acti-vator of the alternative complement pathway, has

been hypothesized to activate platelets in plasma in

a complement- and fibrinogen-dependent way

[9,10,17] Hence, immunological stimulation by OPZ

could trigger a complex cascade of events leading to platelet remodeling and activation

The main result reported here is that OPZ-stimu-lated platelets underwent a time-dependent hyperpo-larization of mitochondria, which started early (30 min) and lasted until 90 min Such mitochondrial hyperpolarization was previously observed in T cells, and was considered as an activation-associated event [12] Although the mechanism underlying this MMP increase remains unclear, it has been suggested that it could be associated with ROS signaling and could represent an early metabolic change ‘preparing’ the cell for the death process [18] On the basis of our results, we can hypothesize that mitochondrial hyper-polarization could be associated, as in lymphocytes, with platelet activation In accordance with results obtained in other cell types [14,15], the fact that the

‘stabilizing’ effect of the ‘mitochondriotropic’ drug FCCP prevented OPZ-induced mitochondrial mem-brane hyperpolarization as well as platelet morpho-logical remodeling seems to suggest that the hyperpolarization state of mitochondria might repre-sent an early transient key event sustaining platelets towards an activated phenotype, probably creating a pseudo-hypoxic redox state characterized by normoxic

Zymosan M = 15

A

B

T 90 min

10 0

10 1 10 2 10 3 10 4

Green fluorescence

J-monomers

Annexin V

10 0

10 1 10 2 10 3 10 4

T 90 min

T 90 min

10.1

7.4 5.4

1.6

Opsonized zymosan M = 63 FCCP + Zymosan M = 21

FCCP + Zymosan

FCCP + Opsonized zymosan M = 32

FCCP + Opsonized zymosan

Fig 6 The mitochondrial membrane

poten-tial plays a key role in zymosan-mediated

effects Quantitative flow cytometry

evalua-tion of (A) ROS producevalua-tion, (B) MMP and

(C) PS externalization in platelets pre-treated

with a low dose of FCCP (20 n M ) before

addition of opsonized or non-opsonized

zymosan A Pre-treatment with FCCP

signifi-cantly reduced OPZ-induced ROS production

(A, compare shaded gray histograms with

black empty histograms), mitochondrial

membrane hyperpolarization (compare

boxed areas in B, first and third panels, with

Fig 2B), mitochondrial membrane

depolari-zation (compare areas under the dashed line

in B, second and fourth panels, with

Fig 2C), and PS externalization (compare

numbers in C with those in Fig 4) The

results shown were obtained in one

experi-ment (representative of four) Values in (A)

represent median fluorescence; those in (B)

and (C) represent percentages of cells.

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decreases of ROS and a shift from oxidative to

glyco-lytic metabolism [19] As in other systems, low doses

of FCCP could inhibit ROS signaling events that lead

to the programmed mitochondrial destruction termed

mitoptosis [20] In nucleated cells, mitochondria

hyperpolarization occurs early after the apoptotic

commitment, and is followed by MMP loss It is

widely accepted that the latter could contribute to

apoptosis [5] Our model system provides some

fur-ther clues on this matter, and underlines the

differ-ences between nucleated and non-nucleated cells We

found that PS externalization, a typical early marker

of apoptosis in nucleated cells, also occurs early in

OPZ-stimulated platelets, together with ROS

produc-tion and mitochondria hyperpolarizaproduc-tion Platelets,

however, maintain their integrity for a long time (at

least 48 h) despite MMP loss and increased PS

exter-nalization As recently reported for other stimuli,

including engagement of immunoreceptors [21], OPZ

induced non-apoptotic externalization of PS

Further-more, OPZ-treated platelets dis not show either

cas-pase activation or an increase in Bcl-2 family

proteins, nor cell death On this basis, we can also

hypothesize that, in some immunopathological

instances, the increased number of platelets could be

due to a defective death of these cells (although

PS-positive) rather than de novo production of these

cells Conversely, other stimuli, such as collagen plus

thrombin, have recently been demonstrated to induce

PS externalization, a decrease in MMP, increased

expression of the Bcl-2 proteins Bax and Bak, caspase

activation and cell death [2,3] In addition, the

physi-ological platelet agonist thrombin also induces Bid,

Bax and Bak translocation to the mitochondria and

endogenous generation of hydrogen peroxide, which

stimulates cytochrome c release and activation of

caspases 3 and 9 [22] Thus, OPZ appears to be a

valuable activating agent triggering a long-term

com-mitment to apoptosis (as also suggested by

OPZ-in-duced PS externalization) rather than a typical

apoptotic inducer The previously hypothesized role

of PS externalization and its role as an adhesion

fac-tor in cell–cell interaction therefore requires

reap-praisal [4,23] For instance, platelet binding to

dysfunctional endothelium was found to be inhibited

by the phosphatidylserine-binding protein annexin V

and enhanced by platelet agonists [24]

Give the importance of the loss of functional

integ-rity of platelets in the pathogenesis of cardiovascular

complications often associated with diabetes and some

autoimmune diseases, e.g antiphospholipid syndrome

or Kawasaki disease [25,26], the results reported

here indicate that OPZ could represent a prototypic

immunological stimulus for study of the pathogenic mechanisms of these diseases

Experimental procedures Platelet isolation and treatments Blood samples were collected from healthy volunteer blood donors who had taken no drugs for at least 10 days The platelets were obtained by mixing fresh blood samples with

a 1⁄ 6th volume of acid ⁄ citrate dextrose (38 mm citric acid,

75 mm Na3 citrate, 135 mm glucose) as anticoagulant All the experiments were performed in platelet-rich plasma (PRP), which was prepared by centrifugation of blood sam-ples at 150 g for 10 min at room temperature Opsonized zymosan was obtained as previously reported [27] Briefly, zymosan A (Sigma Chemical Co., St Louis, MO, USA) was boiled for 20 min and then washed for 5 min three times in NaCl⁄ Pi After washing, boiled zymosan A was added to platelet-poor plasma (obtained by centrifugation of PRP at

1000 g) and incubated at 37C for 30 min After washing three times, OPZ was ready to use Control samples were prepared using non-opsonized zymosan A Stimulation of the platelets was achieved by incubating PRP with

4 mgÆmL)1OPZ at 37C for various durations After incu-bation with zymosan, PRP was centrifuged at 700 g for

5 min, and washed platelets were prepared for various analyses For experiments with FCCP (Molecular Probes, Leiden, The Netherlands), PRP was incubated for 10 min with 20 nm FCCP before addition of zymosan A (both opsonized and non-opsonized) Samples treated with FCCP alone were also studied

Platelets were analyzed at various time points (5, 10, 20,

30 and 90 min and 6, 8 and 24 h) after treatment with non-opsonized zymosan A or OPZ The main changes were detected after 30, 90 min and 24 h: only the results obtained at these time points are shown here In addition,

we also analyzed platelets treated with zymosan A (opson-ized and non-opson(opson-ized) and immediately washed three times These were considered as controls to test the responsiveness of platelets immediately after interaction with zymosan A, and this time point is indicated as T0

Scanning electron microscopy Samples were collected and plated on poly-l-lysine-coated slides, and fixed with 2.5% glutaraldehyde in 0.1 m cacody-late buffer (pH 7.4) at room temperature for 20 min After post-fixation in 1% OsO4 for 30 min, samples were dehy-drated through a graded ethanol series, critical point-dried in

CO2 and gold-coated by sputtering using a Balzers Union SCD 040 apparatus (Balzers, Weisbaden, Germany) The samples were examined using a Cambridge 360 scanning elec-tron microscope (Leica Microsystem, Wetzlar, Germany)

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