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Erythrocyte acetylcholinesterase is a signaling receptor

Abstract

The acetylcholinesterase (AChE), is an enzyme located in the erythrocyte membrane that motivate continually questions, about its physiological function. The aim of this mini review is highlight the receptor behavior of AChE in human red blood cells for chemical signals associated with nitric oxide mobilization and efflux from erythrocytes. Data from the experimental models used are presented. Consequently, key participative proteins in the steps of the signal transduction pathways, in dependence of AChE receptor, are suggested to be further considered as potential therapeutic targets.

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Erythrocyte acetylcholinesterase is a signaling receptor

Author: Saldanha, Carlota,Herdade, Ana Silva
Publisher: JP Juniper Publishers
Year: 2018
Source: https://repositorio.ulisboa.pt/bitstream/10451/34389/1/Erythrocyte_acetylcholinesterase.pdf
Mini Re iew
Volume 3 Issue 4 - Janua y 2018
DOI: 10.19080/NAPDD.2018.03.555617
No App o D ug Des De
Copy igh © All igh s a e ese ed by Ca lo a Saldanha
E y h ocy e Ace ylcholines e ase is a Signaling
Recep o
Ca lo a Saldanha* and Ana Sil a He dade
Ins i u e o Biochemis y, Ins i u e o Molecula Medicine, Facul y o Medicine, Uni e si y o Lisbon, Po ugal
Recei ed Da e: Janua y 12, 2018; Published Da e: Janua y 23, 2018
*Co esponding au ho : Ca lo a Saldanha, Ins i u e o Biochemis y, Ins i u e o Molecula Medicine, Facul y o Medicine, Uni e si y o Lisbon,
Po ugal, Email:
Mini Re iew
The need o cha ac e ize he composi ion, s uc u e and
unc ion o he ed blood cells (RBCs) memb ane, he p esence
o he ace ylcholines e ase (AChE) enzyme, which kine ically
esembled he b ain es e ase, bu ma kedly di e en om
he cholines e ase ound in se um was e idenced [1]. Human
e y h ocy e AChE enzyme ac i i y is he highes one in he
mammalian scale [2,3]. The p esence o AChE a away o he
neu onal sys em aises ques ions abou i s unc ion beyond he
enzyme ac ion. He zand Kaplan in hei e ision pape poin ed
ha a e in i o hemolysis, ace ylcholines e ase ac i i y can be
eco e ed in he e y h ocy e memb ane [4]. Also he endency o
couple ion anspo mechanisms ac oss e y h ocy e memb ane
wi h AChE was explo ed wi h ailu e [4]. La e was epo ed
AChE enzyme ac i i y as a bioma ke o human ed blood
cell aging and o RBC memb ane in eg i y [5,6]. The blood o
heal hy humans p esen s a wide a ie y o a g adien scale wi h
di e en aged classes om olde o younge e y h ocy es each
one showing a iable amoun o RBCs esul ing om i s na u al
li e span o 120 days. Du ing his pe iod, exo esicles en iched
wi h AChE a e eleased om e y h ocy e memb ane o blood
ci cula ion es ing he olde e y h ocy e wi h lowe enzyme
ac i i y [5,7,8]. Conside ing gende he human emale has highe
AChE enzyme ac i i y han he men ma ched in age [9].
Highe human e y h ocy e AChE enzyme ac i i y we e
e i ied in pa ien s wi h glaucoma, essen ial hype ension, and
ALS [10]. These pa hologies a e in lamma o y ascula diseases
cha ac e ized by high concen a ion in blood o in lamma o y
molecules, eac i e oxygen species, and eac i e ni ogen species,
[10]. The RBCs AChE enzyme ac i i y da a ob ained in hose
abo e men ioned ascula diseases ein o ce he Das`s a emen
o e y h ocy e AChE be conside ed a bioma ke o in lamma ion
[11]. Das e i ied also, ha in blood samples o in lamma o y
diseases, wi h high enzyme ac i i y o e y h ocy e AChE, lowe
plasma ace ylcholine (ACh) le els we e ob ained [11].
Ace ylcholine molecule ac ing in he pa asympa he ic
sys em and in he neu on muscula junc ion, was conside ed
as a neu o ansmi e du ing se e al decades. Fu he was
also ecognized also as an an i-in lamma o y agen h ough he
in e play be ween immune and neu onal sys ems, he nomina ed
“choline gic an i-in lamma o y pa hway” [12-14]. This consis s
in he ac i a ion o ad ene gic neu ons in he spleen ha libe a e
no - epineph ine nea he T cell capable o sec e e ace ylcholine.
This non-neu onal ACh ac s on α7 subuni –con aining nico inic
ace ylcholine ecep o s exp essed on mac ophages which a e
binding induce supp ession on he syn hesis and on he sec e ion
o in lamma o y cy okines. Mac ophages ac as an in e ace
be ween he b ain and he immune sys em [15]. The ac i a ion
o a e en agus ne e by endo oxin o p o-in lamma o y
cy okines s imula es hypo halamic-pi ui a y-ad enal an i-
in lamma o y esponses conduc ed by he e e en agus ne e.
No App o D ug Des De 3(4): NAPDD.MS.ID.555617 (2018) 001
Abs ac
The ace ylcholines e ase (AChE), is an enzyme loca ed in he e y h ocy e memb ane ha mo i a e con inually ques ions, abou i s
physiological unc ion. The aim o his mini e iew is highligh he ecep o beha io o AChE in human ed blood cells o chemical signals
associa ed wi h ni ic oxide mobiliza ion and e lux om e y h ocy es. Da a om he expe imen al models used a e p esen ed. Consequen ly, key
pa icipa i e p o eins in he s eps o he signal ansduc ion pa hways, in dependence o AChE ecep o , a e sugges ed o be u he conside ed
as po en ial he apeu ic a ge s.
Keywo ds: E y h ocy e; Ace ylcholines e ase; signaling ; Ace ylcholine; Recep o
Abb e ia ions: RBCs: Red Blood Cells; AChE: Ace ylcholines e ase; ACh: Ace ylcholine; AC: Adenylyl cyclase; cAMP: cyclic Adenosine
Monophospha e (cAMP)
How o ci e his a icle: Ca lo a Saldanha and Ana Sil a He dades. E y h ocy e Ace ylcholines e ase is a Signaling Recep o . No App o D ug Des De
2018; 3(4) : 555617 DOI: 10.19080/NAPDD.2018.03.555617.
002
No el App oaches in D ug Designing & De elopmen
Back o e y h ocy e memb ane enzyme, AChE has he
pa icula i y o be inhibi ed by high concen a ions o ACh
meaning by i s own na u al subs a e, [10,16]. So, di e en ypes
o enzyme complexes may be p esen ed namely, ac i e, inac i e
and less ac i e ones acco ding he amoun o ACh exis en in
he expe imen al medium [16,17]. The unusual AChE kine ic
beha io a non-neu onal en i onmen and he disco e o ni ic
oxide (NO) p oduced in he lumen o abbi ao ic endo helium
cells unde he p esence ACh, aised us he ques ion i he e is
NO inside e y h ocy es [18]. NO was obse ed, in e y h ocy es
wi h added ACh, by luo escence mic oscopy [19]. Human
e y h ocy e suspensions, in p esence o ACh, we e loaded wi h
he pe meable non luo escen p obe diamino luo esceine-2
diace a e (DAF-2Da). In a e y h ocy e luo escence in ensi y
o iazolo luo escein (DAF-2T) was isualized as a esul om
he eac ion be ween NO and he 4,5- diamino luo escein. We
concluded ha ACh, in a dose-dependen way, is able o induce
NO mobiliza ion inside he e y h ocy e [19].
Ace ylcholine is known o be p esen in human blood
ci cula ion being p oduced by T lymphocy es and endo helial
cells [20]. The ci cula ing ACh induces asodila ion o
asocons ic ion in dependence o in eg i y o he endo helium,
ia he NO syn hesized and eleased o smoo h muscle [21].
Also he NO eleased om endo helial cells can mo e o
he lumen o he essels whe e in he blood ci cula ion is
cap u ed by ee hemoglobin o sca enged by e y h ocy e
p esen [22]. The e y h ocy e NO-heme-hemoglobin adduc o
ni osylhemoglobin is o med a high issues oxygen ension,
o example, when deoxygena ed blood en e s in o he ascula
bed o pulmona y ci cula ion [23]. A e , NO is ans e ed o he
hiol g oup o cys eine β93 o Hb o ming S- ni osohemoglobin
(SNOHb) conside ed as a NO ese oi molecule [23]. Low issue
oxygen ension is pe cei ed by e y h ocy es wi h occu ence
o s uc u al allos e ic ansi ions in SNOHb which a o he
ans e o i s NO o he hiol g oup o band 3 p o ein, allowing
he NO e lux om e y h ocy es o he capilla ies sp eading
hose issues [24].
In in i o s udies wi h e y h ocy es ob ained om heal hy
dono s unde he p esence o ACh i was e idenced inc eased
o NO e lux, e y h ocy e de o mabili y (EE) and dec eased
e y h ocy e agg ega ion and hemoglobin oxygen a ini y [25].
O he in i o s udy wi h blood samples aken om pa ien s wi h
ascula diseases such as hype ension, hype choles e olemia
and kidney ansplan , showing lowe EE han heal hy pe sons
ha was amelio a e by he p esence o ACh [24]. A nega i e
associa ion be ween EE alues and NO e lux om e y h ocy es
was showed in blood samples o hose pa ien s [26].
The NO e lux measu emen s om e y h ocy es a e based
on he ACh signal ansduc ion pa hway h ough he AChE–
ACh ac i e enzyme complex ( ac i e con o ma ion), associa ed
wi h Gαip o ein, adenylyl cyclase (AC) inhibi ion , band 3
p o ein phospho yla ion by p o ein y osine kinase (PTK),
p o ein kinase C (PKC) ac i a ion, phosphodies e ase-3 (PDE3)
ac i a ion, and low le el o adenosine iphospha e (cAMP)
molecules [17,27-31]. Lowe NO e lux om e y h ocy es we e
ob ained in p esence o elnac ine and imolol, which a e s ong
and mode a e AChE inhibi o s espec i ely, [27,31,32].
E y h ocy e S-ni osoglu a hione (GSNO) is o he NO
ese oi molecule exis ing inside e y h ocy e bu able o
be sec e ed by he binding o ACh o imolol o AChE o ming
ac i e and less ac i e enzyme complex espec i ely [33]. A
a iance GSNO e lux om e y h ocy e is null in absence o AChE
subs a e o inhibi o [33]. Meanwhile, inside he e y h ocy es
he p esence o he inac i e complex AChE-VM showed highe
GSNO concen a ion in ela ion o he ac i e enzyme complex
AChE-ACh [27,31]. A opposi e GSNO le els inside e y h ocy es
we e lowe in p esence o he less ac i e enzyme complex AChE–
imolol han in he case o he ac i e enzyme complex AChE-ACh
[33,34]. F om all he da a ob ained in he abo e desc ibed s udies
we e idenced ha e y h ocy e AChE beyond i s enzyme ac i i y
unc ion as a ecep o o signal molecules able o induce escue
o NO e lux om human e y h ocy es and i s mobiliza ion om
ese oi molecules. The NO de i a i e molecules inside hem
as ni i e, ni a e and pe oxyni i e we e also quan i ied in all
men ioned s udies.
The key p o ein molecules pa icipan s in he chemical
signal ansduc ion mechanism o NO unde AChE ecep o
once iden i ied we e submi ed o inhibi o s o ac i a o s in in
i o models o hype ib inogenemia [35,36]. The acu e phase
p o ein ib inogen binds o RBCs memb ane CD47p o ein
pa ne o he Rh mac o-complex which is connec ed o he
cy oskele on ia p o ein 4.2, and in e ac s also wi h he majo
RBC mac o- -complex band 3 p o ein [37]. The p esence o
AChE-ACh and AChE- imolol complexes in RBCs induced he
e u n o no mal alues he highe NO e lux ob ained unde
high ib inogen concen a ion [35,38-40]. Consequen ly his NO
sca enged a oids he inc ease concen a ions o he eac i e
ni ogen and oxygen species p esen in in lamma o y condi ions.
Remembe ing ha he in lamma o y esponse is sys emically
associa ed wi h a iable deg ee o endo helium dys unc ion,
high plasma ACh and ib inogen concen a ions, he abo e da a
a e is acco dance wi h o he s ha conside ace ylcholine as an i-
in lamma o y agen . Ou s udies pe o med in i o wi h animal
models o in lamma ion demons a ed he an i-in lamma o y
unc ion o ACh [41].
The e y h ocy es ob ained om blood samples o pa ien s
wi h open glaucoma e idenced ex- i o highe NO e lux alues,
in e nal GSNO le els and AChE enzyme ac i i y alues, han hose
assessed in e y h ocy es o heal hy pe sons [34,42]. Wi h hese
da a we can unde s and he he apeu ic e icacy o o skolin
in glaucoma pa ien s [43]. Fo skolin is AC ac i a o , meaning
syn hesis o cAMP le els inside RBCs, ha e e ed he highe
NO e lux om e y h ocy es model o hype ib inogenemia [44].
Fib inogen binding o RBCs augmen ed he NO e lux unde lowe
le els o cAMP [36]. I will be necessa y o con i m in glaucoma
pa ien s unde o skolin he apy whe he no maliza ion o NO
How o ci e his a icle: Ca lo a Saldanha and Ana Sil a He dades. E y h ocy e Ace ylcholines e ase is a Signaling Recep o . No App o D ug Des De
2018; 3(4) : 555617 DOI: 10.19080/NAPDD.2018.03.555617.
003
No el App oaches in D ug Designing & De elopmen
e lux and lowe ni ogen eac i e species occu [34,44]. Also
NO dono s like ni oglyce in ac s in ea men and p e en ion o
endo helium dys unc ion [45].
Conclusion
In conclusion he p o eins he apeu ic a ge s o con ol he
RBCs bioa ailabili y in NO (e lux o sca enge) in in lamma o y
ascula disease a e AChE, AC, Gi , PTP , PTK, PKC, PI3K and
PD3 . Some ac i a o s and inhibi o s o hose p o eins a e
al eady disposal o examples ace ylcholine, elnac ine, imolol,
ad enaline, o skolin, alsa an, wo mannin de i a e and
ilop os .
Acknowledgmen
This wo k was unded by Fundação pa a a Ciência e Tecnologia:
LISBOA-01-0145-FEDER-007391, p ojec co undedby FEDER,
h ough POR Lisboa 2020 - P og ama Ope acional Regional de
Lisboa, Po ugal 2020. The au ho is also g a e ul o Emilia Al es
o ype-w i ing he e e ences.
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DOI:
10.19080/NAPDD.2018.03.555617