Demonstration of extrapulmonary activity of angiotensin converting enzyme in intact tissue preparations

1 The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Capto...

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Published inBritish journal of pharmacology Vol. 100; no. 1; pp. 49 - 54
Main Authors Lembeck, F., Griesbacher, T., Eckhardt, M.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.05.1990
Nature Publishing
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Abstract 1 The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Captopril was employed as a specific inhibitor of ACE. 2 Captopril augmented the BK‐induced contractions of the rat isolated uterus, the BK‐ and substance P‐induced contractions of the guinea‐pig ileum, and the BK‐induced venoconstriction in the isolated perfused ear of the rabbit. Degradation of BK by ACE was calculated to be 52% in the rat uterus and 75% in the rabbit perfused ear. 3 Captopril inhibited the A I‐induced contractions of the rat isolated colon, the A I‐induced vasoconstriction in the isolated perfused ear of the rabbit and the rise in blood pressure induced by i.a. injections of A I in pithed rats. Conversion of A I to A II was calculated to be 13% in the rat colon and 26% in the rabbit perfused ear. 4 From estimations of the A II activity (bioassay on the rat colon) in the effluent of the perfused ear of the rabbit after injections of A I into the arterial inflow cannula it was calculated that approximately one tenth of A I was converted to A II during a single passage through the ear (less than 15 s). 5 The present experiments suggest that the high activity of ACE in endothelium of blood vessels of extrapulmonary tissues may provide an additional (endothelium‐dependent) local vasoconstrictor mechanism by the rapid formation of A II and inactivation of BK. The ACE activity in non‐vascular smooth muscles, other than those of blood vessels, may also affect the physiological functions of these tissues.
AbstractList 1. The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Captopril was employed as a specific inhibitor of ACE. 2. Captopril augmented the BK-induced contractions of the rat isolated uterus, the BK- and substance P-induced contractions of the guinea-pig ileum, and the BK-induced venoconstriction in the isolated perfused ear of the rabbit. Degradation of BK by ACE was calculated to be 52% in the rat uterus and 75% in the rabbit perfused ear. 3. Captopril inhibited the A I-induced contractions of the rat isolated colon, the A I-induced vasoconstriction in the isolated perfused ear of the rabbit and the rise in blood pressure induced by i.a. injections of A I in pithed rats. Conversion of A I to A II was calculated to be 13% in the rat colon and 26% in the rabbit perfused ear. 4. From estimations of the A II activity (bioassay on the rat colon) in the effluent of the perfused ear of the rabbit after injections of A I into the arterial inflow cannula it was calculated that approximately one tenth of A I was converted to A II during a single passage through the ear (less than 15 s). 5. The present experiments suggest that the high activity of ACE in endothelium of blood vessels of extrapulmonary tissues may provide an additional (endothelium-dependent) local vasoconstrictor mechanism by the rapid formation of A II and inactivation of BK. The ACE activity in non-vascular smooth muscles, other than those of blood vessels, may also affect the physiological functions of these tissues.
1. The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Captopril was employed as a specific inhibitor of ACE. 2. Captopril augmented the BK-induced contractions of the rat isolated uterus, the BK- and substance P-induced contractions of the guinea-pig ileum, and the BK-induced venoconstriction in the isolated perfused ear of the rabbit. Degradation of BK by ACE was calculated to be 52% in the rat uterus and 75% in the rabbit perfused ear. 3. Captopril inhibited the A I-induced contractions of the rat isolated colon, the A I-induced vasoconstriction in the isolated perfused ear of the rabbit and the rise in blood pressure induced by i.a. injections of A I in pithed rats. Conversion of A I to A II was calculated to be 13% in the rat colon and 26% in the rabbit perfused ear. 4. From estimations of the A II activity (bioassay on the rat colon) in the effluent of the perfused ear of the rabbit after injections of A I into the arterial inflow cannula it was calculated that approximately one tenth of A I was converted to A II during a single passage through the ear (less than 15 s).
The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Captopril was employed as a specific inhibitor of ACE. Captopril augmented the BK-induced contractions of the rat isolated uterus, the BK- and substance P-induced contractions of the guinea-pig ileum, and the BK-induced venoconstriction in the isolated perfused ear of the rabbit. Degradation of BK by ACE was calculated to be 52% in the rat uterus and 75% in the rabbit perfused ear.
1 The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Captopril was employed as a specific inhibitor of ACE. 2 Captopril augmented the BK‐induced contractions of the rat isolated uterus, the BK‐ and substance P‐induced contractions of the guinea‐pig ileum, and the BK‐induced venoconstriction in the isolated perfused ear of the rabbit. Degradation of BK by ACE was calculated to be 52% in the rat uterus and 75% in the rabbit perfused ear. 3 Captopril inhibited the A I‐induced contractions of the rat isolated colon, the A I‐induced vasoconstriction in the isolated perfused ear of the rabbit and the rise in blood pressure induced by i.a. injections of A I in pithed rats. Conversion of A I to A II was calculated to be 13% in the rat colon and 26% in the rabbit perfused ear. 4 From estimations of the A II activity (bioassay on the rat colon) in the effluent of the perfused ear of the rabbit after injections of A I into the arterial inflow cannula it was calculated that approximately one tenth of A I was converted to A II during a single passage through the ear (less than 15 s). 5 The present experiments suggest that the high activity of ACE in endothelium of blood vessels of extrapulmonary tissues may provide an additional (endothelium‐dependent) local vasoconstrictor mechanism by the rapid formation of A II and inactivation of BK. The ACE activity in non‐vascular smooth muscles, other than those of blood vessels, may also affect the physiological functions of these tissues.
The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The conversion of angiotensin I (A I) to angiotensin II (A II) and the cleavage of bradykinin (BK) were used as indicators of ACE activity. Captopril was employed as a specific inhibitor of ACE. Captopril augmented the BK‐induced contractions of the rat isolated uterus, the BK‐ and substance P‐induced contractions of the guinea‐pig ileum, and the BK‐induced venoconstriction in the isolated perfused ear of the rabbit. Degradation of BK by ACE was calculated to be 52% in the rat uterus and 75% in the rabbit perfused ear. Captopril inhibited the A I‐induced contractions of the rat isolated colon, the A I‐induced vasoconstriction in the isolated perfused ear of the rabbit and the rise in blood pressure induced by i.a. injections of A I in pithed rats. Conversion of A I to A II was calculated to be 13% in the rat colon and 26% in the rabbit perfused ear. From estimations of the A II activity (bioassay on the rat colon) in the effluent of the perfused ear of the rabbit after injections of A I into the arterial inflow cannula it was calculated that approximately one tenth of A I was converted to A II during a single passage through the ear (less than 15 s). The present experiments suggest that the high activity of ACE in endothelium of blood vessels of extrapulmonary tissues may provide an additional (endothelium‐dependent) local vasoconstrictor mechanism by the rapid formation of A II and inactivation of BK. The ACE activity in non‐vascular smooth muscles, other than those of blood vessels, may also affect the physiological functions of these tissues.
Author Griesbacher, T.
Lembeck, F.
Eckhardt, M.
AuthorAffiliation Department of Experimental and Clinical Pharmacology, University of Graz, Austria
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Cites_doi 10.1161/01.RES.26.5.591
10.1016/0005-2744(71)90142-2
10.1097/00004872-198707002-00013
10.1152/ajplegacy.1962.203.2.261
10.1111/j.1476-5381.1964.tb01591.x
10.1016/0024-3205(68)90086-6
10.1007/BF00173408
10.1111/j.2042-7158.1980.tb12833.x
10.1111/j.1476-5381.1986.tb10178.x
10.1161/01.HYP.6.2.216
10.1001/archderm.1980.01640320052013
10.3181/00379727-64-15828
10.1126/science.175444
10.1016/S0196-9781(81)80027-7
10.1139/y81-022
10.1016/0006-2952(80)90603-6
10.1016/0024-3205(82)90641-5
10.1111/j.1476-5381.1989.tb11850.x
10.1111/j.1476-5381.1989.tb12599.x
10.1007/BF00581069
10.1007/BF00169123
10.1016/0196-9781(84)90020-2
10.1016/0014-2999(84)90225-5
10.1111/j.1476-5381.1967.tb02148.x
10.1007/BF01897474
10.1038/218144a0
10.1097/00004872-198812040-00004
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Issue 1
Keywords Gut
Enzyme inhibitor
Smooth muscle
Muscle contraction
In vitro
Biological activity
Endothelium
Uterus
Animal
Blood vessel
Angiotensin converting enzyme
Blood pressure
Mechanism of action
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References 1968; 7
1962; 203
1974; 37
1980; 116
1965; 148
1983; 398
1980; 29
1986; 332
1984; 100
1982; 30
1987; 5
1981; 2
1947; 64
1964; 23
1976; 191
1968; 218
1989; 96
1976; 198
1989; 98
1986; 87
1987; 335
1988; 6
1984; 6
1967; 30
1980; 32
1984; 5
1969; 25
1981; 59
1984
1981
1980
1971; 250
1988; 338
1970; 26
GEIGY (e_1_2_1_6_1) 1980
e_1_2_1_20_1
e_1_2_1_23_1
CARRETERO O.A. (e_1_2_1_3_1) 1981
e_1_2_1_21_1
e_1_2_1_22_1
e_1_2_1_27_1
e_1_2_1_28_1
e_1_2_1_25_1
e_1_2_1_26_1
e_1_2_1_29_1
WILKIN J.K. (e_1_2_1_34_1) 1980; 116
e_1_2_1_31_1
e_1_2_1_8_1
e_1_2_1_5_1
McCARTHY D.A. (e_1_2_1_13_1) 1965; 148
SCHÖLKENS B.A. (e_1_2_1_24_1) 1986; 332
e_1_2_1_12_1
e_1_2_1_4_1
e_1_2_1_10_1
e_1_2_1_33_1
e_1_2_1_2_1
e_1_2_1_11_1
e_1_2_1_32_1
e_1_2_1_16_1
e_1_2_1_17_1
e_1_2_1_14_1
e_1_2_1_15_1
GOLDBERG M.R. (e_1_2_1_7_1) 1976; 198
VANE J.R. (e_1_2_1_30_1) 1974
ZAR J.A. (e_1_2_1_35_1) 1984
e_1_2_1_9_1
e_1_2_1_18_1
e_1_2_1_19_1
References_xml – volume: 398
  start-page: 175
  year: 1983
  end-page: 177
  article-title: The effect of kininase II inhibitors on the response of feline cerebral arteries to bradykinin and angiotensin
  publication-title: Pflügers Arch. (Eur. J. Physiol.)
– volume: 250
  start-page: 261
  year: 1971
  end-page: 265
  article-title: Concentrations of angiotensin‐converting enzyme in tissues of the rat
  publication-title: Biochim. Biophys. Acta
– volume: 2
  start-page: 145
  year: 1981
  end-page: 152
  article-title: Purification and characterization of human converting enzyme (kininase II)
  publication-title: Peptides
– volume: 332
  start-page: R60
  issue: Suppl.
  year: 1986
  article-title: Inhibition of converting enzyme in isolated arterial preparations with intact or disrupted endothelium
  publication-title: Naunyn-Schmiedebergs Arch. Pharmacol.
– volume: 96
  start-page: 531
  year: 1989
  end-page: 538
  article-title: Effects of the bradykinin antagonist B4310 on smooth muscles and blood pressure in the rat, and its enzymatic degradation
  publication-title: Br. J. Pharmacol.
– start-page: 105
  year: 1981
  end-page: 121
– volume: 218
  start-page: 144
  year: 1968
  end-page: 150
  article-title: Fate of angiotensin I in the circulation
  publication-title: Nature
– volume: 203
  start-page: 261
  year: 1962
  end-page: 265
  article-title: Bradykinin and cardiovascular system: estimation of half‐life
  publication-title: Am. J. Physiol.
– volume: 59
  start-page: 131
  year: 1981
  end-page: 138
  article-title: The degradation of bradykinin (Bk) and of des‐Arg ‐Bk in plasma
  publication-title: Can. J. Physiol. Pharmacol.
– volume: 87
  start-page: 249
  year: 1986
  end-page: 255
  article-title: Role of endothelium on the facilitatory effects of angiotensin I and angiotensin II on noradrenergic transmission in the caudal artery of the rat
  publication-title: Br. J. Pharmacol.
– volume: 198
  start-page: 357
  year: 1976
  end-page: 365
  article-title: Influence of prostaglandin synthesis on venoconstrictor responses to bradykinin
  publication-title: J. Pharmacol. Exp. Ther.
– volume: 37
  start-page: 17
  year: 1974
  end-page: 40
– volume: 32
  start-page: 1
  year: 1980
  end-page: 46
  article-title: Pharmacology of bradykinin and related kinins
  publication-title: Pharmacol. Rev.
– volume: 23
  start-page: 351
  year: 1964
  end-page: 359
  article-title: A sensitive method for the assay of angiotensin
  publication-title: Br. J. Pharmacol.
– volume: 29
  start-page: 1525
  year: 1980
  end-page: 1529
  article-title: Angiotensin I converting enzyme (kininase II) of brush border of human and swine intestine
  publication-title: Biochem. Pharmacol.
– volume: 148
  start-page: 117
  year: 1965
  end-page: 122
  article-title: An estimation of the potencies and half‐lives of synthetic bradykinin and kallidin
  publication-title: J. Pharmacol. Exp. Ther.
– volume: 30
  start-page: 99
  year: 1982
  end-page: 106
  article-title: Renin synthesis by canine aortic smooth muscle cells in culture
  publication-title: Life Sci.
– volume: 6
  start-page: 216
  year: 1984
  end-page: 222
  article-title: Role of endothelium in conversion of angiotensin I to angiotensin II in rabbit aorta
  publication-title: Hypertension
– volume: 98
  start-page: 333
  year: 1989
  end-page: 335
  article-title: Angiotensin converting enzyme activity is present in the endothelium‐denuded aorta
  publication-title: Br. J. Pharmacol.
– volume: 25
  start-page: 1247
  year: 1969
  article-title: Converting enzyme content of different tissues of the rat
  publication-title: Experientia
– year: 1984
– volume: 191
  start-page: 1050
  year: 1976
  end-page: 1051
  article-title: Angiotensin converting enzyme: vascular endothelial localization
  publication-title: Science
– volume: 6
  start-page: S25
  issue: suppl. 4
  year: 1988
  end-page: S28
  article-title: Effects of the angiotensin converting enzyme inhibitor, ramipril, in isolated ischaemic rat heart are abolished by a bradykinin antagonist
  publication-title: J. Hypertension
– year: 1980
– volume: 338
  start-page: 327
  year: 1988
  end-page: 331
  article-title: Angiotensinogen gene expression in extrahepatic rat tissues: Application of a solution hybridization assay
  publication-title: Naunyn-Schmiedebergs Arch. Pharmacol.
– volume: 335
  start-page: 551
  year: 1987
  end-page: 554
  article-title: Metabolism of bradykinin and angiotensin I by human basilar artery and rabbit aorta
  publication-title: Naunyn-Schmiedebergs Arch. Pharmacol.
– volume: 5
  start-page: 769
  year: 1984
  end-page: 776
  article-title: Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
  publication-title: Peptides
– volume: 64
  start-page: 453
  year: 1947
  end-page: 455
  article-title: A pithed rat preparation suitable for assaying pressor substances
  publication-title: Proc. Soc. Exp. Biol. Med.
– volume: 30
  start-page: 417
  year: 1967
  end-page: 424
  article-title: The disappearance of bradykinin and eledoisin in the circulation and vascular beds of the cat
  publication-title: Br. J. Pharmacol. Chemother.
– volume: 100
  start-page: 211
  year: 1984
  end-page: 217
  article-title: Intima‐related vasodilatation of the perfused rat caudal artery
  publication-title: Eur. J. Pharmacol.
– volume: 116
  start-page: 902
  year: 1980
  end-page: 905
  article-title: The captopril‐induced eruption. A possible mechanism: cutaneous kinin potentiation
  publication-title: Arch. Dermatol.
– volume: 7
  start-page: 633
  year: 1968
  end-page: 639
  article-title: A simple method for the determination of angiotensin I converting enzyme
  publication-title: Life Sci.
– volume: 26
  start-page: 591
  year: 1970
  end-page: 599
  article-title: and conversion of angiotensin I to angiotensin II in dog blood
  publication-title: Circ. Res.
– volume: 5
  start-page: S71
  issue: suppl. 2
  year: 1987
  end-page: S76
  article-title: Effects of teprotide, captopril and enalaprilat on arterial wall kininase and angiotensin converting activity
  publication-title: J. Hypertension
– ident: e_1_2_1_15_1
  doi: 10.1161/01.RES.26.5.591
– ident: e_1_2_1_4_1
  doi: 10.1016/0005-2744(71)90142-2
– ident: e_1_2_1_11_1
  doi: 10.1097/00004872-198707002-00013
– ident: e_1_2_1_21_1
  doi: 10.1152/ajplegacy.1962.203.2.261
– ident: e_1_2_1_19_1
  doi: 10.1111/j.1476-5381.1964.tb01591.x
– ident: e_1_2_1_10_1
  doi: 10.1016/0024-3205(68)90086-6
– ident: e_1_2_1_9_1
  doi: 10.1007/BF00173408
– ident: e_1_2_1_18_1
  doi: 10.1111/j.2042-7158.1980.tb12833.x
– ident: e_1_2_1_29_1
  doi: 10.1111/j.1476-5381.1986.tb10178.x
– start-page: 105
  volume-title: Angiotensin Converting Enzyme Inhibitors. Mechanism of Action and Clinical Applications
  year: 1981
  ident: e_1_2_1_3_1
  contributor:
    fullname: CARRETERO O.A.
– ident: e_1_2_1_22_1
  doi: 10.1161/01.HYP.6.2.216
– volume: 116
  start-page: 902
  year: 1980
  ident: e_1_2_1_34_1
  article-title: The captopril‐induced eruption. A possible mechanism: cutaneous kinin potentiation
  publication-title: Arch. Dermatol.
  doi: 10.1001/archderm.1980.01640320052013
  contributor:
    fullname: WILKIN J.K.
– ident: e_1_2_1_25_1
  doi: 10.3181/00379727-64-15828
– ident: e_1_2_1_2_1
  doi: 10.1126/science.175444
– ident: e_1_2_1_28_1
  doi: 10.1016/S0196-9781(81)80027-7
– volume: 198
  start-page: 357
  year: 1976
  ident: e_1_2_1_7_1
  article-title: Influence of prostaglandin synthesis on venoconstrictor responses to bradykinin
  publication-title: J. Pharmacol. Exp. Ther.
  contributor:
    fullname: GOLDBERG M.R.
– ident: e_1_2_1_12_1
  doi: 10.1139/y81-022
– start-page: 17
  volume-title: Angiotensin, Handb. Exp. Pharmacol
  year: 1974
  ident: e_1_2_1_30_1
  contributor:
    fullname: VANE J.R.
– ident: e_1_2_1_31_1
  doi: 10.1016/0006-2952(80)90603-6
– ident: e_1_2_1_17_1
  doi: 10.1016/0024-3205(82)90641-5
– ident: e_1_2_1_8_1
  doi: 10.1111/j.1476-5381.1989.tb11850.x
– ident: e_1_2_1_16_1
  doi: 10.1111/j.1476-5381.1989.tb12599.x
– ident: e_1_2_1_33_1
  doi: 10.1007/BF00581069
– volume: 148
  start-page: 117
  year: 1965
  ident: e_1_2_1_13_1
  article-title: An in vivo estimation of the potencies and half‐lives of synthetic bradykinin and kallidin
  publication-title: J. Pharmacol. Exp. Ther.
  contributor:
    fullname: McCARTHY D.A.
– ident: e_1_2_1_32_1
  doi: 10.1007/BF00169123
– volume-title: Biostatistical Analysis
  year: 1984
  ident: e_1_2_1_35_1
  contributor:
    fullname: ZAR J.A.
– ident: e_1_2_1_26_1
  doi: 10.1016/0196-9781(84)90020-2
– ident: e_1_2_1_27_1
  doi: 10.1016/0014-2999(84)90225-5
– ident: e_1_2_1_5_1
  doi: 10.1111/j.1476-5381.1967.tb02148.x
– ident: e_1_2_1_20_1
  doi: 10.1007/BF01897474
– volume-title: Scientific Tables Geigy (Statistics)
  year: 1980
  ident: e_1_2_1_6_1
  contributor:
    fullname: GEIGY
– ident: e_1_2_1_14_1
  doi: 10.1038/218144a0
– volume: 332
  start-page: R60
  year: 1986
  ident: e_1_2_1_24_1
  article-title: Inhibition of converting enzyme in isolated arterial preparations with intact or disrupted endothelium
  publication-title: Naunyn-Schmiedebergs Arch. Pharmacol.
  contributor:
    fullname: SCHÖLKENS B.A.
– ident: e_1_2_1_23_1
  doi: 10.1097/00004872-198812040-00004
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Snippet 1 The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The...
1. The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The...
The activity of angiotensin converting enzyme (ACE) has been studied on functional parameters of intact isolated preparations of extrapulmonary tissues. The...
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SubjectTerms Angiotensin II - metabolism
Angiotensin-Converting Enzyme Inhibitors - pharmacology
Animals
Antihypertensive agents
Biological and medical sciences
Blood Pressure - drug effects
Bradykinin - physiology
Captopril - pharmacology
Cardiovascular system
Endothelium, Vascular - drug effects
Endothelium, Vascular - physiology
Female
Guinea Pigs
Ileum - drug effects
In Vitro Techniques
Lung - metabolism
Male
Medical sciences
Muscle, Smooth - enzymology
Muscle, Smooth, Vascular - enzymology
Norepinephrine - pharmacology
Peptidyl-Dipeptidase A - metabolism
Pharmacology. Drug treatments
Rabbits
Rats
Rats, Inbred Strains
Uterine Contraction - drug effects
Vasoconstriction - drug effects
Title Demonstration of extrapulmonary activity of angiotensin converting enzyme in intact tissue preparations
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1476-5381.1990.tb12050.x
https://www.ncbi.nlm.nih.gov/pubmed/2164861
https://search.proquest.com/docview/15626432
https://search.proquest.com/docview/79889888
https://pubmed.ncbi.nlm.nih.gov/PMC1917461
Volume 100
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