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Mass-spectrometric identification of a novel angiotensin peptide in human plasma

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Mass-spectrometric identification of a novel angiotensin peptide in human plasma. / Jankowski, Vera; Vanholder, Raymond; van der Giet, Markus; Tölle, Markus; Karadogan, Sevil; Gobom, Johan; Furkert, Jens; Oksche, Alexander; Krause, Eberhard; Tran, Thi Nguyet Anh; Tepel, Martin; Schuchardt, Mirjam; Schlüter, Hartmut; Wiedon, Annette; Beyermann, Michael; Bader, Michael; Todiras, Mihail; Zidek, Walter; Jankowski, Joachim.

In: ARTERIOSCL THROM VAS, Vol. 27, No. 2, 02.2007, p. 297-302.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Jankowski, V, Vanholder, R, van der Giet, M, Tölle, M, Karadogan, S, Gobom, J, Furkert, J, Oksche, A, Krause, E, Tran, TNA, Tepel, M, Schuchardt, M, Schlüter, H, Wiedon, A, Beyermann, M, Bader, M, Todiras, M, Zidek, W & Jankowski, J 2007, 'Mass-spectrometric identification of a novel angiotensin peptide in human plasma', ARTERIOSCL THROM VAS, vol. 27, no. 2, pp. 297-302. https://doi.org/10.1161/01.ATV.0000253889.09765.5f

APA

Jankowski, V., Vanholder, R., van der Giet, M., Tölle, M., Karadogan, S., Gobom, J., Furkert, J., Oksche, A., Krause, E., Tran, T. N. A., Tepel, M., Schuchardt, M., Schlüter, H., Wiedon, A., Beyermann, M., Bader, M., Todiras, M., Zidek, W., & Jankowski, J. (2007). Mass-spectrometric identification of a novel angiotensin peptide in human plasma. ARTERIOSCL THROM VAS, 27(2), 297-302. https://doi.org/10.1161/01.ATV.0000253889.09765.5f

Vancouver

Jankowski V, Vanholder R, van der Giet M, Tölle M, Karadogan S, Gobom J et al. Mass-spectrometric identification of a novel angiotensin peptide in human plasma. ARTERIOSCL THROM VAS. 2007 Feb;27(2):297-302. https://doi.org/10.1161/01.ATV.0000253889.09765.5f

Bibtex

@article{a24a5a13c02d4f58ae1549b0e15ae7a8,
title = "Mass-spectrometric identification of a novel angiotensin peptide in human plasma",
abstract = "OBJECTIVE: Angiotensin peptides play a central role in cardiovascular physiology and pathology. Among these peptides, angiotensin II (Ang II) has been investigated most intensively. However, further angiotensin peptides such as Ang 1-7, Ang III, and Ang IV also contribute to vascular regulation, and may elicit additional, different, or even opposite effects to Ang II. Here, we describe a novel Ang II-related, strong vasoconstrictive substance in plasma from healthy humans and end-stage renal failure patients.METHODS AND RESULTS: Chromatographic purification and structural analysis by matrix-assisted laser desorption/ionisation time-of-flight/time-of-flight (MALDI-TOF/TOF) revealed an angiotensin octapeptide with the sequence Ala-Arg-Val-Tyr-Ile-His-Pro-Phe, which differs from Ang II in Ala1 instead of Asp1. Des[Asp1]-[Ala1]-Ang II, in the following named Angiotensin A (Ang A), is most likely generated enzymatically. In the presence of mononuclear leukocytes, Ang II is converted to Ang A by decarboxylation of Asp1. Ang A has the same affinity to the AT1 receptor as Ang II, but a higher affinity to the AT2 receptor. In the isolated perfused rat kidney, Ang A revealed a smaller vasoconstrictive effect than Ang II, which was not modified in the presence of the AT2 receptor antagonist PD 123319, suggesting a lower intrinsic activity at the AT1 receptor. Ang II and Ang A concentrations in plasma of healthy subjects and end-stage renal failure patients were determined by matrix-assisted laser desorption/ionisation mass-analysis, because conventional enzyme immunoassay for Ang II quantification did not distinguish between Ang II and Ang A. In healthy subjects, Ang A concentrations were less than 20% of the Ang II concentrations, but the ratio Ang A/Ang II was higher in end-stage renal failure patients.CONCLUSIONS: Ang A is a novel human strong vasoconstrictive angiotensin-derived peptide, most likely generated by enzymatic transformation through mononuclear leukocyte-derived aspartate decarboxylase. Plasma Ang A concentration is increased in end-stage renal failure. Because of its stronger agonism at the AT2 receptor, Ang A may modulate the harmful effects of Ang II.",
keywords = "Aged, Angiotensin II, Angiotensins, Animals, Cardiovascular Physiological Phenomena, Cardiovascular System, Cell Line, Cells, Cultured, Female, Humans, Kidney Failure, Chronic, Male, Mass Spectrometry, Mice, Mice, Knockout, Middle Aged, Rats, Receptor, Angiotensin, Type 2, Vasoconstriction, Journal Article",
author = "Vera Jankowski and Raymond Vanholder and {van der Giet}, Markus and Markus T{\"o}lle and Sevil Karadogan and Johan Gobom and Jens Furkert and Alexander Oksche and Eberhard Krause and Tran, {Thi Nguyet Anh} and Martin Tepel and Mirjam Schuchardt and Hartmut Schl{\"u}ter and Annette Wiedon and Michael Beyermann and Michael Bader and Mihail Todiras and Walter Zidek and Joachim Jankowski",
year = "2007",
month = feb,
doi = "10.1161/01.ATV.0000253889.09765.5f",
language = "English",
volume = "27",
pages = "297--302",
journal = "ARTERIOSCL THROM VAS",
issn = "1079-5642",
publisher = "Lippincott Williams and Wilkins",
number = "2",

}

RIS

TY - JOUR

T1 - Mass-spectrometric identification of a novel angiotensin peptide in human plasma

AU - Jankowski, Vera

AU - Vanholder, Raymond

AU - van der Giet, Markus

AU - Tölle, Markus

AU - Karadogan, Sevil

AU - Gobom, Johan

AU - Furkert, Jens

AU - Oksche, Alexander

AU - Krause, Eberhard

AU - Tran, Thi Nguyet Anh

AU - Tepel, Martin

AU - Schuchardt, Mirjam

AU - Schlüter, Hartmut

AU - Wiedon, Annette

AU - Beyermann, Michael

AU - Bader, Michael

AU - Todiras, Mihail

AU - Zidek, Walter

AU - Jankowski, Joachim

PY - 2007/2

Y1 - 2007/2

N2 - OBJECTIVE: Angiotensin peptides play a central role in cardiovascular physiology and pathology. Among these peptides, angiotensin II (Ang II) has been investigated most intensively. However, further angiotensin peptides such as Ang 1-7, Ang III, and Ang IV also contribute to vascular regulation, and may elicit additional, different, or even opposite effects to Ang II. Here, we describe a novel Ang II-related, strong vasoconstrictive substance in plasma from healthy humans and end-stage renal failure patients.METHODS AND RESULTS: Chromatographic purification and structural analysis by matrix-assisted laser desorption/ionisation time-of-flight/time-of-flight (MALDI-TOF/TOF) revealed an angiotensin octapeptide with the sequence Ala-Arg-Val-Tyr-Ile-His-Pro-Phe, which differs from Ang II in Ala1 instead of Asp1. Des[Asp1]-[Ala1]-Ang II, in the following named Angiotensin A (Ang A), is most likely generated enzymatically. In the presence of mononuclear leukocytes, Ang II is converted to Ang A by decarboxylation of Asp1. Ang A has the same affinity to the AT1 receptor as Ang II, but a higher affinity to the AT2 receptor. In the isolated perfused rat kidney, Ang A revealed a smaller vasoconstrictive effect than Ang II, which was not modified in the presence of the AT2 receptor antagonist PD 123319, suggesting a lower intrinsic activity at the AT1 receptor. Ang II and Ang A concentrations in plasma of healthy subjects and end-stage renal failure patients were determined by matrix-assisted laser desorption/ionisation mass-analysis, because conventional enzyme immunoassay for Ang II quantification did not distinguish between Ang II and Ang A. In healthy subjects, Ang A concentrations were less than 20% of the Ang II concentrations, but the ratio Ang A/Ang II was higher in end-stage renal failure patients.CONCLUSIONS: Ang A is a novel human strong vasoconstrictive angiotensin-derived peptide, most likely generated by enzymatic transformation through mononuclear leukocyte-derived aspartate decarboxylase. Plasma Ang A concentration is increased in end-stage renal failure. Because of its stronger agonism at the AT2 receptor, Ang A may modulate the harmful effects of Ang II.

AB - OBJECTIVE: Angiotensin peptides play a central role in cardiovascular physiology and pathology. Among these peptides, angiotensin II (Ang II) has been investigated most intensively. However, further angiotensin peptides such as Ang 1-7, Ang III, and Ang IV also contribute to vascular regulation, and may elicit additional, different, or even opposite effects to Ang II. Here, we describe a novel Ang II-related, strong vasoconstrictive substance in plasma from healthy humans and end-stage renal failure patients.METHODS AND RESULTS: Chromatographic purification and structural analysis by matrix-assisted laser desorption/ionisation time-of-flight/time-of-flight (MALDI-TOF/TOF) revealed an angiotensin octapeptide with the sequence Ala-Arg-Val-Tyr-Ile-His-Pro-Phe, which differs from Ang II in Ala1 instead of Asp1. Des[Asp1]-[Ala1]-Ang II, in the following named Angiotensin A (Ang A), is most likely generated enzymatically. In the presence of mononuclear leukocytes, Ang II is converted to Ang A by decarboxylation of Asp1. Ang A has the same affinity to the AT1 receptor as Ang II, but a higher affinity to the AT2 receptor. In the isolated perfused rat kidney, Ang A revealed a smaller vasoconstrictive effect than Ang II, which was not modified in the presence of the AT2 receptor antagonist PD 123319, suggesting a lower intrinsic activity at the AT1 receptor. Ang II and Ang A concentrations in plasma of healthy subjects and end-stage renal failure patients were determined by matrix-assisted laser desorption/ionisation mass-analysis, because conventional enzyme immunoassay for Ang II quantification did not distinguish between Ang II and Ang A. In healthy subjects, Ang A concentrations were less than 20% of the Ang II concentrations, but the ratio Ang A/Ang II was higher in end-stage renal failure patients.CONCLUSIONS: Ang A is a novel human strong vasoconstrictive angiotensin-derived peptide, most likely generated by enzymatic transformation through mononuclear leukocyte-derived aspartate decarboxylase. Plasma Ang A concentration is increased in end-stage renal failure. Because of its stronger agonism at the AT2 receptor, Ang A may modulate the harmful effects of Ang II.

KW - Aged

KW - Angiotensin II

KW - Angiotensins

KW - Animals

KW - Cardiovascular Physiological Phenomena

KW - Cardiovascular System

KW - Cell Line

KW - Cells, Cultured

KW - Female

KW - Humans

KW - Kidney Failure, Chronic

KW - Male

KW - Mass Spectrometry

KW - Mice

KW - Mice, Knockout

KW - Middle Aged

KW - Rats

KW - Receptor, Angiotensin, Type 2

KW - Vasoconstriction

KW - Journal Article

U2 - 10.1161/01.ATV.0000253889.09765.5f

DO - 10.1161/01.ATV.0000253889.09765.5f

M3 - SCORING: Journal article

C2 - 17138938

VL - 27

SP - 297

EP - 302

JO - ARTERIOSCL THROM VAS

JF - ARTERIOSCL THROM VAS

SN - 1079-5642

IS - 2

ER -