Reninlike enzymes in human vasculature.

J, Rosenthal; Thurnreiter, M; Plaschke, M.; Geyer, M.A.; Reiter, W; Dahlheim, H.

doi:10.1161/01.hyp.15.6.848

Cited by 19 publications

(11 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cathepsin G and chymase can convert angiotensin I to angiotensin II [34, 35, 36, 37, 38, 39, 40, 41]. Converting enzyme inhibitors do not inhibit these enzymes.…”

Section: Proximal Tubule Renin-angiotensin Systemmentioning

confidence: 99%

Regulation of Proximal Tubule Transport by Endogenously Produced Angiotensin II

Quan

Baum

2000

Nephron

View full text Add to dashboard Cite

“…Cathepsin G and chymase can convert angiotensin I to angiotensin II [34, 35, 36, 37, 38, 39, 40, 41]. Converting enzyme inhibitors do not inhibit these enzymes.…”

Section: Proximal Tubule Renin-angiotensin Systemmentioning

confidence: 99%

Regulation of Proximal Tubule Transport by Endogenously Produced Angiotensin II

Quan

Baum

2000

Nephron

View full text Add to dashboard Cite

“…[1][2][3][4] The synthesis of renin in blood vessels is still a matter of debate, 1,4 but it is widely recognized that generation of Ang I and Ang II in vivo occurs to some extent in the wall of the blood vessels and heart. 4 -7 The role of the endothelium and endothelium-dependent mediators has been a focus of research in the last decade, 8,9 but its contribution to the local vascular generation of Ang I and Ang II is still controversial.…”

mentioning

confidence: 99%

Renin Uptake by the Endothelium Mediates Vascular Angiotensin Formation

et al. 2001

View full text Add to dashboard Cite

Abstract-We investigated the role of the vascular endothelium in the local production of angiotensin. Angiotensin release from isolated rat hindquarters perfused with an artificial medium was measured by high-performance liquid chromatography and radioimmunoassay. Perfused hindquarters with endothelium released angiotensin I spontaneously, indicating ongoing renin-angiotensinogen reaction. Endothelium denudation (by a detergent, validated by electron microscopy and by the absence of a vasodilator response to acetylcholine) reduced angiotensin I release by Ͼ90%, whereas bilateral nephrectomy 24 hours before perfusion abolished the release completely. Infusion of renin into perfused hindquarters induced sustained local angiotensin I release in the presence of an intact endothelium but not after endothelium denudation. The conversion of angiotensin I to angiotensin II was abrogated by endothelium denudation, whereas the disappearance of angiotensin II was unchanged. Endothelium denudation diminished the pressor response to angiotensin II but abolished the response to renin and angiotensin I. Expression of renin messenger RNA, investigated by reverse-transcription polymerase chain reaction using 4 different primer combinations, was not detected in up to 5 g vascular RNA, whereas a renin signal was readily detected with 5 ng kidney RNA.

show abstract

“…[6][7][8] Studies have demonstrated alternative pathways for Ang II formation involving proteinases other than renin and ACE and have been observed in several species, including humans. [9][10][11] In tissues, including blood vessels, brain, heart, and adipose tissue, it is possible to generate Ang II directly from AG, independently of renin and ACE. It has been postulated that chymase, cathepsin G and tonin are part of alternative enzymatic pathways for Ang II production.…”

Section: Introductionmentioning

confidence: 99%

“…[12][13][14] Tonin (rat kallikrein 2, rKLK2) is a serine proteinase present in several rat tissues, such as the brain, kidney, prostate, and mainly in the submandibular gland. [15][16][17][18][19][20] Tonin releases Ang II from peptides presenting the sequence corresponding to the N-terminal portion of AG like Ang I and tetradecapeptide (AG (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)), 13,21,22 the synthetic renin substrate. There is evidence that tonin plays a role in blood pressure control 23 and participates in the local hydromineral balance in several sites.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the renal renin-angiotensin system in transgenic mice that express rat tonin

Ribeiro

Palomino

Lima

et al. 2015

J Renin Angiotensin Aldosterone Syst

View full text Add to dashboard Cite

Introduction: Tonin is an enzyme that is able to generate angiotensin II (Ang II) from angiotensin I (Ang I) or directly from angiotensinogen. Our goal was to characterize the renal renin-angiotensin system in transgenic mice that express rat tonin (TGM`(rTon)). Materials and methods: Mice were euthanized and the kidneys removed for analysis. Tonin activity was evaluated by radioimmunoassay and angiotensin I-converting enzyme (ACE) activity by HPLC. Tonin, ACE and angiotensin II-converting enzyme (ACE2) expression was analyzed by Western blotting. Results: Tonin activity was significantly increased in TGM`(rTon) compared to their respective wild-type (WT) littermates (1.7 ± 0.21 vs 0.11 ± 0.02 nmol of Ang II/min/mg of protein). Tonin activity had a strong positive correlation with tonin expression in both TGM`(rTon) and their respective wild-type littermates. The ACE activity and expression levels of 65-kDa N-domain angiotensin I-converting enzyme isoform were significantly increased in the TGM`(rTon) when compared with WT. ACE2 expression levels were statistically significantly higher in the TGM`(rTon) when compared with WT. Angiotensin 1–7 (Ang(1–7)) and Ang I levels were significantly lower in the TGM`(rTon). Conclusions: We suggest that the environment of tonin abundance may increase N-domain ACE activity liberated by a secretase able to cleave somatic ACE.

show abstract

Reninlike enzymes in human vasculature.

Cited by 19 publications

References 8 publications

Regulation of Proximal Tubule Transport by Endogenously Produced Angiotensin II

Regulation of Proximal Tubule Transport by Endogenously Produced Angiotensin II

Renin Uptake by the Endothelium Mediates Vascular Angiotensin Formation

Characterization of the renal renin-angiotensin system in transgenic mice that express rat tonin

Contact Info

Product

Resources

About