Human endothelial cells selectively express large amounts of secretory (pancreatic-type) ribonuclease

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Human endothelial cells selectively express large amounts of secretory (pancreatic-type) ribonuclease. / Landre, JBP; Hewett, Peter; Olivot, JM; Friedl, P; Ko, Y; Sachinidis, A; Moenner, M.

In: Journal of Cellular Biochemistry, Vol. 86, No. 3, 17.07.2002, p. 540-552.

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Landre, JBP ; Hewett, Peter ; Olivot, JM ; Friedl, P ; Ko, Y ; Sachinidis, A ; Moenner, M. / Human endothelial cells selectively express large amounts of secretory (pancreatic-type) ribonuclease. In: Journal of Cellular Biochemistry. 2002 ; Vol. 86, No. 3. pp. 540-552.

Bibtex

@article{9f794e82925549908de5cc51be02f939,
title = "Human endothelial cells selectively express large amounts of secretory (pancreatic-type) ribonuclease",
abstract = "Pyrimidine-specific ribonucleases are a superfamily of structurally related enzymes with distinct catalytic and biological properties. We used a combination of enzymatic and non-enzymatic assays to investigate the release of such enzymes by isolated cells in serum-free and serum-containing media. We found that human endothelial cells typically expressed large amounts of a pancreatic-type RNase that is related to, if not identical to, human pancreatic RNase. This enzyme exhibits pyrimidine-specific catalytic activity, with a marked preference for poly(C) substrate over poly(U) substrate. It was potently inhibited by placental RNase inhibitor, the selective pancreatic-type RNase inhibitor Inhibit-Ace, and a polyclonal antibody against human pancreatic RNase. The enzyme isolated from medium conditioned by immortalized umbilical vein endothelial cells (EA.hy926) possesses an amino-terminal sequence identical to that of pancreatic RNase, and shows molecular heterogeneity (molecular weights 18,000-26,000) due to different degrees of N-glycosylation. Endothelial cells from arteries, veins, and capillaries secreted up to 100 ng of this RNase daily per million cells, whereas levels were low or undetectable in media conditioned by other cell types examined. The corresponding messenger RNA was detected by RT-PCR in most cell types tested so far, and level of its expression was in keeping with the amounts of protein. The selective strong release of pancreatic-type RNase by endothelial cells suggests that it is endowed with non-digestive functions and involved in vascular homeostasis.",
author = "JBP Landre and Peter Hewett and JM Olivot and P Friedl and Y Ko and A Sachinidis and M Moenner",
year = "2002",
month = jul,
day = "17",
doi = "10.1002/jcb.10234",
language = "English",
volume = "86",
pages = "540--552",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley",
number = "3",

}

RIS

TY - JOUR

T1 - Human endothelial cells selectively express large amounts of secretory (pancreatic-type) ribonuclease

AU - Landre, JBP

AU - Hewett, Peter

AU - Olivot, JM

AU - Friedl, P

AU - Ko, Y

AU - Sachinidis, A

AU - Moenner, M

PY - 2002/7/17

Y1 - 2002/7/17

N2 - Pyrimidine-specific ribonucleases are a superfamily of structurally related enzymes with distinct catalytic and biological properties. We used a combination of enzymatic and non-enzymatic assays to investigate the release of such enzymes by isolated cells in serum-free and serum-containing media. We found that human endothelial cells typically expressed large amounts of a pancreatic-type RNase that is related to, if not identical to, human pancreatic RNase. This enzyme exhibits pyrimidine-specific catalytic activity, with a marked preference for poly(C) substrate over poly(U) substrate. It was potently inhibited by placental RNase inhibitor, the selective pancreatic-type RNase inhibitor Inhibit-Ace, and a polyclonal antibody against human pancreatic RNase. The enzyme isolated from medium conditioned by immortalized umbilical vein endothelial cells (EA.hy926) possesses an amino-terminal sequence identical to that of pancreatic RNase, and shows molecular heterogeneity (molecular weights 18,000-26,000) due to different degrees of N-glycosylation. Endothelial cells from arteries, veins, and capillaries secreted up to 100 ng of this RNase daily per million cells, whereas levels were low or undetectable in media conditioned by other cell types examined. The corresponding messenger RNA was detected by RT-PCR in most cell types tested so far, and level of its expression was in keeping with the amounts of protein. The selective strong release of pancreatic-type RNase by endothelial cells suggests that it is endowed with non-digestive functions and involved in vascular homeostasis.

AB - Pyrimidine-specific ribonucleases are a superfamily of structurally related enzymes with distinct catalytic and biological properties. We used a combination of enzymatic and non-enzymatic assays to investigate the release of such enzymes by isolated cells in serum-free and serum-containing media. We found that human endothelial cells typically expressed large amounts of a pancreatic-type RNase that is related to, if not identical to, human pancreatic RNase. This enzyme exhibits pyrimidine-specific catalytic activity, with a marked preference for poly(C) substrate over poly(U) substrate. It was potently inhibited by placental RNase inhibitor, the selective pancreatic-type RNase inhibitor Inhibit-Ace, and a polyclonal antibody against human pancreatic RNase. The enzyme isolated from medium conditioned by immortalized umbilical vein endothelial cells (EA.hy926) possesses an amino-terminal sequence identical to that of pancreatic RNase, and shows molecular heterogeneity (molecular weights 18,000-26,000) due to different degrees of N-glycosylation. Endothelial cells from arteries, veins, and capillaries secreted up to 100 ng of this RNase daily per million cells, whereas levels were low or undetectable in media conditioned by other cell types examined. The corresponding messenger RNA was detected by RT-PCR in most cell types tested so far, and level of its expression was in keeping with the amounts of protein. The selective strong release of pancreatic-type RNase by endothelial cells suggests that it is endowed with non-digestive functions and involved in vascular homeostasis.

UR - http://www.scopus.com/inward/record.url?scp=0036942183&partnerID=8YFLogxK

U2 - 10.1002/jcb.10234

DO - 10.1002/jcb.10234

M3 - Article

C2 - 12210760

VL - 86

SP - 540

EP - 552

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 3

ER -