scholarly journals Inhibition of neointima formation in an organ culture of human saphenous vein: A comparison of dual endothelin-converting enzyme/neutral endopeptidase and selective neutral endopeptidase inhibition

2001 ◽  
Vol 34 (3) ◽  
pp. 548-554 ◽  
Author(s):  
Karen E. Porter ◽  
Timothy Dickinson ◽  
Nicholas J.M. London
Keyword(s):  
Organ Culture ◽  
Saphenous Vein ◽  
Neutral Endopeptidase ◽  
Neointima Formation ◽  
Converting Enzyme ◽  
Human Saphenous Vein ◽  
Endothelin Converting Enzyme

Nature and origin of the neointima in whole vessel wall organ culture of the human saphenous vein

1996 ◽  
Vol 428 (1) ◽  
pp. 59-67 ◽  
Author(s):  
J. Slomp ◽  
A. C. Gittenberger-de Groot ◽  
J. C. van Munsteren ◽  
R. E. Poelmann ◽  
H. A. Huysmans ◽  
...  
Keyword(s):  
Organ Culture ◽  
Saphenous Vein ◽  
Vessel Wall ◽  
Human Saphenous Vein

Differential expression of neutral endopeptidase-24.11 (neprilysin) and endothelin-converting enzyme in human prostate cancer cell lines

2002 ◽  
Vol 103 (s2002) ◽  
pp. 314S-317S ◽  
Author(s):  
Badar A. USMANI ◽  
Ben HARDEN ◽  
Norman J. MAITLAND ◽  
Anthony J. TURNER
Keyword(s):  
Prostate Cancer ◽  
Epithelial Cells ◽  
Cell Lines ◽  
Prostate Cancer Cell ◽  
Neutral Endopeptidase ◽  
Prostatic Hyperplasia ◽  
Converting Enzyme ◽  
Prostate Cancer Cell Lines ◽  
Endothelin Converting Enzyme ◽  
Androgen Independent

Neutral endopeptidase-24.11 (neprilysin; NEP/CD10) is a cell surface metallopeptidase expressed by prostatic epithelial cells that degrades various bioactive peptides including endothelin. Endothelin-converting enzyme (ECE), the key enzyme of endothelin biosynthesis, catalyses the final processing step in the pathway. Neuropeptide substrates of NEP, including endothelin, have been implicated in the growth of androgen-independent prostate cancer. We have surveyed the expression of NEP and ECE in a range of prostate cancer cell lines. Western analysis reveals that ECE-1 is expressed abundantly in all the malignant cell lines tested, except for LNCaP. In contrast, LNCaP cells express high levels of NEP, while NEP was not detected in PC-3, DU145 and other metastatic cell lines that were tested. Of the normal immortalized prostate epithelial cell lines, PNT1a shows equivalent amounts of NEP and ECE. PNT2-C2 shows poor NEP expression but an abundance of ECE. P4E6, by comparison, has low levels of both ECE and NEP. These differences in expression may render these cell lines useful in experimental models for future study. Benign prostatic hyperplasia primary epithelial cells express much higher levels of NEP than malignant primary epithelial cells, but neither show ECE expression. On the other hand, surrounding stromal cell populations have detectable ECE levels. An absence of ECE in malignant and benign prostatic hyperplasia cells of primary epithelial origin suggests an important role for stromal interaction and paracrine production of ECE within the host. The upregulation of ECE expression in metastatic cells in culture may be indicative of its role in metastatic progression. A differential profile of ECE and NEP could contribute to an abundance of mitogenic peptides aiding the progression of androgen-independent prostate cancer.

Comparison of response to injury in organ culture of human saphenous vein and internal mammary artery

1993 ◽  
Vol 55 (6) ◽  
pp. 1522-1528 ◽  
Author(s):  
Cathy M. Holt ◽  
Sheila E. Francis ◽  
Andrew C. Newby ◽  
Suzanne Rogers ◽  
Patricia A. Gadsdon ◽  
...  
Keyword(s):  
Organ Culture ◽  
Saphenous Vein ◽  
Internal Mammary Artery ◽  
Human Saphenous Vein ◽  
Internal Mammary

Role of endothelin-converting enzyme, chymase and neutral endopeptidase in the processing of big ET-1, ET-1(1-21) and ET-1(1-31) in the trachea of allergic mice

2002 ◽  
Vol 103 (s2002) ◽  
pp. 353S-356S ◽  
Author(s):  
Benjamin A. DE CAMPO ◽  
Roy G. GOLDIE ◽  
Arco Y. JENG ◽  
Peter J. HENRY
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Response Curve ◽  
Histological Analysis ◽  
Neutral Endopeptidase ◽  
Converting Enzyme ◽  
Rightward Shift ◽  
Endothelin Converting Enzyme ◽  
Mast Cell Chymase

The present study examined the roles of endothelin-converting enzyme (ECE), neutral endopeptidase (NEP) and mast cell chymase as processors of the endothelin (ET) analogues ET-1(1–21), ET-1(1–31) and big ET-1 in the trachea of allergic mice. Male CBA/CaH mice were sensitized with ovalbumin (10µg) delivered intraperitoneal on days 1 and 14, and exposed to aerosolized ovalbumin on days 14, 25, 26 and 27 (OVA mice). Mice were killed and the trachea excised for histological analysis and contraction studies on day 28. Tracheae from OVA mice had 40% more mast cells than vehicle-sensitized mice (sham mice). Ovalbumin (10µg/ml) induced transient contractions (15±3% of the Cmax) in tracheae from OVA mice. The ECE inhibitor CGS35066 (10µM) inhibited contractions induced by big ET-1 (4.8-fold rightward shift of dose-response curve; P<0.05), but not those induced by either ET-1(1–21) or ET-1(1–31). The chymase inhibitors chymostatin (10µM) and Bowman-Birk inhibitor (10µM) had no effect on contractions induced by any of the ET analogues used. The NEP inhibitor CGS24592 (10µM) inhibited contractions induced by ET-1(1–31) (6.2-fold rightward shift; P<0.05) but not ET-1(1–21) or big ET-1. These data suggest that big ET-1 is processed predominantly by a CGS35066-sensitive ECE within allergic airways rather than by mast cell-derived proteases such as chymase. If endogenous ET-1(1–31) is formed within allergic airways, it is likely to undergo further conversion by NEP to more active products.

Potent non-peptidic dual inhibitors of endothelin-converting enzyme and neutral endopeptidase 24.11

1997 ◽  
Vol 7 (8) ◽  
pp. 1059-1064 ◽  
Author(s):  
Stéphane De Lombaert ◽  
Lisa B. Stamford ◽  
Louis Blanchard ◽  
Jenny Tan ◽  
Denton Hoyer ◽  
...  
Keyword(s):  
Neutral Endopeptidase ◽  
Converting Enzyme ◽  
Endopeptidase 24.11 ◽  
Endothelin Converting Enzyme ◽  
Dual Inhibitors
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