Structure, Evolutionary Conservation, and Functions of Angiotensin- and Endothelin-Converting Enzymes

Macours, Nathalie; Poels, Jeroen; Hens, Korneel; Francis, Carmen; Huybrechts, Roger

doi:10.1016/s0074-7696(04)39002-9

Cited by 29 publications

(16 citation statements)

References 207 publications

(202 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The endothelin system, which includes at least three related peptides, at least two endothelin specific receptors and several enzymes involved in peptide processing and activation has been identified in most mammals, as well as several fish, amphibian and invertebrate species (Miller et al, 2000; Zhang et al, 2001; Macours et al, 2004; Masaki. 2004; Quan et al, 2004; Wang et al, 2006) .…”

Section: Introductionmentioning

confidence: 99%

Endothelin-1 production by the canine macrophage cell line DH82: Enhanced production in response to microbial challenge

Divino

Chawla

Silva

et al. 2010

Veterinary Immunology and Immunopathology

View full text Add to dashboard Cite

Endothelin-1 (ET-1) is a potent vasoconstrictive peptide which plays an important role in regulating mammalian cardiovascular development and homeostasis. Originally identified as a factor released by vascular endothelial cells, ET-1 is now recognized as a product of numerous cells and tissues with demonstrated involvement in an array of physiological and pathological processes. An area of great interest is the production of ET-1 by mononuclear cells (monocytes and macrophages) and its role in inflammation. We report that the canine macrophage cell line, DH82, constitutively secretes both ET-1 and its biologically inactive precursor big ET-1. The production of both peptides was increased following stimulation with lipopolysaccharide (endotoxin) from gram-negative bacteria. ET-1 production was also increased in response to stimulation with intact and viable gram-positive and gram-negative bacteria. In addition to producing ET-1, DH82 cells express transcripts encoding two receptors for the ET-1 peptide (ET A and ET B receptors) and an enzyme involved in the conversion of big ET-1 to ET-1. The constitutive secretion of ET-1 and the expression of ET A and ET B receptors may be related to the malignant origin of this cell line. Our results are the first report of ET-1 production by a canine cell line and provide the basis for further investigation into the role of ET-1 during infection and inflammation.

show abstract

Section: Introductionmentioning

confidence: 99%

Endothelin-1 production by the canine macrophage cell line DH82: Enhanced production in response to microbial challenge

Divino

Chawla

Silva

et al. 2010

Veterinary Immunology and Immunopathology

View full text Add to dashboard Cite

show abstract

“…ET-1 is produced as Big Endothelin-1 (Big ET-1) and requires conversion to an active 21 amino acid form. The process of activation is controlled by the metalloproteinase members endothelin converting enzymes (ECEs) [77]. However, MMP-2 has also been described as generating functional ET-1 from Big ET-1, and ET-1 in turn can induce the expression of MMPs such as MMP-2 and MMP-9 [78,79].…”

Section: Et-1mentioning

confidence: 99%

How MMPs Impact Bone Responses to Metastatic Prostate Cancer

Lynch¹

2011

View full text Add to dashboard Cite

Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. (From -To) 1 FEB 200 -JAN 30 2010 REPORT DATE (DD-MM-YYYY) 04/ /2011 REPORT TYPE Final DATES COVERED TITLE AND SUBTITLE How MMPs impact bone responses to metastatic prostate cancer 5a. CONTRACT NUMBERW81XWH-07-1-0208 5b. GRANT NUMBER 5c. PROGRAM ELEMENT NUMBER AUTHOR(S)Conor C Lynch 5d. PROJECT NUMBER 5e. TASK NUMBER 5f. WORK UNIT NUMBER PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES) 8. PERFORMING ORGANIZATION REPORT NUMBER VanderbiltNashville TN, 37232 SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S) U.S. Army Medical Research and Materiel Command Fort Detrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S)12. DISTRIBUTION / AVAILABILITY STATEMENT Approved for public release; distribution unlimited SUPPLEMENTARY NOTES ABSTRACTUsing an animal model of prostate tumor progression in the bone we have previously shown that MMPs, namely MMP-2,-3,-9 and -13, are overexpressed at the tumor bone interface and these MMPs are for the most part expressed by the host cells of the bone. To test the contribution of MMPs in prostate tumor progression in the bone, we have generated mice that are immunocompromized and deficient for MMP-2,-3 and -9 during the current period. We have found that MMP-9 does not contribute to prostate tumor progression in the bone since no difference in osteolytic or osteoblastic responses between wild type and MMP-9 deficient animals were detected by Faxitron, CT, SPECT and histomorphometry. These results, while negative, are important for the generation of selective MMP inhibitors that lack the deleterious side effects associated with broad spectrum inhibitors. In addition, we have also identified PTHrP as an MMP substrate and postulate that MMP processing of PTHrP may be a mechanism through which MMPs can contribute to tumor induced osteolysis. SUBJECT TERMSOsteolysis, osteoblastic changes, prostate progression in bone, matrix metalloproteinases, MMPs, receptor activator of nuclear kappa B ligand, RANKL, bone metastasis. Conclusion…………………………………………………………………………… 13References…………………………………………………………………………….14 Summary and Introduction……………………………………………………...

show abstract

“…The ECE are neutral membrane-bound metalloproteases, a 120 kD endopeptidase-24 family of proteins, which belong to M13 group of proteins that includes neutral endopeptidases, kell blood group antigens (Kell), a peptide from phosphate regulating gene (PEX), X-converting enzyme (XCE), “secreted” endopeptidases, and the ECEs [21] found in brain [22-24]. Three isoforms of ECE have been reported [25], namely ECE-1, ECE-2 and ECE-3; ECE-1 and ECE-2 are most prominent [24].…”

Section: Introductionmentioning

confidence: 99%

“…ECE's. M13 family members contain type II integral membrane proteins with zinc metalloprotease activity [21], and their function is inhibited by phosphoramidon [24]. Four variants of ECE-1 have been reported in humans [26], namely ECE-1a, ECE-1b, ECE-1c and ECE-1d which are a result of alternate splicing of ECE-1 mRNA.…”

Section: Introductionmentioning

confidence: 99%

“…ECE-2 is localized to the trans-Golgi network and is expressed abundantly in neural tissues and endothelial cells. Its optimal activity is at pH 5 [21,28]; the acidic activity marks ECE-2 as an intracellular enzyme [28]. Substrate selectivity experiments indicate that both ECE-1 and ECE-2 show preference for big ET-1 over big ET-2 or big ET-3 [29].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Endothelin and hepatic wound healing

Khimji

Rockey

2011

Pharmacological Research

View full text Add to dashboard Cite

Liver wound healing is a coordinated response to injury caused by infections (hepatitis) or toxins (alcohol) or other processes where activation of hepatic stellate cells are a central component. During stellate cell activation, a major phenotypic transformation occurs which leads to increased production of increased extracellular matrix proteins and smooth muscle α-actin the results is organ dysfunction due to gross architectural disruption and impaired blood flow. Endothelin-1 (ET-1) is produced in increased amounts and the cellular source of ET-1 shifts from endothelial cells to stellate cells during liver injury thus setting a feedback loop which accentuates further activation, stellate cell proliferation, and production of extracellular matrix proteins. Therapy directed at intervening the ET-1 signaling pathway has significant therapeutic potential in patients with liver disease.

show abstract

Structure, Evolutionary Conservation, and Functions of Angiotensin- and Endothelin-Converting Enzymes

Cited by 29 publications

References 207 publications

Endothelin-1 production by the canine macrophage cell line DH82: Enhanced production in response to microbial challenge

Endothelin-1 production by the canine macrophage cell line DH82: Enhanced production in response to microbial challenge

How MMPs Impact Bone Responses to Metastatic Prostate Cancer

Endothelin and hepatic wound healing

Contact Info

Product

Resources

About