ArticleProceedings of the National Academy of Sciences of the United States of America1998
The distal ectodomain of angiotensin-converting enzyme regulates its cleavage-secretion from the cell surface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 61 citations in OpenAlex.
- The serum angiotensin-converting enzyme and angiotensin II response to altered posture and acute exercise, and the influence of ACE genotype.European journal of applied physiology · 2004Trial
- Naturally occurring ACE2 stalk variants are differentially released from the cell.bioRxiv : the preprint server for biology · 2026Article
- Green Synthetic Approach for Synthesis of Fluorescent Carbon Dots for Lisinopril Drug Delivery System and their Confirmations in the Cells.Journal of fluorescence · 2017Article
- Kinetic and structural characterization of amyloid-β peptide hydrolysis by human angiotensin-1-converting enzyme.The FEBS journal · 2016Article
- Article
- A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme.Pharmacological reviews · 2013Review
- Glycoprotein nonmetastatic melanoma protein b, a melanocytic cell marker, is a melanosome-specific and proteolytically released protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
- The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
- Ectodomain shedding of angiotensin converting enzyme 2 in human airway epithelia.American journal of physiology. Lung cellular and molecular physiology · 2009Article
- A small region in the angiotensin-converting enzyme distal ectodomain is required for cleavage-secretion of the protein at the plasma membrane.Biochemistry · 2008Article
- The influence of mouse Ped gene expression on postnatal development.The Journal of physiology · 2006Article
- The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity.The Biochemical journal · 2005Article
- Epitope-specific antibody-induced cleavage of angiotensin-converting enzyme from the cell surface.The Biochemical journal · 2002Article
- Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding.The Biochemical journal · 2001Article
- Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites.The Biochemical journal · 2000Article
- Selective restoration of male fertility in mice lacking angiotensin-converting enzymes by sperm-specific expression of the testicular isozyme.The Journal of clinical investigation · 1998Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Angiotensin-converting enzyme (ACE) is a type I ectoprotein that is cleaved off the cell surface by a plasma membrane-bound metalloprotease. However, CD4, another type I ectoprotein does not undergo such cleavage-secretion. In this study, we investigated the structural determinants of the ACE protein that regulate the cleavage-secretion process. Substitution and deletion mutations revealed that the cytoplasmic domain, the transmembrane domain, and the juxtamembrane region encompassing the major and the minor cleavage sites of ACE do not regulate its cleavage. Moreover, a chimeric protein containing the distal extracellular domain of CD4 and the juxtamembrane, transmembrane, and the cytoplasmic domains of ACE, although transported to the cell surface, was not cleavage-secreted. In contrast, the distal extracellular domain of ACE was shown to be the important determinant: a protein containing the distal extracellular domain of ACE and the juxtamembrane, transmembrane, and cytoplasmic domain of CD4 was efficiently cleaved off the cell surface. The chimeric protein was cleaved within the CD4 sequence and the responsible enzymatic activity was inhibited by Compound 3, a relatively specific inhibitor of the ACE secretase activity. These results demonstrate that, in a chimeric protein, the distal extracellular domain of a cleavable protein, such as ACE, can induce a proteolytic cleavage within the juxtamembrane domain of an uncleaved protein such as CD4.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.