1999
DOI: 10.1074/jbc.274.3.1509
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Constitutive Lysosomal Targeting and Degradation of Bovine Endothelin-converting Enzyme-1a Mediated by Novel Signals in Its Alternatively Spliced Cytoplasmic Tail

Abstract: Endothelin-converting enzyme-1 (ECE-1) is a type II membrane protein that catalyzes the proteolytic activation of big endothelin-1 to endothelin-1 (ET-1). The subcellular distribution of ECE-1, and hence the exact site of physiological activation of big ET-1, remains controversial. Here, we demonstrate with several complementary methods that the two alternatively spliced bovine ECE-1 isoforms, ECE-1a and ECE-1b, differing only in the first 30 amino acids of their N-terminal cytoplasmic tails, exhibit strikingl… Show more

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Cited by 47 publications
(46 citation statements)
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“…However, in contrast to human ECE-1a, bovine ECE-1a has convincingly been shown to be constitutively targeted to the lysosome (28). This difference between the localization of human and bovine ECE-1a may be due to the fact that the isoformspecific N-terminal region of ECE-1a is poorly conserved between the species.…”
mentioning
confidence: 92%
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“…However, in contrast to human ECE-1a, bovine ECE-1a has convincingly been shown to be constitutively targeted to the lysosome (28). This difference between the localization of human and bovine ECE-1a may be due to the fact that the isoformspecific N-terminal region of ECE-1a is poorly conserved between the species.…”
mentioning
confidence: 92%
“…Bovine ECE-1b, which corresponds to human ECE-1c, is also localized predominantly on the plasma membrane (28). However, in contrast to human ECE-1a, bovine ECE-1a has convincingly been shown to be constitutively targeted to the lysosome (28).…”
mentioning
confidence: 99%
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“…31 Emoto et al have described that the isoform cleaving big ET-1 is different between endogenously synthesized and exogenously supplied one; the former is mainly catalyzed by isoform expressing intracellular, whereas the latter is cleaved by it expressing on the cell surface. 32 Based on this report, endogenously increased ET-1 in the postischemic heart should be mostly generated inside the cell, whereas exogenously applied big ET-1 may be cleaved at cell surfaces. If this isoform expressing on the cell surface is close to ET B receptors, we can explain why ET-1 produced by exogenous big ET-1 preferentially acts on ET B receptors but not on ET A receptors.…”
Section: Discussionmentioning
confidence: 83%
“…The findings of this study are intriguing, but difficult to explain. The explanation provided by the authors, based on previous work, 10 is currently the only plausible one. A graphic illustration is shown in Figure 1.…”
Section: Pathophysiological Role Of Et-1mentioning
confidence: 95%