Two di-leucine-based motifs account for the different subcellular localizations of the human endothelin-converting enzyme (ECE-1) isoforms

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Population

CHO cells expressing human endothelin-converting enzyme (ECE-1) isoforms

Comparison

Construction of chimeric proteins and point… vs Wild-type ECE-1 isoforms (ECE-1a, ECE-1b, ECE-1c)

Design

Preclinical

Authors

Discussion

Does not yet inform clinical endothelin management; leaves open the in vivo impact of ECE-1b surface trafficking.

Population

CHO cells expressing human endothelin-converting enzyme (ECE-1) isoforms

Intervention

Construction of chimeric proteins and point mutants of di-leucine-based motifs (LL and LV) in the N-terminal part of ECE-1b

Comparator

Wild-type ECE-1 isoforms (ECE-1a, ECE-1b, ECE-1c)

Outcome

Subcellular localization of ECE-1 isoforms (cell surface vs intracellular expression)surrogate

The study identifies two di-leucine-based motifs in the N-terminal region of ECE-1b that are critical for its intracellular localization.

Valdenaire et al. (1999) studied this question.

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