Identification of a novel alternatively spliced variant endothelin converting enzyme-1 lacking a transmembrane domain
| Autor: | Klipper, E., Levy, N., Gilboa, T., laurent Muller, Meidan, R. |
|---|---|
| Přispěvatelé: | Centre interdisciplinaire de recherche en biologie (CIRB), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM) |
| Rok vydání: | 2006 |
| Předmět: |
Umbilical Veins
[SDV]Life Sciences [q-bio] MESH: Metalloendopeptidases MESH: Umbilical Veins [SDV.BC]Life Sciences [q-bio]/Cellular Biology Endothelin-Converting Enzymes Cell Line MESH: Protein Structure Tertiary Corpus Luteum Animals Aspartic Acid Endopeptidases Humans MESH: Animals MESH: Endothelin-Converting Enzymes [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology RNA Messenger MESH: Corpus Luteum Cells Cultured MESH: RNA Messenger MESH: Humans MESH: Alternative Splicing MESH: Molecular Weight Metalloendopeptidases MESH: Cell Line Protein Structure Tertiary Isoenzymes Molecular Weight MESH: Cattle Alternative Splicing MESH: Isoenzymes Cattle Female MESH: Endothelium Vascular MESH: Aspartic Acid Endopeptidases Endothelium Vascular MESH: Female MESH: Cells Cultured |
| Zdroj: | Experimental Biology and Medicine Experimental Biology and Medicine, SAGE Publications (UK and US), 2006, 231 (6), pp.723-728. ⟨10.3181/00379727-231-2310723⟩ ResearcherID |
| ISSN: | 1535-3702 1535-3699 |
| DOI: | 10.3181/00379727-231-2310723⟩ |
| Popis: | International audience; Endothelin-converting enzyme (ECE)-1 cleaves big endothelins, as well as bradykinin and beta-amyloid peptide. Several isoforms of ECE-1 (ECE-1a, 1b, 1c, and 1d) have been identified to date, they differ only in their amino terminus and share the catalytic domain located in the C-terminal end. In addition to full-length ECE-1 forms, we identified novel, alternatively spliced messenger RNAs (mRNAs) of ECE-1b, 1c, and 1d. These splice variants (SVs) lack exon 3', which codes for the transmembrane (TM) region and is present in full-length forms. SV mRNAs were highly expressed in endothelial cells (EC) derived from macrovascular and microvascular beds. Analyses of ECE-1d and its SV forms in stably transfected human embryonic kidney (HEK)-293 cells revealed that both proteins were recognized by antibodies to C-terminal ECE-1, but an antibody to the N-terminal only bound ECE-1d. The novel protein, designated ECE-1sv, has an apparent molecular weight of 75 kDa. ECE-1sv lacks the TM sequence (or signal peptide) and, therefore, is expected to remain cytosolic. Presence of ECE-1sv in different cellular compartments than the full-length forms of the ECE-1 may suggest a distinct physiologic role for these proteins. |
| Databáze: | OpenAIRE |
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