5′-End RET Splicing: Absence of Variants in Normal Tissues and Intron Retention in Pheochromocytomas

• Published in: Oncology Vol. 63; no. 1; pp. 84 - 91
• Main Authors: Le Hir, Hervé, Charlet-Berguerand, Nicolas, de Franciscis, Vittorio, Thermes, Claude
• Format: Journal Article
• Language: English
• Published: Basel, Switzerland Karger 01.01.2002; S. Karger AG
• Subjects: 5' Untranslated Regions - genetics; Adrenals. Adrenal axis. Renin-angiotensin system (diseases); Alternative Splicing; Biological and medical sciences; Drosophila Proteins; Endocrinopathies; Humans; Introns - genetics; Laboratory Investigation; Life Sciences; Medical sciences; Non tumoral diseases. Target tissue resistance. Benign neoplasms; Pheochromocytoma - genetics; Pheochromocytoma - metabolism; Protein Isoforms - genetics; Proto-Oncogene Proteins - genetics; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins c-ret; Receptor Protein-Tyrosine Kinases - genetics; Receptor Protein-Tyrosine Kinases - metabolism; RNA, Messenger - metabolism; Tumor Cells, Cultured; RET; Pheochromocytomas; MEN2; Intron retention; Splicing; Endocrinopathy; Human; Pheochromocytoma; RNA; Enzyme; Pathogenesis; Transferases; Retention; Secretory tumor; Intron; Molecular biology; Protein-tyrosine kinase; Reverse transcription polymerase chain reaction

The Ret tyrosine kinase is implicated in neuronal cell survival, kidney development and tumorigenesis. Several 3′ and 5′ transcript variants have been described resulting from alternative splicing of the RET pre-mRNA. The 3′ variants code for three C-terminal isoforms, RET51, RET9 and RET43. The 5′...