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PubMed · 11571936

Antidiuretic hormone. Normal and disordered function.

G L Robertson
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Abstract

In humans and most other mammals, the antidiuretic hormone (ADH) is a nonapeptide often referred to as arginine vasopressin (AVP). It is produced by large neurons that originate in the supraoptic and paraventricular nucleus of the hypothalamus and project through the pituitary stalk to terminate on capillary plexuses scattered throughout the posterior pituitary. These plexuses drain into the systemic circulation by way of the cavernous sinus and superior vena cava.

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Arginine VasopressinHumansHypernatremiaInappropriate ADH SyndromeVasopressinsJournal ArticleResearch Support, U.S. Gov't, P.H.S.Review

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G L Robertson. 2001. Antidiuretic hormone. Normal and disordered function.. https://doi.org/10.1016/s0889-8529(05)70207-3

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Upstream stimulatory factor activates the vasopressin promoter via multiple motifs, including a non-canonical E-box.

We have described previously a complex E-box enhancer (-147) of the vasopressin promoter in small-cell lung cancer (SCLC) extracts [Coulson, Fiskerstrand, Woll and Quinn, (1999) Biochem. J. 344, 961-970]. Upstream stimulatory factor (USF) heterodimers were one of the complexes binding to this site in vitro. We now report that USF overexpression in non-SCLC (NSCLC) cells can functionally activate vasopressin promoter-driven reporters that are otherwise inactive in this type of lung cancer cell. Site-directed mutagenesis and electrophoretic mobility-shift analysis demonstrate that although the -147 E-box contributes, none of the previously predicted E-boxes (-147, -135, -34) wholly account for this USF-mediated activation in NSCLC. 5' Deletion showed the key promoter region as -52 to +42; however, USF-2 binding was not reliant on the -34 E-box, but on a novel adjacent CACGGG non-canonical E-box at -42 (motif E). This mediated USF binding in both SCLC and USF-2-transfected NSCLC cells. Mutation of motif E or the non-canonical TATA box abolished activity, implying both are required for transcriptional initiation on overexpression of USF-2. Co-transfected dominant negative USF confirmed that binding was required through motif E for function, but that the classical activation domain of USF was not essential. USF-2 bound motif E with 10-fold lower affinity than the -147 E-box. In NSCLC, endogenous USF-2 expression is low, and this basal level appears to be insufficient to activate transcription of arginine vasopressin (AVP). In summary, we have demonstrated a novel mechanism for USF activation, which contributes to differential vasopressin expression in lung cancer.

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