TAILIEUCHUNG - Báo cáo Y học: Transglutaminase-mediated polyamination of vasoactive intestinal peptide (VIP) Gln16 residue modulates VIP/PACAP receptor activity

Previous data showing an increase of receptor binding activity of [R16]VIP, a vasoactive intestinal peptide (VIP) structural analogue containing arginine at the position 16 of its amino acid sequence, have pointed out the importance of a positive charge at this site. Here, the functional characterization of three VIP polyaminated adducts (VIPDap, VIPSpd, and VIPSpm), obtained by a transglutaminasecatalysed reaction between the VIP Gln16 residue and 1,3-diaminopropane (Dap), spermidine (Spd), or spermine (Spm), is reported. . | Eur. J. Biochem. 269 3211-3219 2002 FEBS 2002 doi Transglutaminase-mediated polyamination of vasoactive intestinal peptide VIP Gln16 residue modulates VIP PACAP receptor activity Salvatore De Maria1 Salvatore Metafora2 Vittoria Metafora2 Francesco Morelli2 Patrick Robberecht3 Maaali Waelbroeck3 Paola Stiuso4 Alfredo De Rosa1 Anna Cozzolino4 Carla Esposito4 Angelo Facchiano5 and Maria Carteni1 1 Department of Experimental Medicine and Centro di Ricerca Interdipartimentale di Scienze Computazionali e Biotecnologiche II University of Naples Italy 2CNR Institute of Genetics and Biophysics Adriano Buzzati Traverso Naples Italy 3Department of Biochemistry and Nutrition Medical School of Medicine Universite Libre de Bruxelles Bruxelles Belgium 4Department of Chemistry University of Salerno Salerno Italy 5Istituto di Scienze dell Alimentazione CNR Avellino Italy Previous data showing an increase of receptor binding activity of R16 VIP a vasocciive intettnial ppptide VIP structural analogue containing arginine at the position 16 of its amino acid sequence have pointed out hie importance of a positive charge at this site. Here the l unciional characterization of three VIP polyaminated adducts VIPDap VIPSpd ami VIPSpllj. bbtained by a a ansglummlnase-catalysed reaction between the VIP Gln16 residue and 1 3-diaminopcopane Dap sppl miaine p p cl or epmi mine Spm is eeported. A .pa OỊa iate binding asaays and adenylate cyclase enzymatic determinations have shown that these VIP adducts act as structural VIP agonists 130th in vitro and in vivo. In particular their IC50 and EC50 values of human and rat VIP pituitary adenylate cyclase activating peptide PACAP 1 and VIP pACAp2 receptors indicate ccVc VIPDap is a VIP agonist with an ahmity and a poeency higher than that of VIP whine VIIPSpd and VIPSpm are also agonists but with affinities lower than that of VIP. These findings suggest that the difference in adduct agonist activity reflects the .

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