High impact information on Gly-phe-ala-asp

• Molecular mechanism of the binding of neuropeptide achatin-I (Gly-D-Phe-Ala-Asp) to large unilamellar vesicles of zwitterionic egg-yolk phosphatidylcholine (EPC) was investigated by means of natural-abundance (13)C and high-resolution (of 0.01 Hz order) (1)H NMR spectroscopy [1].
• The binding caused upfield changes Delta delta of the (13)C resonance for almost all the carbon sites in achatin-I [1].
• The molecular conformation of achatin-II neutral form (H-Gly-Phe-Ala-Asp-OH), an endogenous peptide from the Achatina fulica ganglia, was elucidated by X-ray crystal analysis [2].
• We succeeded in cloning a cDNA encoding a precursor of achatin-I from the Achatina ganglia, revealing that the d-Phe present in achatin-I is coded by a common l-Phe codon, TTT or TTC [3].
• Dose (pressure duration)-response study of achatin-I on PON in a physiological solution and in the presence of H-89, and Lineweaver-Burk plot of these data, indicated that H-89 inhibited the Iin in a noncompetitive manner [4].

Biological context of Gly-phe-ala-asp

• Molecular conformation of achatin-I, an endogenous neuropeptide containing D-amino acid residue. X-ray crystal structure of its neutral form [5].
• The amino acid sequence of achatin-I is Gly-D-Phe-Ala-Asp [6].
• Multiple intracellular signal transduction pathways mediating inward current produced by the neuropeptide, achatin-I [4].
• Northern blot analysis of transcripts and Southern blot analysis of reverse transcription (RT)-PCR products demonstrated that achatin-I mRNA was localized in the subesophageal ganglia, whereas expression of fulicin mRNA was detected in the atrium as well as in the subesophageal ganglia [3].
• Structure-activity relationship studies on the endogenous neuroactive tetrapeptide achatin-I on giant neurons of Achatina fulica Ferussac [7].

Associations of Gly-phe-ala-asp with other chemical compounds

• Following a preliminary report on the isolation of a neuroactive tetrapeptide, achatin-I (Gly-D-Phe-L-Ala-L-Asp) that has a D-phenylalanine residue, from the Achatina fulica ganglia, the pharmacological features of this peptide on Achatina giant neurones were now worked out in detail [8].
• These data suggested that achatin-I plays an essential role in the regulation of the heart as a neurotransmitter or neurohormone through production in the pedal ganglia and transport to the atrium, whereas fulicin serves not only as a neurotransmitter or neurohormone but also as a novel atrial hormone [3].
• H-89 (N-[2-(p-bromocinnamylamino)-ethyl]-5-isoquinolinesulfonamide) (adenosine-3',5'-cyclic monophosphate (cyclic AMP)-dependent protein kinase inhibitor) markedly suppressed the achatin-I-induced Iin on PON, whereas this drug was ineffective on the Iin of v-RCDN [4].
• IBMX (3-isobutyl-1-methylxanthine) (cyclic nucleotide phosphodiesterase inhibitor) enhanced the achatin-I-induced Iin of v-RCDN, but this drug was ineffective on the Iin of PON [4].
• 3. N-beta-phenylpropionyl-L-tyrosine (BPLT), a membrane hyperpolarizant, at 10(-6) M and concanavalin A (Con A), which altered the response to L-glutamate, at 100 micrograms/ml-1 were considered to hardly influence the PON excitation caused by achatin-I [9].

Gene context of Gly-phe-ala-asp

• Some histamine H1 receptor antagonists suppressed the inward current (Iin) of an Achatina identifiable neurone type, PON (periodically oscillating neurone), caused by an Achatina endogenous tetrapeptide having a D-phenylalanine residue, achatin-I (Gly-D-Phe-Ala-Asp), under voltage clamp [10].

Analytical, diagnostic and therapeutic context of Gly-phe-ala-asp

• Achatin-I was applied locally to the neurone by brief pneumatic pressure ejection and antagonists were administered by perfusion [10].
• The data of instrumental analyses (1H-NMR, SIMS, CD and HPLC) of isolated achatin-I and achatin-II were identical to those of synthetic ones [11].

References