5'-Terminal sequences of eucaryotic mRNA can be cloned with high efficiency.
#Caerulein precursor fragment 3 skin
An unusual repetitive structure of caerulein mRNA from the skin of Xenopus laevis. Molecular cloning and nucleotide sequence of cDNA coding for rat brain cholecystokinin precursor. Kuwano R, Araki K, Usui H, Fukui T, Ohtsuka E, Ikehara M, Takahashi Y.Cloning and sequence analysis of a cDNA encoding rat preprocholecystokinin. Deschenes RJ, Lorenz LJ, Haun RS, Roos BA, Collier KJ, Dixon JE.Cloned cDNA to cholecystokinin mRNA predicts an identical preprocholecystokinin in pig brain and gut. Gubler U, Chua AO, Hoffman BJ, Collier KJ, Eng J.Molecular cloning of human gastrin precursor cDNA. Kato K, Himeno S, Takahashi Y, Wakabayashi T, Tarui S, Matsubara K.Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin. Evidence for a common evolutionary origin of gastrin and cholecystokinin. Action of caerulein and caerulein-like peptides on "short-circuit current" and acid secretion in the isolated gastric mucosa of amphibians. Biogenic amines and active polypeptides in the skin of Australian amphibians. Erspamer V, Roseghini M, Endean R, Anastasi A.Links to PubMed are also available for Selected References.
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#Caerulein precursor fragment 3 full
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The relationship of caerulein to mammalian gastrointestinal hormones is discussed. It appears that caerulein has different physiological function(s) from mammalian gastrin and cholecystokinin-pancreozymin (CCK). The result of Northern blotting indicated that caerulein mRNA was only present in frog skin, not in stomach, upper intestine or liver. Analyses of several caerulein encoding cDNAs revealed some interesting features of caerulein mRNA species, which were highly heterogeneous and consisted of a repetition of two fundamental RNA sequences, a 45-nucleotide caerulein fragment and a 147-nucleotide ICS. It coded for four caerulein peptides interspersed with three 147 bp segments (intercaerulein segment ICS). The sequence was composed of 705 bp of coding region, accounting for 234 amino acids, 58 bp of 5'-untranslated region and 158 bp of 3'-untranslated region containing two putative poly(A) signals. All rights reserved.The complete nucleotide sequence of mRNA for caerulein precursor in the skin of Xenopus laevis was determined. Consistent with previous data, the CPF peptides showed the highest growth inhibitory activity against bacteria with CPF-W6 (GIGSLLAKAAKLAAGLV.NH2) combining high antimicrobial potency against Staphylococcus aureus (MIC=4 μM) with relatively low hemolytic activity (LC50=190 μM).Īllopolyploidy Antimicrobial Caerulein-precursor fragment Frog skin Xenopus.Ĭopyright © 2014 Elsevier Inc. wittei is more closely related to the Xenopus amieti-Xenopus andrei group suggesting a common tetraploid ancestor. vestitus and Xenopus lenduensis, suggestive of bifurcating speciation after allopolyploidization, whereas X. The data support a sister-group relationship between X. The primary structures of the peptides provide insight into phylogenetic relationships among the octoploid Xenopus frogs. The variability in the numbers of paralogs in each peptide family indicates a selective silencing of the host-defense peptide genes following the polyploidization events. wittei secretions contains the novel peptide xenopsin. In addition, secretions from both species contain caerulein, identical to the peptide from Xenopus laevis, but X. wittei peptides comprise magainin (4 peptides), PGLa (1 peptide), XPF (2 peptides), and CPF (7 peptides). vestitus peptides belong to the magainin (3 peptides), peptide glycine-leucine-amide (PGLa 4 peptides), xenopsin-precursor fragment (XPF 1 peptide), and caerulein-precursor fragment (CPF 5 peptides) families. Structural characterization demonstrated that the X. Peptidomic analysis was used to compare the diversity of host-defense peptides in norepinephrine-stimulated skin secretions from the octoploid frogs, Xenopus vestitus (Kivu clawed frog) and Xenopus wittei (De Witte's clawed frog) in the family Pipidae. The primary structures of host-defense peptides have proved useful in elucidating the evolution history of frogs.
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