High impact information on LOC397740

• These contain one or two copies of caerulein and five additional amino acids located between pairs of arginine residues [1].
• The extra glycine at the carboxy terminus is considered to serve as the signal for amidation, while the tetrapeptide Phe-Ala-Asp-Gly, linked to the amino end of caerulein in these precursors, must be cleaved by an unusual processing mechanism [1].
• The other peptides isolated are members of the magainin family of antimicrobial peptides, and include magainins I and II, PGLa, xenopsin precursor fragment, and four caerulein precursor fragments [2].
• In the homologous precursor polypeptides deduced from the nucleotide sequence of these cloned cDNAs, the caerulein copies are flanked by complex processing sequences [3].
• From skin of Xenopus laevis, cDNA libraries were constructed and clones coding for the precursors of caerulein were isolated and sequenced [3].

Biological context of LOC397740

• Besides deletions/insertions encompassing one or two caerulein sequences, these types also differ from each other by several point mutations [3].
• The concentrations of 5-HT and caerulein in the skin of tadpoles were below 1 ng per mg wet tissue at St [4].
• In the type I gene, in place of one of the caerulein exons, a potential exon with conserved splice sites was discovered [5].
• The caerulein sequences are separated by homologous sequences which potentially could give rise to additional constituents of skin secretion [6].

Associations of LOC397740 with chemical compounds

• The genes for the frog skin peptides GLa, xenopsin, levitide and caerulein contain a homologous export exon encoding a signal sequence and part of an amphiphilic peptide [7].
• Novel peptide fragments originating from PGLa and the caerulein and xenopsin precursors from Xenopus laevis [8].
• Preliminary assignments of these components were made by comparing these experimental molecular weights to those predicted for regions within the xenopsin, caerulein, thyrotropin-releasing hormone, and PGLa precursors [8].
• The immunoreactivities of 5-HT and caerulein were first detected in the spherical gland rudiments in the stratum spongiosum at St [4].
• Addition of thyroxine to the chFCS medium had no significant effect on the caerulein content [9].

Analytical, diagnostic and therapeutic context of LOC397740

• The HPLC chromatograms showed the secretion to be a complex mixture with over 30 components at similar levels to the four peptides previously isolated from X. laevis skin, i.e. xenopsin, caerulein, thyrotropin-releasing hormone, and PGLa [8].
• The result of Northern blotting indicated that caerulein mRNA was only present in frog skin, not in stomach, upper intestine or liver [10].
• We studied the development of glands producing 5-hydroxytryptamine (5-HT) and caerulein using immunohistochemistry, HPLC-fluorometric systems and RIA [4].
• High performance liquid chromatography (HPLC) of crude and Sephadex G-10 chromatographed secretions showed that many more peptides were present in these secretions than those previously identified, i.e., xenopsin, caerulein, TRH and PGLa [11].

References