Isolation and identification of multiple neuropeptides of the allatostatin superfamily in the shore crab Carcinus maenas
| Autor: | Jose-Luis Maestro, Alan Thorpe, Anders H. Johnsen, Peter P. Jaros, Alan G. Scott, Hanne Duve |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
medicine.medical_specialty
animal structures Insecta Brachyura Molecular Sequence Data Radioimmunoassay Peptide Biochemistry Pentapeptide repeat Homology (biology) Mass Spectrometry Evolution Molecular Internal medicine medicine Animals Carcinus maenas Amino Acid Sequence Thoracic ganglia Chromatography High Pressure Liquid chemistry.chemical_classification biology Sequence Homology Amino Acid Neuropeptides Allatostatin biology.organism_classification Amino acid medicine.anatomical_structure Endocrinology chemistry Sequence Analysis Periplaneta |
| Zdroj: | European journal of biochemistry. 250(3) |
| ISSN: | 0014-2956 |
| Popis: | 20 neuropeptides belonging to the allatostatin superfamily were isolated from extracts of cerebral and thoracic ganglia of the shore crab Carcinus maenas. They were purified by HPLC, monitored by radioimmunoassay and identified by mass spectrometry and amino acid sequencing. The allatostatins are characterised by a common C-terminal pentapeptide sequence -YXFGL-NH2. Previously such peptides have only been reported from insects. In insects the variable post-tyrosyl residue is restricted to Ala, Asn, Asp, Gly or Ser. In C. maenas, however, there are only two types; thirteen of the peptides having a post-tyrosyl Ala and the other seven, a post-tyrosyl Ser. The crab peptides include the shortest allatostatins so far identified (YAFGL-NH2 and YSFGL-NH2) as well as the longest, a 27-residue peptide. The total of 20 peptides exceeds the highest number of allatostatins found in any of the insects investigated so far (14 in Periplaneta americana). It is of interest that, despite their clear homology, none of the peptides of C. maenas is identical to any of the more than 50 known insect allatostatins. The crab allatostatins show evidence of gene duplication and mutation that has resulted in several sub-groups with close structural similarities. For example, there are four heptapeptides with the common C-terminus -PYAFGL-NH2 that differ only at the N-terminal residue, which is either Glu, Asp, Asn or Ser. Other motifs, variously extended at the N-terminus, include -GPY(A/S)FGL-NH2 (three peptides), -DMY(A/S)FGL-NH2 (three peptides), and -GQY(A/S)FGL-NH2 (two peptides). Unique among the allatostatin superfamily, one of the crab peptides has a Tyr for Phe substitution at position three from the C-terminus (GGPYSYGL-NH2). Immunocytochemistry has provided clues to the functions of the allatostatins in crustaceans by showing their widespread presence in the central and stomatogastric nervous systems. |
| Databáze: | OpenAIRE |
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