%0 Journal Article %1 Dircksen:2001p45356 %A Dircksen, H %A Böcking, D %A Heyn, U %A Mandel, C %A Chung, J S %A Baggerman, G %A Verhaert, P %A Daufeldt, S %A Plösch, T %A Jaros, P P %A Waelkens, E %A KELLER, R %A Webster, S G %D 2001 %J Biochem J %K Acid Alternative Amino Analysis: Animals, Assay, Base Biological Blood Brachyura, Cloning: Complementary, DNA, DNA: Data, Distribution, Ecdysteroids, Genetic, Glucose, Hemolymph, Hormones, Invertebrate Male, Models: Molecular Molecular, Neurons, Neurosecretory Peptides, Precursors, Protein Sequence Sequence, Splicing, Steroids, Systems, Tissue %N Pt 1 %P 159--70 %T Crustacean hyperglycaemic hormone (CHH)-like peptides and CHH-precursor-related peptides from pericardial organ neurosecretory cells in the shore crab, Carcinus maenas, are putatively spliced and modified products of multiple genes %V 356 %X About 24 intrinsic neurosecretory neurons within the pericardial organs (POs) of the crab Carcinus maenas produce a novel crustacean hyperglycaemic hormone (CHH)-like peptide (PO-CHH) and two CHH-precursor-related peptides (PO-CPRP I and II) as identified immunochemically and by peptide chemistry. Edman sequencing and MS revealed PO-CHH as a 73 amino acid peptide (8630 Da) with a free C-terminus. PO-CHH and sinus gland CHH (SG-CHH) share an identical N-terminal sequence, positions 1-40, but the remaining sequence, positions 41-73 or 41-72, differs considerably. PO-CHH may have different precursors, as cDNA cloning of PO-derived mRNAs has revealed several similar forms, one exactly encoding the peptide. All PO-CHH cDNAs contain a nucleotide stretch coding for the SG-CHH(41-76) sequence in the 3'-untranslated region (UTR). Cloning of crab testis genomic DNA revealed at least four CHH genes, the structure of which suggest that PO-CHH and SG-CHH arise by alternative splicing of precursors and possibly post-transcriptional modification of PO-CHH. The genes encode four exons, separated by three variable introns, encoding part of a signal peptide (exon I), the remaining signal peptide residues, a CPRP, the PO-CHH(1-40)/SG-CHH(1-40) sequences (exon II), the remaining PO-CHH residues (exon III) and the remaining SG-CHH residues and a 3'-UTR (exon IV). Precursor and gene structures are more closely related to those encoding related insect ion-transport peptides than to penaeid shrimp CHH genes. PO-CHH neither exhibits hyperglycaemic activity in vivo, nor does it inhibit Y-organ ecdysteroid synthesis in vitro. From the morphology of the neurons it seems likely that novel functions remain to be discovered.

@article{Dircksen:2001p45356, abstract = {About 24 intrinsic neurosecretory neurons within the pericardial organs (POs) of the crab Carcinus maenas produce a novel crustacean hyperglycaemic hormone (CHH)-like peptide (PO-CHH) and two CHH-precursor-related peptides (PO-CPRP I and II) as identified immunochemically and by peptide chemistry. Edman sequencing and MS revealed PO-CHH as a 73 amino acid peptide (8630 Da) with a free C-terminus. PO-CHH and sinus gland CHH (SG-CHH) share an identical N-terminal sequence, positions 1-40, but the remaining sequence, positions 41-73 or 41-72, differs considerably. PO-CHH may have different precursors, as cDNA cloning of PO-derived mRNAs has revealed several similar forms, one exactly encoding the peptide. All PO-CHH cDNAs contain a nucleotide stretch coding for the SG-CHH(41-76) sequence in the 3'-untranslated region (UTR). Cloning of crab testis genomic DNA revealed at least four CHH genes, the structure of which suggest that PO-CHH and SG-CHH arise by alternative splicing of precursors and possibly post-transcriptional modification of PO-CHH. The genes encode four exons, separated by three variable introns, encoding part of a signal peptide (exon I), the remaining signal peptide residues, a CPRP, the PO-CHH(1-40)/SG-CHH(1-40) sequences (exon II), the remaining PO-CHH residues (exon III) and the remaining SG-CHH residues and a 3'-UTR (exon IV). Precursor and gene structures are more closely related to those encoding related insect ion-transport peptides than to penaeid shrimp CHH genes. PO-CHH neither exhibits hyperglycaemic activity in vivo, nor does it inhibit Y-organ ecdysteroid synthesis in vitro. From the morphology of the neurons it seems likely that novel functions remain to be discovered.}, added-at = {2009-11-12T16:21:13.000+0100}, affiliation = {Institut f{\"u}r Zoophysiologie, Universit{\"a}t Bonn, Endenicher Allee 11-13, D-53115 Bonn, Germany. Dircksen@uni-bonn.de}, author = {Dircksen, H and B{\"o}cking, D and Heyn, U and Mandel, C and Chung, J S and Baggerman, G and Verhaert, P and Daufeldt, S and Pl{\"o}sch, T and Jaros, P P and Waelkens, E and KELLER, R and Webster, S G}, biburl = {https://www.bibsonomy.org/bibtex/2d1e3f43ce684eb80cfc0feb9140ad7a6/fdiehl}, date-added = {2009-09-23 23:15:56 +0200}, date-modified = {2009-11-10 09:45:22 +0100}, description = {bib-komplett}, interhash = {797387caa520beab7244c1c21c4bbc0a}, intrahash = {d1e3f43ce684eb80cfc0feb9140ad7a6}, journal = {Biochem J}, keywords = {Acid Alternative Amino Analysis: Animals, Assay, Base Biological Blood Brachyura, Cloning: Complementary, DNA, DNA: Data, Distribution, Ecdysteroids, Genetic, Glucose, Hemolymph, Hormones, Invertebrate Male, Models: Molecular Molecular, Neurons, Neurosecretory Peptides, Precursors, Protein Sequence Sequence, Splicing, Steroids, Systems, Tissue}, language = {eng}, local-url = {file://localhost/Neurobio/Papers/11336648.pdf}, month = May, number = {Pt 1}, pages = {159--70}, pmid = {11336648}, rating = {0}, timestamp = {2009-11-12T16:21:16.000+0100}, title = {Crustacean hyperglycaemic hormone (CHH)-like peptides and CHH-precursor-related peptides from pericardial organ neurosecretory cells in the shore crab, Carcinus maenas, are putatively spliced and modified products of multiple genes}, uri = {papers://7B65697B-E216-4648-8A41-C67830C0DC73/Paper/p45356}, volume = 356, year = 2001 }