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Crustacean hypergly...
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.
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- Dircksen, Heinrich, 1954- (author)
- Institute of Zoophysiology, University of Bonn, Germany
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Böcking, D (author)
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Heyn, U (author)
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Mandel, C (author)
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Chung, J S (author)
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Baggerman, G (author)
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Verhaert, P (author)
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Daufeldt, S (author)
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Plösch, T (author)
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Jaros, P P (author)
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Waelkens, E (author)
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Keller, R (author)
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Webster, S G (author)
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(creator_code:org_t)
- 2001
- 2001
- English.
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In: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 356:Pt 1, s. 159-70
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Abstract
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Biology
- Biologi
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Dircksen, Heinri ...
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Böcking, D
-
Heyn, U
-
Mandel, C
-
Chung, J S
-
Baggerman, G
-
show more...
-
Verhaert, P
-
Daufeldt, S
-
Plösch, T
-
Jaros, P P
-
Waelkens, E
-
Keller, R
-
Webster, S G
-
show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
- Articles in the publication
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Biochemical Jour ...
- By the university
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Stockholm University