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.
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.
Dircksen
H
H
Institut für Zoophysiologie, Universität Bonn, Endenicher Allee 11-13, D-53115 Bonn, Germany. Dircksen@uni-bonn.de
Böcking
D
D
Heyn
U
U
Mandel
C
C
Chung
J S
JS
Baggerman
G
G
Verhaert
P
P
Daufeldt
S
S
Plösch
T
T
Jaros
P P
PP
Waelkens
E
E
Keller
R
R
Webster
S G
SG
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins; D001483:Base Sequence; D001681:Biological Assay; D001786:Blood Glucose / Q000378:metabolism; D003386:Brachyura; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D026461:Ecdysteroids; D006458:Hemolymph; D007447:Invertebrate Hormones / Q000235:genetics / Q000302:isolation & purification*; D008297:Male; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009474:Neurons / Q000737:chemistry*; D009490:Neurosecretory Systems / Q000737:chemistry*; D010455:Peptides / Q000235:genetics / Q000302:isolation & purification*; D011498:Protein Precursors / Q000235:genetics / Q000302:isolation & purification*; D017422:Sequence Analysis, DNA; D013256:Steroids / Q000378:metabolism; D014018:Tissue Distribution
D060829:Arthropod Proteins; D001786:Blood Glucose; C116855:CHH-like protein, shrimp; D018076:DNA, Complementary; D026461:Ecdysteroids; D007447:Invertebrate Hormones; D010455:Peptides; D011498:Protein Precursors; D013256:Steroids