scholarly journals 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

2001 ◽  
Vol 356 (1) ◽  
pp. 159-170 ◽  
Author(s):  
Heinrich DIRCKSEN ◽  
Detlef BÖCKING ◽  
Uwe HEYN ◽  
Christa MANDEL ◽  
J. Sook CHUNG ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Carcinus Maenas ◽  
Penaeid Shrimp ◽  
Neurosecretory Cells ◽  
Shore Crab ◽  
Amino Acid Peptide ◽  
C Terminus ◽  
Gene Structures

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 (8630Da) 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-CHH41–76 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-CHH1–40/SG-CHH1–40 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.

The Uptake of Cadmium Into the Haemolymph of the Shore Crab Carcinus Maenas: The Relationship With Copper and Other Divalent Cations

1977 ◽  
Vol 67 (1) ◽  
pp. 147-161
Author(s):  
D. A. WRIGHT
Keyword(s):  
Divalent Cations ◽  
Cadmium Concentration ◽  
Carcinus Maenas ◽  
Shore Crab ◽  
Cadmium Level ◽  
Haemolymph Protein ◽  
Urine Cadmium ◽  
The Relationship

When Carcinus was exposed to 20 μ-mol l−1 cadmium, the haemolymph cadmium level was initially dependent upon the salinity of the external medium. After 14 days the mean haemolymph cadmium level in 50% s.w. animals was nearly twice that of 100% s.w. animals. This trend was not sustained, however, and the situation was complicated by occasional inconsistent values. In both in vivo and in vitro conditions nearly all the haemolymph cadmium becomes bound to haemolymph protein within a few days. The relationship between haemolymph cadmium, copper and protein concentration has been investigated. Although the latter are highly correlated with each other, cadmium formed a significant positive relationship with haemolymph copper (r = 0.523) and protein (r = 0.533) only after 3–4 weeks uptake. Exposure to 20 μ-mol l−1 cadmium has no obvious effects on haemolymph protein and copper concentrations, which are clearly dependent on feeding status. Mortalities among experimental animals were often preceded by a rise in haemolymph cadmium concentration. This is usually seen before there are any obvious signs of tissue breakdown. Urine cadmium loss is probably unimportant as a pathway for the elimination of this metal. Urine cadmium concentrations often exceeded serum cadmium levels indicating that cadmium may sometimes be eliminated in bound form.

Abstract 5432: Mutation of Three Amino Acids in the Disulfide-Ring of a CNP Based Chimeric Natriuretic Peptide Alters its Vascular Properties

Circulation ◽  
2008 ◽  
Vol 118 (suppl_18) ◽  
Author(s):  
Horng H Chen ◽  
Brenda K Huntley ◽  
Candace Y Lee ◽  
Fernando L Martin ◽  
John A Schirger ◽  
...  
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Right Atrial ◽  
Bolus Administration ◽  
Amino Acid Peptide ◽  
Arterial Blood ◽  
C Terminus ◽  
Cardiac Unloading

BACKGROUND: C-type natriuretic peptide (CNP) is a 22-amino-acid peptide produced mainly in the endothelium with potent cardiac unloading and modest blood pressure lowering actions, but minimal renal actions. Based on our previous knowledge, we recently fused a 6 aa sequence from BNP to the C-terminus and a 5 aa sequence from ANP to the N-terminus of CNP. This novel hybrid peptide, CBA-NP, has cardiac unloading actions and mild hypotensive effects similar to CNP. Importantly however, the N and C terminus alterations resulted in potent renal excretory actions. here we test the hypothesis that the 3 aa GSM 15–17 in the disulfide-ring mediate the vascular and hypotensive actions. We therefore mutated GSM 15–17 to REA 15–17 , which we named ABC-NP and compared its in vivo and in vitro actions to CBA-NP. METHODS: We determined the cardiorenal and humoral actions of intravenous bolus administration of CBA-NP (n=5) and ABC-NP (n=5) at 25 microgram/Kg in 2 separate group of normal anesthetized dogs. We also assessed the cGMP response of both peptides in human aortic endothelial cells (HAEC), human cardiac fibroblast (HCF) and isolated canine glomeruli. * p<0.05 RESULTS: IV bolus administration of CBA-NP and ABC-NP resulted in diuresis* and natriuresis*. There was a significant decrease in mean arterial blood (MAP) pressure with CBA-NP (126±6 to113±7 mmHg*) but no change with ABC-NP(126±8 to126±8 mmHg) . In addition, the reduction in pulmonary capillary wedge pressure (PCWP) and right atrial pressure (RAP) was significantly greater with CBA-NP as compared to ABC-NP. cGMP generation in HAEC and HCF was minimal with ABC-NP and was significantly higher with CBA-NP*. In contrast, cGMP generation was similar in isolated glomeruli between the two peptides. CONCLUSION: Our studies demonstrates that mutation of three amino acid (aa) residues within the CNP ring of CBA-NP from GSM 15–17 to REA alters the vascular but not the renal excretory properties. Hence by this strategic mutation within the ring of CBA-NP, we have designed a renal specific peptide ABC-NP resulting in new sequence specific functional information which can be used to design organ specific therapeutic peptides with unique properties tailored for a specific disease state.

Host Defence Reactions of the Shore Crab, Carcinus Maenas (L.): Clearance and Distribution of Injected Test Particles

1980 ◽  
Vol 60 (1) ◽  
pp. 89-102 ◽  
Author(s):  
Valerie J. Smith ◽  
N. A. Ratcliffe
Keyword(s):  
Specific Activity ◽  
Carcinus Maenas ◽  
Shore Crab ◽  
Foreign Material ◽  
Defence Mechanisms ◽  
Test Particles ◽  
Cellular Defence ◽  
Defence Reactions

It is well established that crustaceans can overcome infection and clear foreign material introduced into the circulation (Cornick & Stewart, 1968; Tyson & Jenkin, 1973; Stewart & Zwicker, 1974). In the absence of vertebrate-type specific acquired immunity, the non-specific activity mediated by the circulating blood cells appears to be of considerable importance in resistance to disease (Sindermann, 1971). Among the cellular defence mechanisms of the Crustacea, phagocytosis has received most attention and there is considerable evidence from in vitro studies that this process plays an important part in the removal of foreign particles from the blood (McKay & Jenkin, 1970a; Paterson & Stewart, 1974; Tyson & Jenkin, 1974; Paterson, Stewart & Zwicker, 1976; Smith & Ratcliffe, 1978). Such studies, however, may not always reflect the true in vivo condition, and there is a great need for correlated in vitro and in vivo investigations.

PROPRIOCEPTIVE INPUT FROM TWO BASAL JOINT STRETCH RECEPTORS TO LEG MOTONEURONES IN THE ISOLATED THORACIC GANGLION OF THE SHORE CRAB

1992 ◽  
Vol 163 (1) ◽  
pp. 187-208
Author(s):  
STEWART I. HEAD ◽  
BRIAN M.H. BUSH
Keyword(s):  
Motor Nerve ◽  
Carcinus Maenas ◽  
Thoracic Ganglion ◽  
Shore Crab ◽  
Chordotonal Organ ◽  
Leg Muscles ◽  
Receptor Organ ◽  
Motor Nerves

The reflex effects and interactions of two proprioceptors upon motoneurones supplying the four basal leg muscles of the shore crab Carcinus maenas have been studied in a new in vitro preparation consisting of the thoracic-coxal muscle receptor organ (TCMRO) and the coxo-basal chordotonal organ (CBCO) isolated together with the whole thoracic ganglion complex to which they were still connected by their afferent nerves. Each receptor strand was stimulated mechanically, while recording intracellularly from motoneurones in the ganglion, and extracellularly from the cut motor nerves innervating the promotor and remotor muscles of the thoracic-coxal (T—C) joint and the levator and depressor muscles of the coxo-basal (C—B) joint. Stretch of the TCMRO evoked reflex firing in several units in the promotor motor nerve, confirming previous studies. In addition to this ‘intrajoint’ reflex, however, TCMRO stretch also elicited ‘interjoint’ reflex responses in motoneurones of both the levator and depressor muscles. Similarly, stretch and release of the CBCO produced intrajoint resistance reflexes in levator and depressor motoneurones, respectively, as well as interjoint reflexes in promotor and remotor motoneurones. In general, the CBCO produced stronger reflex effects in all four motor nerves than did the TCMRO. Intracellular recordings from individual motoneurones of all four muscles revealed that the majority of them received convergent input from both proprioceptors. The importance of such convergent input in vivo is discussed

scholarly journals A Peptide Found in Human Serum, Derived from the C-Terminus of Albumin, Shows Antifungal Activity In Vitro and In Vivo

2020 ◽  
Vol 8 (10) ◽  
pp. 1627
Author(s):  
Tecla Ciociola ◽  
Pier Paolo Zanello ◽  
Tiziana D’Adda ◽  
Serena Galati ◽  
Stefania Conti ◽  
...  
Keyword(s):  
Antifungal Activity ◽  
Human Serum ◽  
Fungicidal Activity ◽  
Galleria Mellonella ◽  
Serum Proteins ◽  
Morphological Alterations ◽  
C Terminus ◽  
Different Sources

The growing problem of antimicrobial resistance highlights the need for alternative strategies to combat infections. From this perspective, there is a considerable interest in natural molecules obtained from different sources, which are shown to be active against microorganisms, either alone or in association with conventional drugs. In this paper, peptides with the same sequence of fragments, found in human serum, derived from physiological proteins, were evaluated for their antifungal activity. A 13-residue peptide, representing the 597–609 fragment within the albumin C-terminus, was proved to exert a fungicidal activity in vitro against pathogenic yeasts and a therapeutic effect in vivo in the experimental model of candidal infection in Galleria mellonella. Studies by confocal microscopy and transmission and scanning electron microscopy demonstrated that the peptide penetrates and accumulates in Candida albicans cells, causing gross morphological alterations in cellular structure. These findings add albumin to the group of proteins, which already includes hemoglobin and antibodies, that could give rise to cryptic antimicrobial fragments, and could suggest their role in anti-infective homeostasis. The study of bioactive fragments from serum proteins could open interesting perspectives for the development of new antimicrobial molecules derived by natural sources.

scholarly journals C-Terminal Deletions Can Suppress Temperature-Sensitive Mutations and Change Dominance in the Phage Mu Repressor

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 661-672 ◽  
Author(s):  
Jodi L Vogel ◽  
Vincent Geuskens ◽  
Lucie Desmet ◽  
N Patrick Higgins ◽  
Ariane Toussaint
Keyword(s):  
Binding Activity ◽  
Temperature Sensitive ◽  
Dna Binding Activity ◽  
Heat Stable ◽  
C Terminus ◽  
Acid Domain ◽  
Mutant Forms ◽  
Amino Acid Domain

Abstract Mutations in an N-terminal 70-amino acid domain of bacteriophage Mu's repressor cause temperature-sensitive DNA-binding activity. Surprisingly, amber mutations can conditionally correct the heat-sensitive defect in three mutant forms of the repressor gene, cts25 (D43-G), cts62 (R47-Q and cts71 (M28-I), and in the appropriate bacterial host produce a heat-stable Sts phenotype (for survival of temperature shifts). Sts repressor mutants are heat sensitive when in supE or supF hosts and heat resistant when in Sup° hosts. Mutants with an Sts phenotype have amber mutations at one of three codons, Q179, Q187, or Q190. The Sts phenotype relates to the repressor size: in Sup° hosts sts repressors are shorter by seven, 10, or 18 amino acids compared to repressors in supE or supF hosts. The truncated form of the sts62-1 repressor, which lacks 18 residues (Q179–V196), binds Mu operator DNA more stably at 42° in vitro compared to its full-length counterpart (cts62 repressor). In addition to influencing temperature sensitivity, the C-terminus appears to control the susceptibility to in vivo Clp proteolysis by influencing the multimeric structure of repressor.

Activation of the peptidergic neurosecretory system in Diphyllobothrium dendriticum (Cestoda: Pseudophyllidea)

Parasitology ◽  
1981 ◽  
Vol 83 (2) ◽  
pp. 243-247 ◽  
Author(s):  
Margaretha K. S. Gustafsson ◽  
Marianne C. Wikgren
Keyword(s):  
Neurosecretory Cells ◽  
Final Host ◽  
Fish Host ◽  
Neurosecretory System ◽  
Weak Reaction ◽  
Diphyllobothrium Dendriticum ◽  
Large Numbers ◽  
Short Times

SUMMARYThe activation of the peptidergic neurosecretory system in Diphyllobothrium dendriticum was studied following cultivation of plerocercoids for short times in vitro and in vivo. In the plerocercoid the neurosecretory cells gave a very weak reaction with paraldehyde fuchsin (PAF). After cultivation for 1 h large numbers of neurosecretory cells filled with PAF-positive granules were evident. The significance of the activation of the neurosecretory system during the transfer of the worm from the cold-blooded fish host to the warm-blooded final host is discussed.

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