RESUMEN
Fourth ventricular outlet obstruction (FVOO) is a rare cause of obstructive hydrocephalus. Although FVOO accompanied by malformative syndrome and secondary causes of obstruction are common, there are few reports of primary FVOO (PFVOO). The syndrome of inappropriate antidiuretic hormone secretion (SIADH) is a rare presenting feature of hydrocephalus. A 1-year, 8-month-old boy with a normal head circumference developed SIADH accompanied by rapid deterioration of symptoms of intracranial hypertension. PFVOO was diagnosed because magnetic resonance imaging revealed an enlarged ventricular system with a barely visible membranous obstacle at the foramen of Magendie. All symptoms were resolved by endoscopic third ventriculostomy. PFVOO should be considered as a rare form of congenital obstructive hydrocephalus, especially in patients with tetraventricular hydrocephalus. To the best of our knowledge, this is the first case of an infant with SIADH, resulting from acute deterioration of non-tumoral raised pressure hydrocephalus.
Asunto(s)
Cuarto Ventrículo , Hidrocefalia/complicaciones , Síndrome de Secreción Inadecuada de ADH/etiología , Humanos , Hidrocefalia/congénito , Lactante , Imagen por Resonancia Magnética , MasculinoRESUMEN
The GLW-amide family is a neuropeptide family found in cnidarian species and is characterized by the C-terminal amino acid sequence -Gly-Leu-Trp-NH(2). To detect mammalian peptides structurally related to the GLW-amide family, we examined rat brain by immunohistochemistry with an anti-GLW-amide antibody. GLW-amide-like immunoreactivity (GLW-amide-LI) was observed in thin varicose fibers in some regions of the brain. Most neurons showing GLW-amide-LI were observed in the laterodorsal tegmental nucleus, pedunculopontine tegmental nucleus, and trigeminal/spinal ganglia. These results strongly suggest that the rat nervous system contains as yet unidentified GLW-amide-like peptides, and that GLW-amide-LI in the brain is a good marker for ascending projections from mesopontine cholinergic neurons.
Asunto(s)
Neuropéptidos/análisis , Animales , Biomarcadores/análisis , Biomarcadores/metabolismo , Encéfalo/citología , Encéfalo/metabolismo , Fibras Colinérgicas/metabolismo , Hydra/metabolismo , Inmunohistoquímica , Masculino , Neuropéptidos/biosíntesis , Ratas , Ratas Wistar , Médula Espinal/citología , Médula Espinal/metabolismo , Ganglio del Trigémino/metabolismoRESUMEN
Pigment-dispersing factors (PDFs) are octadeca-peptides widely distributed in insect optic lobes and brain. In this study, we have purified PDF and determined its amino acid sequence in the cricket Gryllus bimaculatus. Its primary structure was NSEIINSLLGLPKVLNDA-NH(2), homologous to other PDH family members so far reported. When injected into the optic lobe of experimentally blinded adult male crickets, Gryllus-PDF induced phase shifts in their activity rhythms in a phase dependent and dose dependent manner. The resulted phase response curve (PRC) showed delays during the late subjective night to early subjective day and advances during the mid subjective day to mid subjective night. The PRC was different in shape from those for light, serotonin and temperature. These results suggest that PDF plays a role in phase regulation of the circadian clock through a separate pathway from those of other known phase regulating agents.
Asunto(s)
Ritmo Circadiano/fisiología , Proteínas de Drosophila , Gryllidae/fisiología , Neuropéptidos/genética , Secuencia de Aminoácidos , Animales , Ritmo Circadiano/efectos de los fármacos , Ensayo de Inmunoadsorción Enzimática , Gryllidae/genética , Datos de Secuencia Molecular , Neuropéptidos/farmacología , Análisis de Secuencia de ADNRESUMEN
KPNAYKGKLPIGLWamide, a novel member of the GLWamide peptide family, was isolated from Hydra magnipapillata. The purification was monitored with a bioassay: contraction of the retractor muscle of a sea anemone, Anthopleura fuscoviridis. The new peptide, termed Hym-370, is longer than the other GLWamides previously isolated from H. magnipapillata and another sea anemone, A. elegantissima. The amino acid sequence of Hym-370 is six residues longer at its N-terminal than a putative sequence previously deduced from the cDNA encoding the precursor protein. The new longer isoform, like the shorter GLWamides, evoked concentration-dependent muscle contractions in both H. magnipapillata and A. fuscoviridis. In contrast, Hym-248, one of the shorter GLWamide peptides, specifically induced contraction of the endodermal muscles in H. magnipapillata. This is the first case in which a member of the hydra GLWamide family (Hym-GLWamides) has exhibited an activity not shared by the others. Polyclonal antibodies were raised to the common C-terminal tripeptide GLWamide and were used in immunohistochemistry to localize the GLWamides in the tissue of two species of hydra, H. magnipapillata and H. oligactis, and one species of sea anemone, A. fuscoviridis. In each case, nerve cells were specifically labeled. These results suggest that the GLWamides are ubiquitous among cnidarians and are involved in regulating the excitability of specific muscles.
Asunto(s)
Hydra/química , Neuropéptidos/análisis , Neuropéptidos/farmacología , Amidas/análisis , Secuencia de Aminoácidos , Animales , Cnidarios/citología , Relación Dosis-Respuesta a Droga , Hydra/citología , Hydra/efectos de los fármacos , Datos de Secuencia Molecular , Neuropéptidos/química , Biblioteca de PéptidosRESUMEN
Aplysia Mytilus inhibitory peptide-related peptides (AMRPs) are multiple hexapeptides coded on a single precursor. By comparing the AMRP precursors of two species of Aplysia (Aplysia californica and Aplysia kurodai), we found that there are substantial numbers of species-specific AMRPs. We next compared the function of AMRPs on the anterior aorta between A. kurodai and Aplysia juliana. In A. juliana, AMRPs inhibited the contractile activity of the aorta (EC(50)=10(-9) to 10(-8)M), whereas the peptides had no obvious action in A. kurodai up to 10(-7)M. These results indicate that AMRPs are both structurally and functionally diverse neuropeptides even among closely related species.
Asunto(s)
Aplysia/química , Péptidos/química , Péptidos/farmacología , Secuencia de Aminoácidos , Animales , Aorta/efectos de los fármacos , Aorta/fisiología , Secuencia de Bases , Cartilla de ADN , Datos de Secuencia Molecular , Contracción Muscular/efectos de los fármacos , Homología de Secuencia de Aminoácido , Relación Estructura-ActividadRESUMEN
The anterior aorta is one of the largest blood vessels in the marine mollusc Aplysia kurodai. We examined the actions of recently identified neuropeptides, the enterins, on this blood vessel. Immunohistochemistry revealed that the enterin-immunopositive nerve fibers and varicosity-like structures are abundant in the aorta. When the enterins were applied to the aorta, the basal tonus of the arterial muscles was diminished. The enterins also decreased the contraction amplitude of the anterior aorta evoked either by the application of an Aplysia cardioactive peptide, NdWFamide, or by the stimulation of a nerve innervating the aorta (the vulvar nerve). We found that the enterins activate the 4-aminopyridine (4-AP)-sensitive K(+) channels, and thereby hyperpolarize the membrane potential of the aortic muscles. In the presence of 4-AP, the enterins failed to inhibit the muscle contraction evoked by the vulvar nerve stimulation, suggesting that the inhibition is mainly due to the activation of the 4-AP-sensitive K(+) channels. The inhibition of the NdWFamide-evoked contraction by the enterin was not, however, affected by 4-AP. These results suggest that the enterins are involved in inhibitory regulation of the contractile activity of the anterior aorta, and that the inhibition could be due to multiple mechanisms.
Asunto(s)
Aplysia/fisiología , Hormonas de Invertebrados/farmacología , Contracción Muscular/efectos de los fármacos , Músculo Liso Vascular/fisiología , Neuropéptidos/farmacología , Precursores de Proteínas/farmacología , 4-Aminopiridina/farmacología , Animales , Aorta/química , Aorta/inervación , Hormonas de Invertebrados/análisis , Potenciales de la Membrana/efectos de los fármacos , Fibras Nerviosas/química , Neuropéptidos/análisis , Canales de Potasio/efectos de los fármacos , Canales de Potasio/fisiología , Precursores de Proteínas/análisisRESUMEN
Gonadotropin-releasing hormone (GnRH) is the key peptide in the hypothalamo-hypophysial-gonadal axis, the core of regulation of reproduction in vertebrates. In this study, an octopus peptide with structural features similar to vertebrate GnRHs was isolated from brains of Octopus vulgaris. This peptide showed luteinizing hormone-releasing activity in quail anterior pituitary cells. A cDNA encoding the precursor protein was cloned. The RT-PCR transcripts were expressed in the supraesophageal and subesophageal brains, peduncle complex, and optic gland. The presence of the peptide in the different brain region was confirmed with enzyme-linked immunosorbent assay and time-of-flight mass spectrometric analysis. Immunoreactive neuronal cell bodies and fibers were observed in the subpedunculate lobe that controls the optic-gland activity. Optic gland nerves and glandular cells in the optic gland were immunostained. The isolated peptide may be octopus GnRH that contributes to octopus reproduction not only as a neurohormone but also as an endocrine hormone.