[Neurosecretion in several parasitic nematodes].

Parazitologiia

Published: October 1975

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Free endings of peripheral neurosecretory neurons (NNs) were found in the tegument of plerocercoids of five species of parasitic cestodes of fish in an ultrastructural study. The free terminals secreted vesicles on the tegument surface and into the host body. Secretion was experimentally shown to increase in response to the host fish blood serum.

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The neuro-exocrine secretion: A new type of gland in tapeworms?

Zoology (Jena)

October 2023

Lomonosov Moscow State University, Faculty of Biology, Department of Invertebrate Zoology, Moscow 119234, Russia.

The phenomenon of exocrine secretion via nervous cells into the host tissue has been discovered in cestodes. In five cestode species of different orders specialized "cup-shaped" free nerve endings located in the tegument have been found. Their ultrastructure is characterized by the presence of a septate junction, a thin support ring and neurosecretory vesicles 90-110 nm in diameter, which are secreted onto the surface of the tegument through a thin pore.

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The discovery of the ability of the nervous system to communicate through "public" circuits with other systems of the body is attributed to Ernst and Berta Scharrer, who described the neurosecretory process in 1928. Indeed, the immune system has been identified as another important neuroendocrine target tissue. Opioid peptides are involved in this communication (i.

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Neurosecretion involves fusion of vesicles with the plasma membrane. Such membrane fusion is mediated by the SNARE complex, which is composed of the vesicle-associated protein synaptobrevin (VAMP2), and the plasma membrane proteins syntaxin-1A and SNAP-25. Although clearly important at the point of membrane fusion, the precise structural and functional requirements for the transmembrane domains (TMDs) of SNAREs in bringing about neurosecretion remain largely unknown.

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The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C termini of cytosolic SNARE complexes are in apposition, and it involves residues from the vesicle-associated SNARE synaptobrevin 2 that lie close to the cytosol-membrane interface within the full-length protein.

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