Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20366 (substance P)
 21,176 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This investigation was performed to determine whether antisera raised against microtubule-associated proteins, i.e. MAP1 and MAP2, may constitute an alternative to the silver-impregnation studies for the identification of the distinct morphological enteric neuronal cell types in the porcine small intestine. MAP1-immunostaining seems less suited since it preferentially stains the neuronal somata and axons and hardly permits to observe the dendritic processes. MAP2-immunostaining chiefly visualizes the perikaryal-dendritic domain and the proximal part of the axonal processes in the enteric neurons of the porcine gut. Hence, MAP2-immunostaining enables for the first time the unambiguous immunocytochemical identification of enteric multi(short)dendritic uniaxonal type I neurons. Double labelling techniques using antisera against MAP2 and substance P indicate that part of the type I neurons in the myenteric plexus of the porcine small intestine, which are taking part in an ascending pathway, are substance P-immunoreactive, whereas the substance P/neuromedin U-minineurons in the Meissner's plexus do not stain for MAP2. We may conclude that, although MAP2-immunostaining falls short of the quality achieved with silver-impregnation, the possibility to combine MAP2-immunostaining with neuropeptide immunocytochemistry to study the intestinal neurons has the advantage that part of the enteric neuron types stained with a distinct neurotransmitter or neuromodulator can be classified morphologically.
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PMID:Immunohistochemical visualization of the nervous system in the porcine small intestine using antisera raised against the cytoskeletal proteins MAP1 and MAP2, in combination with neuropeptide immunocytochemistry. 172 68

Binding of the peptide neurotransmitter substance P to brain tubulin in vitro inhibits self-assembly of the protein into microtubules and disrupts preassembled microtubules. This cooperative inhibition of the maximum extent of self-assembly by substance P is explicable in terms of preferential binding to the protomer state as compared to the polymer state of tubulin. The inhibition is relieved by the microtubule-associated protein MAP2, which evidently acts in a mixed competitive-noncompetitive fashion. Substance P interacts directly with the isolated C-terminal 4-kDa peptide fragment of tubulin, which appears to contain the specific binding area for MAP2, but is without effect on the self-assembly of the larger (48-kDa) part of the tubulin molecule called S-tubulin. The results are consistent with the C-terminal fragment having a binding site for the cationic substance P as well as for MAP2. However, factors other than electrostatic interaction must be operative, since the sulfoxide of substance P, a derivative with oxidized methionine but similar electrostatic characteristics, is inactive in inhibiting the extent of microtubule assembly.
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PMID:Interaction of substance P with tubulin. 241 40

The evolution of cellular damage over time and the selective vulnerability of different neuronal subtypes was characterized in the striatum following 30-minute middle cerebral artery occlusion and reperfusion in the mouse. Using autoradiography we found an increase in the density of [3H]PK11195 binding sites--likely reflecting microglial activation--in the lesion border at 3 days and in the whole striatum from 10 days to 6 weeks. This was accompanied by a distinct loss of [3H]flumazenil and [3H]CGP39653 binding sites from 10 days up to 6 weeks reflecting neuronal loss. Brain ischemia resulted in a substantial loss of medium spiny projection neurons as seen at three days by Nissl staining, TUNEL and immunocytochemistry using antibodies against microtubule-associated protein (MAP2), NeuN, mu-opioid receptors, substance P, L-enkephalin, neurokinin B, choline acetyltransferase, parvalbumin, calretinin and somatostatin. Both patch and matrix compartments were involved in ischemic damage. In contrast, the numbers of cholinergic, GABAergic, and somatostatin-containing interneurons in the ischemic striatum were not different from those in the contralateral hemisphere at 3 and 14 days. A low density of glutamate receptors, the ability to sequester calcium by calcium-binding proteins and other hitherto unidentified factors may explain this relative resistance of interneurons to acute ischemia.
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PMID:Selective neuronal vulnerability following mild focal brain ischemia in the mouse. 1465 51

Synapses between nociceptive dorsal root ganglion (DRG) neurons and spinal cord dorsal horn neurons represent the first loci for transmission of painful stimuli. Our knowledge of the molecular organization and development of these synapses is sparse due, partly, to a lack of a reliable model system that reconstitutes synaptogenesis between these two neuronal populations. To address this issue, we have established an in vitro assay system consisting of separately purified DRG neurons and dorsal horn neurons on astrocyte microislands. Using immunocytochemistry, we have found that 97%, 93%, 98%, 96%, and 94% of DRG neurons on these microislands express markers often associated with nociceptive neurons including Substance P, TRPV1, calcitonin-gene related peptide (CGRP), TrKA, and peripherin, respectively. Triple labeling with these nociceptive-like markers, synaptic vesicle marker Vglut2 and using MAP2 as a dendritic marker revealed the presence of nociceptive-like markers at synaptic terminals. Using this immunocytochemical approach, we counted contact points as overlapping MAP2/Vglut2 puncta and showed that they increased with time in culture. Single and dual patch-clamp recordings showed that overlapping Vglut2/MAP2 puncta observed after a few days in culture are likely to be functional synapses between DRG and dorsal horn neurons in our in vitro assay system. Taken together, these data suggest our co-culture microisland model system consists of mostly nociceptive-like DRG neurons that express presynaptic markers and form functional synapses with their dorsal horn partners. Thus, this model system may have direct application for studies on factors regulating development of nociceptive DRG/dorsal horn synapses.
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PMID:An in vitro assay system for studying synapse formation between nociceptive dorsal root ganglion and dorsal horn neurons. 2038 65