Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
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Drug
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Target Concepts:
Gene/Protein
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Query: UNIPROT:P20366 (
substance P
)
21,176
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The isolated, spontaneously active portal vein of guinea pig was stimulated by the following compounds (the pD2 is given in parentheses): caerulein (
CER
, 8.02), cholecystokinin octapeptide (CCK-8, 7.59),
substance P
(SP, 4.68), and carbachol (5.37), whereas neurotensin (NT) was ineffective and angiotensin II (AII) produced inhibition. On the portal vein of the rat,
CER
and CCK-8 were ineffective, whereas stimulation occurred with SP (5.72), NT (6.79), AII (7.89), and carbachol (5.50). Tetrodotoxin did not modify these effects in both types of preparation. Cyclic dibutyryl guanosine monophosphate reduced the effect of CCK-8 and
CER
but not that of carbachol. It is concluded that the peptides stimulate the portal vein in a way independent from intramural neurons. It may be speculated that receptors for CCK-8 and
CER
are absent in the portal vein of rat and those for NT in the guinea pig vein.
...
PMID:Cholecystokinin octapeptide, caerulein, substance P, neurotensin, and angiotensin II: species-typical effects on the isolated portal vein of guinea pig and rat. 243 99
We have developed a specific radioimmunoassay for "cerebellin", a 16-amino acid peptide recently isolated from rat cerebellum. In both rat and guinea-pig, cerebellin-like immunoreactivity was highest in the cerebellum but was also present in high concentrations elsewhere in the central nervous system, especially in the hypothalamus. In both species, cerebellin-like immunoreactivity was found in other organs (heart, kidney and stomach) and at lower concentrations in the gastrointestinal tract. In the brain of both species, cerebellin-like immunoreactivity consisted of a single molecular form with an elution position on gel filtration and high-performance liquid chromatography identical to that of synthetic rat cerebellin. However, peripheral tissue contained an additional immunoreactive peak of higher molecular weight.
Cerebellin
was concentrated in synaptosomal preparations of rat brain, and its subcellular distribution pattern in rat brain was identical to that of two other known synaptosomal peptides, vasoactive intestinal polypeptide and
substance P
. Studies with superfused cerebellar synaptosomes and slices of rat cerebellum and hypothalamus demonstrated calcium-dependent cerebellin release when stimulated by high potassium concentrations as well as the addition of the calcium ionophore A23187.
Cerebellin
has therefore a widespread distribution and fulfils two criteria for a neurotransmitter, in that it is found in brain synaptosomes and shows calcium dependent, depolarization-induced release from nervous tissues and isolated nerve endings. It may, therefore, be a component of a novel neurotransmitter system.
...
PMID:Cerebellin-like peptide: tissue distribution in rat and guinea-pig and its release from rat cerebellum, hypothalamus and cerebellar synaptosomes in vitro. 339 60