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)

A variety of histochemical findings have contributed to a more differentiated architectonical description of the bed nucleus of the stria terminalis (BNST) in the mammalian brain. However, in the human brain investigations of the chemoarchitecture of this nucleus have been rare. Therefore we chose this region in six human autopsy brains in order to map the distribution patterns of 13 immunohistochemical markers for neurotensin (NT), neuropeptide Y (NPY), somatostatin (SOM), enkephalins (ENK), vasoactive intestinal polypeptide (VIP), substance P (SP), neurophysins (NPH), glial fibrillary acid protein, 3-fucosyl-N-acetyl-lactosamine epitope, myelin basic protein (MBP), calbindin (CAB), synaptophysin (SYN) and chromogranin-A (CHR-A). Three chemoarchitectonically distinct areas could be defined. The lateral subdivision of the BNST contained high amounts of NPY and SP-fibre immunoreactivity and was further characterized by the occurrence of neurons labelled for NPY. The central subdivision of the BNST appeared as a histochemically clearly circumscribed compartment with massive fibre immunoreactivity for SOM, ENK, VIP, SYN, CHR-A, CAB as well as SOM, ENK, NT and CAB positive cells but lacked cytosolic or fibre-like immunolabel for NPY and SP. This structure was also ensheathed by myelinated fibres identified by means of MBP immunohistochemistry. The medial subdivision of the BNST showed moderate to high SP and NPY fibre immunoreactivity but lacked immunolabelled neurons and was only scarcely supplied with varicose or punctiform ENK immunoproduct. In the most posterior levels of our sections a cell group labelled for NPH was located lateral to the fornix columns. The lateral subdivision of the BNST (with NPY, SYN) and mainly the central BNST (with SOM, ENK, VIP, SYN and CHR-A) contributed to ventrolateral extensions of dense patchy fibre immunoreactivity throughout the basal forebrain region.
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PMID:Differential distribution of immunohistochemical markers in the bed nucleus of the stria terminalis in the human brain. 171 18

Substance P (SP), S-100 protein, methionine-enkephalin, serotonin and myelin basic protein were studied in two solitary glomus tumours of the skin by peroxidase-antiperoxidase immunohistochemistry. Multiple SP-containing nerve fibres were distributed in the parenchyma of the tumour among proliferating glomus cells, and in the oedematous stroma of the tumour. Positive staining for myelin basic protein was detected in nerve fascicles in the capsule of the tumour, but not within the glomus tumour. S-100 protein immunoreactivity was found in nerve fascicles in the capsule of the tumour, and in addition, a few cells positive for S-100 protein were scattered throughout the stroma of the tumour. No positive staining for methionine-enkephalin and serotonin was found. The present finding may explain the clinical experience that the tumour is tender and can cause severe paroxysmal pain, because SP is known to be a primary sensory afferent neurotransmitter for mediating nociception. A possible role of SP for vasodilation in the glomus tumour is also discussed.
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PMID:Immunohistochemical demonstration of substance P-containing nerve fibres in glomus tumours. 241 Dec 82

Non-hairy and hairy human skin were investigated with the use of the indirect immunohistochemical technique employing antisera to different neuronal and non-neuronal structural proteins and neurotransmitter candidates. Fibers immunoreactive to antisera against neurofilaments, neuron-specific enolase, myelin basic protein, protein S-100, substance P, neurokinin A, neuropeptide Y, tyrosine hydroxylase and vasoactive intestinal polypeptide hydroxylase and vasoactive intestinal polypeptide (VIP) were detected in the skin with specific distributional patterns. Neurofilament-, neuron-specific enolase-, myelin basic protein-, protein S-100, neuropeptide Y-, tyrosine hydroxylase- and vasoactive intestinal polypeptide (VIP)-like immunoreactivities were found in or in association with sensory nerves; moreover, neuron-specific enolase-, myelin basic protein-, protein S-100, neuropeptide Y-, tyrosine hydroxylase- and vasoactive intestinal polypeptide (VIP)-like immunoreactivities occurred in or in association with autonomic nerves. It was concluded that antiserum against neurofilaments labels sensory nerve fibers exclusively, whereas neuron-specific enolase-, myelin basic protein- and protein S-100-like immunoreactivities are found in or in association with both sensory and autonomic nerves. Substance P- and neurokinin A-like immunoreactivities were observed only in sensory nerve fibers, and neuropeptide Y- and tyrosine hydroxylase-like immunoreactivities occurred only in autonomic nerve fibers, whereas vasoactive intestinal polypeptide (VIP)-like immunoreactivities was seen predominantly in autonomic nerves, but also in some sensory nerve fibers.
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PMID:Sensory and autonomic innervation of non-hairy and hairy human skin. An immunohistochemical study. 241 23

Antisera raised against porcine myelin basic protein (MBP) in Syrian hamsters were assayed by an ELISA method. The specificity of a high-titered antiserum was probed with synthetic peptides representing a hexapeptide and a decapeptide of the JC virus (JCV) large T-antigen C-terminus which is homologous to the MBP triproline region, a decapeptide from MBP which is encephalitogenic in guinea pigs, and peptides unrelated to MBP, i.e., substance P and poly-L-lysine. In an ELISA inhibition assay, preincubation of the hamster antiserum to MBP with either the JCV T-antigen C-terminal decapeptide or the encephalitogenic determinant inhibited binding activity in a dose-dependent manner. In contrast, the T-antigen C-terminal hexapeptide, substance P, and poly-L-lysine were not inhibitory. These results suggest that the triproline region of MBP can be immunogenic in hamsters, and support the concept that a conformation of the MBP triproline region is shared with certain of its viral homologues. In an effort to detect similar cross-reactive specificities in hamster antisera to JCV T-antigen, sera of 50 hamsters bearing subcutaneous tumors induced by JCV-transformed glial cells were tested for ability to bind to MBP in the ELISA assay. While significant increases in response compared to prebleed levels were observed in about one-fourth of the sera, some of them showed similar increases in binding to other basic proteins such as histones, and the binding to MBP was not inhibited by the triproline-containing decapeptide.
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PMID:Inhibition of binding of hamster antibody to myelin basic protein by a synthetic triproline-containing peptide from JC virus T-antigen. 243 49

The differentiation of intracerebral and intraspinal transplants of fetal (E14-E15) rat spinal cord was studied to determine the extent to which myelin-free zones in these embryonic grafts exhibit cytological features and immunocytochemical characteristics of the substantia gelatinosa (SG) of the normal spinal cord. Immunocytochemical staining with antiserum to myelin basic protein (MBP) revealed myelin-free areas of varying proportions within fetal spinal cord grafts. These regions were identified in both newborn and adult recipients regardless of whether donor tissue was grafted to heterotopic (intracerebral) or homotopic (intraspinal) sites. As in the SG of the intact spinal cord, the myelin-free regions consisted mainly of small (7-15 microns) diameter neurons. At the ultrastructural level, these cells were surrounded by a neuropil composed of numerous small caliber, unmyelinated axons and intermediate-sized dendrites. Synaptic terminals in these areas were primarily characterized by the presence of clear, round vesicles, although granular vesicles were occasionally found within these terminals. Immunocytochemical staining demonstrated met- and leu-enkephalin-, neurotensin-, substance P-, and somatostatin-like immunoreactive elements within these myelin-free areas. Thus, regions within embryonic spinal cord grafts undergo some topographical differentiation which parallels that of the normal superficial dorsal horn. The presence of SG-like regions illustrates the potential capacity of fetal spinal cord transplants for replacing some intraspinal neuronal populations at the site of a spinal cord injury in neonatal and adult animals. These graft regions may serve as a source of intersegmental projection neurons or establish an extensive intrinsic circuitry similar to that seen in the normal SG. In addition, the definition of these areas provides a useful model to study the innervation patterns of host axons that typically project to the substantia gelatinosa of the normal spinal cord.
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PMID:Differentiation of substantia gelatinosa-like regions in intraspinal and intracerebral transplants of embryonic spinal cord tissue in the rat. 291 47

Calmodulin, a ubiquitous Ca2+-binding regulatory protein, is phosphorylated exclusively on tyrosine-99 in an insulin-dependent manner by wheat germ lectin-purified preparations of insulin receptors from rat adipocyte plasma membranes. Calmodulin is phosphorylated in the presence of polylysine, histone Hf2b, and protamine sulfate, but not in the absence of these cofactors or in the presence of other basic compounds known to interact with calmodulin, such as mellitin, myelin basic protein, chlorpromazine, trifluoperazine, substance P, glucagon, polyarginine, mastoparin, beta-endorphin, spermine, spermidine, and putrescine. The incorporation of 32P into calmodulin, expressed in terms of moles of phosphate per moles of calmodulin and assayed at calmodulin concentrations of 1.2 and 0.06 microM, is 0.023 + 0.002 and 0.046 + 0.006, respectively. This low stoichiometry is likely due to the relative impurity of the receptor preparation, as similar studies not shown here, using highly purified human insulin receptors, yield a stoichiometry of 1 mol phosphate/mol calmodulin. The time course of phosphorylation is characterized by a short initial lag phase of approximately 5 min, a rapid linear rate from approximately 5 to 40 min, with a steady state of 32P incorporation being approached at approximately 60 min. The K0.5 for ATP is 104 + 18 microM. Phosphorylated calmodulin is partially purified by HPLC on a C4 column using a trifluoroacetic acid/acetonitrile gradient solvent system. Phosphoamino acid analysis and limited thrombin digestion were used to determine that the site of insulin-induced phosphorylation of calmodulin is exclusively on tyrosine-99 regardless of the basic protein cofactor used. Phosphorylated calmodulin does not exhibit the characteristic Ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule. Thus, the tyrosine phosphorylation of calmodulin represents a potentially important post-translational modification altering calmodulin's ability to regulate a variety of enzymes involved in growth, differentiation, and metabolic regulation.
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PMID:The in vitro phosphorylation of calmodulin by the insulin receptor tyrosine kinase. 341 47

Purified rat brain cathepsin B (EC 3.4.22.1) converted prodynorphins or proenkephalins to shorter active forms by the preferential removal of C-terminal dipeptides. The substrate affinities for Met-enkephalin-Arg-Phe or -Arg-Gly-Leu were Km 46 and 117 microM, and kcat/Km ratios were 67 and 115 microM-1, min-1, respectively. Met-Enkephalin was inactivated by the same mechanism (Km-450 microM; kcat/Km = 0.12 microM-1 min-1). The comparison of cathepsin B hydrolysis for pro-opioids, a synthetic hexapeptide and its fragments, C-blocked peptides (pro-opioid amides, Met-enkephalin amide, substance P), and bovine myelin basic protein, provided information on the influence of the C-terminal residues on dipeptide release, the rates as correlated to peptide length, and the optimal arrangement of residues favoring scission at the P1-P'1 sites. The brain enzyme was stereospecific and did not act on peptides with C-terminal D-amino acid substituents. Arg hindered and Pro blocked the release of C-terminal dipeptides when in the P'2 positions. The suppression of dipeptide release by agents inhibiting endopeptidase actions such as E-64 and leupeptin, and the endogenous brain factor (cerebrocystatin) point to similar catalytic mechanisms for the exopeptidase action.
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PMID:Preferential action of rat brain cathepsin B as a peptidyl dipeptidase converting pro-opioid oligopeptides. 353 Jan 35

1. A thiol proteinase from human pituitaries was purified approximately 400 fold and shown to have different chromatographic properties from that of calf brain. Among substrates cleaved were myelin basic protein, histones, beta-lipotropin, neurophysin, and Substance P. 2. The enzyme showed properties associated with a cathepsin-B like enzyme: dependence on -SH groups, pH optimum of 6.5, inhibition by leupeptin and a synthetic analog, Boc-D-Phe-Pro-arginal, and cleavage of dipeptidyl arylamides with basic residues adjacent to or penultimate to the chromatographic grouping. 3. Membranes present in the P2 fraction of rat brain contained three or more enkephalinases when submitted to DEAE-cellulose chromatography. Further purification on an IgG-Sepharose affinity column prepared with antibody to lung angiotensin converting enzyme indicated the presence of dipeptidyl carboxypeptidase(s) with properties distinct from those of ACE. In addition, the DEAE-cellulose fractions contained various aminopeptidase activities when tested with Leu-Gly-Gly, Leu-Nap, and Ala-Ala-Nap as substrates.
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PMID:Peptide processing in the central nervous system. 625 8

Calmodulin (CaM) binding by turkey gizzard myosin light chain kinase (MLCK) causes subtle changes in the fluorescence emission and polarization excitation spectra of the enzyme. Fluorescence experiments using 9-anthroyl-choline (9AC), which competes with ATP in binding, demonstrate mutually stabilizing interactions between the CaM and ATP binding sites corresponding to delta G = -0.6 to -0.7 kcal/mol. Fluorescence titrations in the presence of 9AC or 5,5'-bis[8-(phenylamino)-1-naphthalenesulfonate] confirm the stoichiometry of 1 mol of CaM/MLCK. Phosphorylation of MLCK has no effect on either the protein fluorescence or the binding of ATP and 9AC. The dissociation constant for the MLCL-CaM complex is increased approximately 500-fold on phosphorylation. Values of Kd for the phosphorylated enzyme range from 0.5 to 1.1 microM in 0.2 N KCl, pH 7.3, 25 degrees C. We showed competition between MLCK and other CaM binding proteins and peptides by using both fluorescence and catalytic activity measurements. Competition for CaM occurs with ACTH, beta-endorphin, substance P, glucagon, poly(L-arginine), myelin basic protein, troponin I, and histone H2A. Phosphorylation of the last three proteins by the adenosine cyclic 3',5'-phosphate dependent protein kinase diminishes their ability to compete. Phosphorylation of MLCK by the protein kinase gives 0.95 +/- 0.04 and 2.2 +/- 0.4 mol of incorporated 32P in the presence and absence of CaM, respectively. These stoichiometries agree with those recently reported [Conti, M. A. & Adelstein, R. S. (1981) J. Biol. Chem. 256, 3178].
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PMID:Functional interactions between smooth muscle myosin light chain kinase and calmodulin. 689 95

Neuropathological and immunohistochemical studies were done on the brain-stem of neonates who had congenital hydrocephalus with aqueductal stenosis or Arnold-Chiari malformation (ACM). The infants with aqueductal stenosis showed heterogeneity in their clinicopathological findings while the infants with ACM were relatively similar in neuropathological findings. There were prominent astrogliosis, decreased immunoreactivity with antisera to tyrosine hydroxylase and myelin basic protein in the periaqueductal area, and an increased reactivity with antiserum to substance P in the tegmentum of most patients with aqueductal stenosis and other malformations. In ACM, there was little gliosis in the tegmentum and periaqueductal area and minimal immunoreactivity of tyrosine hydroxylase, myelin basic protein and substance P. In both groups of cases, the cells in the periaqueductal region differ in neurotransmitter/neuromodulator immunoreactivity and degree of myelination reflecting a difference possibly in their maldevelopment.
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PMID:Neuropathology and immunohistochemistry of the brain-stem in neonates with congenital hydrocephalus: comparative studies between aqueductal stenosis and Arnold-Chiari malformation. 752 58


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