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Occurrence of neuropeptides and tyrosine hydroxylase in the olfactory epithelium of the lesser-spotted catshark (Scyliorhinus canicula Linnaeus, 1758).
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Immunohistochemical studies using antisera against various neuropeptides (Substance P, vasoactive intestinal polypeptide, and cholecystokinin octapeptide) and tyrosine hydroxylase revealed both olfactory sensory neuron (OSN) polymorphisms and transepithelial-subepithelial nerves in the olfactory
High Expression of EphA4 Predicted Lesser Degree of Tumor Regression after Neoadjuvant Chemoradiotherapy in Rectal Cancer.
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Background: Numerous transmembrane receptor tyrosine kinase pathways have been found to play an important role in tumor progression in some cancers. This study was aimed to evaluate the clinical impact of Eph receptor A4 (EphA4) in patients with rectal cancer treated with neoadjuvant concurrent
Temporal and spatial organization of tyrosine hydroxylase-immunoreactive cell groups in the embryonic brain of an elasmobranch, the lesser-spotted dogfish Scyliorhinus canicula.
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We have studied the development of catecholaminergic (CA) neuronal groups in the brain of the dogfish Scyliorhinus canicula using immunohistochemistry to tyrosine hydroxylase (TH). The earliest TH-immunoreactive (THir) cells were detected in the primordia of the posterior tubercle and
Immunohistochemical study of the distribution of endocrine cells in the gastrointestinal tract of the lesser mouse deer (Tragulus javanicus).
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The occurrence and distribution of endocrine cells in the gastrointestinal tract of the lesser mouse deer, Tragulus javanicus, were studied immunohistochemically. Fourteen types of endocrine cells immunoreactive for serotonin, somatostatin, enteroglucagon, pancreatic glucagon, bovine pancreatic
Analysis of EphA4 in the lesser spotted catshark identifies a primitive gnathostome expression pattern and reveals co-option during evolution of shark-specific morphology.
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The Eph family is the largest known group of structurally related receptor tyrosine kinases (RTKs). Each Eph receptor has a specific Ephrin ligand, and these function to define spatial boundaries during development. Analyses of EphA4 in mouse, chick, frog and zebrafish embryos have implicated this
Protein-bound D-amino acids, and to a lesser extent lysinoalanine, decrease true ileal protein digestibility in minipigs as determined with (15)N-labeling.
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Heat and alkali treatment of food may increase the concentrations of protein-bound D-amino acids and cross-links such as lysinoalanine (LAL). To examine how protein treatment affects digestibility, purified test meals [total protein 150 g/kg dry matter (DM), 0.44 MJ/(kg BW(0.75). d)] were prepared,
Tyrosine hydroxylase immunoreactivity in cerebellar Purkinje cells of the rat.
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Employing tyrosine hydroxylase (TH) immunohistochemistry, we have revealed that TH immunoreactivity occurs in cerebellar Purkinje cells in the rat. These TH-immunoreactive Purkinje cells were distributed predominantly in the crus I & II ansiform lobules and the paraflocculus, and to a lesser extent
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) administration to C57-black mice leads to parallel decrements in neostriatal dopamine content and tyrosine hydroxylase activity.
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The administration of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) to C57-black mice (4 doses of 20 mg/kg, at 2 h intervals) led to a large decrement in the neostriatal content of dopamine (92%) and a parallel decrease in tyrosine hydroxylase activity (91%). MPTP administration also caused
Tyrosine hydroxylase-like (TH) immunoreactivity in human mesolimbic system.
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A practical methodology has been described for the use of human postmortem brain tissue in both tyrosine hydroxylase and dopamine beta-hydroxylase immunohistochemistry in which in situ perfusion with paraformaldehyde is followed by immersion fixation in Bouin's fixative. These studies indicate that
Tyrosine hydroxylation in the rat striatum after fentanyl and droperidol in vivo.
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The effects of fentanyl, droperidol, and morphine on tyrosine hydroxylation in the rat striatum was measured after inhibition of aromatic amino acid decarboxylase with R04-4602. Any direct change in the product of hydroxylation (i.e.dopa) was supposed to reflect a change in enzyme activity. Fentanyl
Phosphorylation of the lysosomal enzyme binding receptor protein from monkey brain and evidence for a tyrosine kinase activity associated with it.
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The lysosomal enzyme binding receptor protein prepared from monkey brain by phosphomannan-Sepharose affinity chromatography could undergo phosphorylation in the presence of [gamma-32P] ATP. The phosphorylated receptor protein appeared as a single radioactive band on polyacrylamide gel
Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene.
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A new human gene encoding a putative receptor-type tyrosine kinase (RTK) was isolated by screening a placenta cDNA library with a mouse Flt3 probe. The deduced amino acid sequence of the intracellular region of the molecule showed that it was strongly related to the FLT1 and KDR/FLK1 gene products
Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src.
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A mutant in src, the oncogene of Rous sarcoma virus, has been constructed in which the major phosphorylated tyrosine (Tyr-416, located in the carboxy-terminal half of the protein) has been replaced by phenylalanine. Mouse cells transformed with this mutant src form foci and grow in soft agar,
The dephosphorylation characteristics of the receptors for epidermal growth factor and platelet-derived growth factor in Swiss 3T3 cell membranes suggest differential regulation of receptor signalling by endogenous protein-tyrosine phosphatases.
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Comparison of the phosphotyrosine-specific dephosphorylation of the autophosphorylated receptors for epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) in Swiss 3T3 cell membranes by the endogenous phosphatases revealed striking differences. EGF receptor dephosphorylation was
Partial purification of a tyrosine kinase activity associated with a 28-kDa phosphoprotein from the particulate fraction of rat spleen.
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A phosphoprotein with associated tyrosine kinase activity has been purified from a 26,000 x g particulate fraction of rat spleen. The molecular weight of the native kinase is 85-90 kDa as estimated by gel permeation chromatography on Superdex 200 while SDS/PAGE of an autophosphorylated sample
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