Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Some parameters of the receptor element from the rat olfactory epithelium are evaluated; it is characterized by high affinity for camphor (KD = 1.5. x 10(-9) M). Triton X-100 has no marked effect on the binding of [3H]camphor. Neither RNAase nor phospholipase C affected [3H]camphor-binding activity. Pronase and trypsin abolished [3H]camphor binding activity by 65 and 40%, respectively. Sulfhydryl reagents decrease the binding of [3H]camphor by a factor of 5--8. The isoelectric point of the receptor solubilized with Triton X-100 is 4.8, as determined by isoelectric focusing. The molecular weight of the receptor as determined by gel electrophoresis is about 120 000. It is proposed that the camphor receptor is a membrane protein containing sulfhydryl groups and playing a key role in olfactory reception.
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PMID:Molecular mechanisms of olfactory reception. IV. Some biochemical characteristics of the camphor receptor from rat olfactory epithelium. 4 3

Binding sites for the dipeptide L-carnosine (beta-alanyl-L-histidine) have been detected in membranes prepared from mouse olfactory bulbs. The binding of L-[3H]-carnosine was saturable, reversible and stereospecific and had a Kd of about 770 nM. The stereospecific binding of L-carnosine represented about 30% of the total binding at pH 6.8, and decreased markedly with increasing pH. Binding was stimulated by calcium, unaffected by zinc, magnesium or manganese and inhibited by sodium and potassium. Carnosine binding was sensitive to trypsin and phospholipases A and C, but not to neuraminidase. Nystatin and filipin, which interact with membrane lipids, also interferred with binding. Some peptide analogues of carnosine were potent inhibitors of binding, but a variety of drugs serving as potent inhibitors in other binding systems had no effect on carnosine binding. Carnosine binding to mouse olfactory bulb membranes was 15-fold higher than that seen in membranes prepared from cerebral hemispheres, 5-fold higher than that seen in membranes prepared from cerebral hemispheres, 5-fold higher than in cerebellum membranes and 3-fold higher than in membranes from spinal medulla and the olfactory tubercle-lateral olfactory tract area. Binding sites for 6 other radiolabeled receptor ligands were also detected in bulb membranes. Peripheral deafferentation of the olfactory bulbs by intranasal irrigation with ZnSO4 led to a loss greater than 90% of the L-[3H]carnosine binding in 4--5 days with much smaller losses in binding of the other 6 ligands over a 180-day observation period. This initial loss of carnosine binding after denervation was due to a loss of binding site stereo-specificity followed by a loss of binding sites. The characteristics of the carnosine binding site in olfactory bulb fulfil 6 of the 7 criteria considered relevant for a functional receptor.
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PMID:Ligand binding studies in the mouse olfactory bulb: identification and characterization of a L-[3H]carnosine binding site. 21 75

During the first 10 days after peripheral deafferentation of the mouse olfactory bulb stereoselective binding of L-[3H]carnosine declines markedly. The initial phase of this decline is due to a decrease in binding site stereoselectivity, which is then followed by a loss of assayable binding sites. The specificity of inhibition of L-[3H]carnosine binding by various peptides is also altered after denervation. Competitive inhibitors of carnosine binding become less potent after denervation, while analogues which are not competitive inhibitors remain equipotent before and after denervation. Several carnosine analogues that are normally poor inhibitors become more potent after denervation. Treatment of bulb membranes with trypsin, RNase and hyaluronidase, but not DNase or collagenase, resulted in significant alterations in carnosine binding. L-, but not D-carnosine, protected the binding site from trypsin digestion, and induced additional binding in bulb membranes in a dose-and temperature-dependent fashion. Preincubation of membranes with L-carnosine also led to the induction of additional carnosine binding in membranes from cerebral cortex, cerebellum and deafferentated bulbs but not from muscle. Bulbs from newborn mice contain about one-half of the adult levels of binding and no significant sex differences in carnosine binding were detected in bulbs from adult rats. L-[3H]carnosine binding was two-fold higher in the anterior compared to the posterior portion of the bulb, but there were no significant differences in binding of opiate, GABA, alpha-adrenergic, muscarinic cholinergic, benzodiazepine of glutamic acid receptor ligands.
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PMID:L-[3H]Carnosine binding in the olfactory bulb. II. Biochemical and biological studies. 48 25

In this morphological and immunohistochemical study we show that olfactory schwann cells (OSC) are derived from precursor cells residing in the olfactory epithelium. During development, they migrate out of the epithelium and extend processes to ensheath the olfactory axons. Olfactory mucosa from E14 rat embryos and juvenile rats were treated with trypsin-pancreatin to remove the underlying connective tissue. The epithelial explant was then maintained for two days in culture, during which cells migrated out from the explant. Among them were spindly bipolar cells which were identified as OSC by their positive immunoreaction for glial fibrillary acidic protein, ultrastructure, and association with growing axons. Axonal growth was significantly more profuse in the embryonic explants, in which the polarity of the OSC was oriented parallel with the axons. Ultrastructural observations showed that ensheathment of the bundles of axons resembled those in vivo.
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PMID:Olfactory Schwann cells are derived from precursor cells in the olfactory epithelium. 189 Jun 98

High concentrations of pregnenolone and its sulfate have been found in several areas of rat and human brain and seem to be controlled by local mechanisms. In the present experiments we have demonstrated pregnenolone binding sites in the cytosolic fraction of the rat olfactory bulb. The pregnenolone binding component showed a Kd = 2.34 +/- 0.66 x 10(-7) M and Nmax = 7.25 +/- 1.20 pmol/mg protein. Pregnenolone, pregnenolone sulfate and 17OH-pregnenolone competed equally for the binding sites while other steroids were less competitive. Protease and trypsin inhibited binding by 48 and 60% respectively. Sucrose density gradient analysis showed a minor peak at 4.6 s and a major one at 3.6 s. After gel filtration chromatography the pregnenolone binding component appeared as 2 peaks corresponding to molecular weights of approximately 150 and 220 kDa. Heating at 60 degrees C increased binding by 150%. These results indicate that the olfactory bulb pregnenolone binding component is complex in nature. Rat plasma also bound pregnenolone. Plasma binding sites could be partially differentiated from those in the olfactory bulb on the basis of susceptibility to lipoprotein lipase, effect of heating and mobility during polyacrylamide gel electrophoresis.
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PMID:Pregnenolone binding sites in the rat olfactory bulb. 232 15

The binding of [125I]physalaemin to rat brain slices was investigated. Radiolabeled physalaemin bound with high affinity (Kd = 0.3 nM) to a single class of sites (Bmax = 22 fmol/mg protein). Kinetic studies indicated that binding was time-dependent and all specific binding was reversible. Pharmacology studies indicated that specific [125I]physalaemin binding was inhibited by structurally related peptides such as substance P and eledoisin. Biochemical studies indicated that specific binding of radiolabeled physalaemin was greatly reduced if the brain slices were pretreated with heat, trypsin or N-ethyl maleimide. Autoradiographic studies indicated that the [125I]physalaemin binding sites were discretely distributed throughout the brain. Highest grain densities were present in the olfactory bulb, dentate gyrus, amygdala, superficial layers of the superior colliculus, subiculum, dorsal parabrachial nucleus, locus coeruleus, nucleus tractus solitarii and dorsal horn of the spinal cord. Moderate grain densities were present in the nucleus accumbens, olfactory tubercle, pyriform cortex, striatum, hippocampus, inferior colliculus and central gray of the midbrain. Low grain densities were present in most thalamic nuclei, the substantia nigra and cerebellum. The corpus callosum and controls treated with 1 microM unlabeled physalaemin had negligible levels of binding. The unique pharmacological and regional distribution data obtained suggest that [125I]physalaemin may serve as a valuable probe to study central substance P receptors.
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PMID:Biochemical characterization and autoradiographic localization of central substance P receptors using [125I]physalaemin. 258 53

Aphrodisin is a protein which is secreted in hamster vaginal discharge and acts via the vomeronasal organ of the accessory olfactory system to elicit copulatory behavior in male hamsters. The complete primary structure of aphrodisin was determined by sequence analysis of intact aphrodisin after unblocking the amino terminus with pyroglutamate aminopeptidase and from peptides generated by trypsin and Lys-C digests. Alignment of the peptides was obtained from sequence analysis of peptides from cyanogen bromide and hydroxylamine cleavages. The protein consists of 151 residues of Mr = 17,000. It has disulfide bonds linking cysteine residues at positions 38 and 42 and at 57 and 149. N-acetylglucosamine residues are linked to asparagines at positions 41 and 69. Based on its similarity to the major urinary proteins in rats and mice, aphrodisin is a putative member of the alpha 2u-globulin superfamily of extracellular proteins.
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PMID:The primary structure of aphrodisin. 318 9

A previous study of cholinergic development indicated a possible trophic relationship between the olfactory bulb and its afferents from the basal forebrain (Large et al., J. Neurochem., 46 (1986) 671-680). To examine this possibility further, cultured embryonic basal forebrain neurons from rat were used as a test system for trophic factor activity hypothesized to be present in olfactory bulb. Basal forebrain neurons grown in defined medium typically died within 2-3 days. However, survival and differentiation were strikingly enhanced by soluble extracts of olfactory bulb tissue. This trophic effect was noticeable with 2 micrograms/ml olfactory bulb protein, and plateaued at 100 micrograms/ml. The activity was heat- and trypsin-sensitive, non-dialyzable, stable in the cold, resistant to NGF antiserum, and approximately 100-150 kDa in size. Nerve growth factor, bovine serum albumin, laminin and extracts from heart did not mimic the activity. Long-term growth (21 days) in the presence of olfactory bulb proteins resulted in extensive neurite production, formation of thick neurite fascicles, and aggregation of cells. Some glia were present, as evidenced by the presence of glial fibrillary acidic protein, and large numbers of cells were positive for neuron-specific enolase and true acetylcholinesterase. Trophic activity was also present in medium conditioned by olfactory bulb slices, implying secretion of active factors.
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PMID:Soluble proteins from rat olfactory bulb promote the survival and differentiation of cultured basal forebrain neurons. 340 3

The sensory neurons of the olfactory epithelium form an anatomically uniform population but are differentially excited by odorants. We have discovered an unexpected biochemical heterogeneity within this population that extends to its axonal projection onto the olfactory bulb. This heterogeneity is recognized by a newly generated monoclonal antibody, designated RB-8, that differentially stains the primary olfactory projection in rats and divides it into 2 nonoverlapping zones. With light-microscopic immunohistochemistry, RB-8 densely labels the fascicles of the olfactory nerve from the ventral and lateral parts of the olfactory epithelium, where there is also some epithelial staining. This area, which we designate RB-8-positive, comprises about two-thirds of the epithelial sheet. RB-8 labeling of the other third of the epithelium, which includes the dorsal recess and medial tips of the dorsal turbinals, is not detectable, and the fascicles from these RB-8-negative areas are only weakly stained. These RB-8-negative areas form a contiguous zone on flattened maps of the epithelial sheet. In the olfactory bulb, RB-8 staining of the glomeruli in the ventrolateral part is correspondingly dense, while that in the dorsomedial glomeruli is undetectable or very light. In the labeled glomeruli, the RB-8 staining is precisely coextensive with anti-olfactory marker protein staining, which serves as a marker for the olfactory axons and terminals. In addition, knife-cut lesions of the olfactory nerve totally eliminate the RB-8 staining in the glomeruli where the destruction of the olfactory terminals is complete. There is also a good correlation between the staining patterns in the bulb and epithelium and what is known from tract-tracing studies of the arrangement of the axonal projection of the epithelium onto the bulb. This evidence strongly suggests that, in the olfactory nerve and glomeruli, RB-8 stains the olfactory axons and their terminals. A survey of the CNS and peripheral tissues demonstrates that staining with RB-8 is nervous system-specific; not all components of the CNS and PNS are stained. The antigen recognized by RB-8 was characterized in immunoblots and by use of a direct radioimmunoassay (RIA) which assessed binding of 125I-RB-8. With this assay, the RB-8 binding sites in whole brain are shown to be membrane-associated, saturable, immunologically specific for RB-8, and trypsin-sensitive. In SDS-PAGE immunoblots of membrane proteins, the antigen in rat forebrain and in the olfactory nerve is a protein of 125 kDa Mr, which comigrates in mixtures of membranes from the 2 sources.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:The primary olfactory projection has two chemically distinct zones. 377 38

Recent studies have suggested that diffusible factors released by neural target tissues enhance survival, growth, and differentiation of neurons within the central, as well as the peripheral, nervous system. In this report, we use catecholamine cytofluorescence to demonstrate that a soluble factor from the striatum produces a 4-fold increase in number of catecholamine cytofluorescent-positive dopaminergic neurons in dissociated mesencephalon cultures prepared from embryonic 14-day-old rats. The same soluble extract enhances the number of neurites per cell and the length of neurites, and also produces a greater than 3.5-fold stimulation of high affinity dopamine uptake into neurons. Such stimulation is significantly reduced following trypsin treatment. The trophic effects on dopaminergic neurons are maximal in extracts of the striatum, but are also found in extracts of the hippocampus-entorhinal cortex-amygdaloid nucleus and the cerebral cortex, although they are less in extracts of the cerebellum, negligible in the olfactory bulb, and absent in the liver. With molecular sieving chromatography, the soluble factors stimulating high affinity dopamine uptake are partially separable from the factors stimulating neuronal high affinity GABA uptake. The approximate molecular weight of the factors influencing dopaminergic neurons is 1500-2200 Da.
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PMID:Soluble striatal extracts enhance development of mesencephalic dopaminergic neurons in vitro. 380 14


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