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:1.9.3.1 (cytochrome oxidase)
8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The principally mitochondrial enzyme glutamate dehydrogenase (GDH) exhibited low-intensity, uniform immunoreactivity in neurons and intense heterogeneous labeling of glial cells of rat brain. Simultaneous peroxidase labeling for GDH and immunoautoradiography for glial fibrillary acidic protein (GFAP) confirmed the astrocytic localization of the enzyme. Immunoreactivity in astrocytes, but not in neurons, required the presence of Triton X-100 as a solubilizing agent. Most of the intensely labeled glial processes were localized to regions previously reported as containing moderate to high densities of binding sites for the excitatory amino acids, L-glutamate or L-aspartate, and glutamatergic fibers. These included several forebrain regions, such as the superficial layers of the rostral neocortex, dorsal neostriatum, nucleus accumbens, septohippocampal nucleus, intralaminar thalamic nuclei, and external capsules. However, the central gray of the midbrain, the nuclei of the reticular formation, brain stem regions projecting to the cerebellum, and cranial nuclei of the trigeminal and vagal nerves also exhibited intense glial labeling for GDH, even though some of these regions are known to receive only weak glutamatergic projections. A second factor determining the distribution of GDH appeared to be neuronal activity, as assessed by correspondence with reported high densities of cytochrome oxidase. We conclude that GDH enriched in glial populations exists in a subcellular compartment distinct from that of neurons and may serve as one of the enzymes involved in glutamatergic transmission. Deficiencies of glial GDH and the consequent cytotoxic effects of high levels of excitatory amino acids may contribute to a number of neurodegenerative disorders.
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PMID:Regional distribution of astrocytes with intense immunoreactivity for glutamate dehydrogenase in rat brain: implications for neuron-glia interactions in glutamate transmission. 330 25

Single and multiunit mapping was used to determine the extent of the representation of ipsilateral structures in the ventral posterior medial (VPM) nucleus of the thalamus in cynomolgus monkeys. The extent of the VPM occupied by terminations of afferent fibers arising in the ipsilateral principal trigeminal nucleus was also determined by anterograde transport of horseradish peroxidase. Both methods indicate that most of the medial half of VPM is occupied by the ipsilateral representation. This is much larger than previously suspected. Units in the medial half of VPM have small, well localized receptive fields on the ipsilateral side of the lower lip, tongue and palate, in the ipsilateral cheek pouch and on the ipsilateral teeth. The representation is largest for the ipsilateral side of the tongue and the cheek pouch. Most units in the lateral half of VPM have small, contralateral receptive fields. Few units in VPM have bilateral receptive fields. VPM is clearly distinguishable by cytochrome oxidase (CO) staining. Anteroposteriorly elongated, CO-positive aggregations correspond to elongated aggregations of units with the same or closely similar receptive fields, especially in the medial, ipsilateral representation.
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PMID:Extent of the ipsilateral representation in the ventral posterior medial nucleus of the monkey thalamus. 375 48

The callosal connectivity of areas V1 and V2 in the newborn monkey has been investigated with the neuroanatomical tracers wheat germ agglutinin conjugated to horseradish peroxidase and free horseradish peroxidase. In the adult, callosal projecting neurons in cortex subserving the lower parafoveal visual field were found to extend from the V1/V2 border for a distance of 1-2.5 mm into V1 and 8 mm into V2. In the newborn, the tangential extent and total number of callosal projecting neurons were the same as in the adult. Within area V1, callosal projecting neurons in the adult and newborn were limited to supragranular layers. In the adult, axon terminals of callosal projections were located in layers 4B and 5 and were excluded from layer 4C. In the newborn, axon terminals were more extensively distributed than in the adult and invaded layer 4C. In area V2, the laminar distribution and the patchy location of callosal connections in regions of high cytochrome oxidase activity were similar in the newborn and adult animals. In both newborns and adults, the patchy distribution of callosal projections persisted when the neuroanatomical tracers were injected over extensive regions of the contralateral striate and extrastriate cortex. In the adult, area V1 and V2 project contralaterally to two heterotopic sites located in the fundus of the lunate sulcus and the superior temporal sulcus. This was also found to be the case in the newborn. In the adult the terminals of these heterotopic projections were focused in layer 4. This was not the case in the newborn, where after injection limited to the contralateral V1/V2 border they were more evenly distributed among the different cortical layers. Following extensive contralateral injection of tracer, terminals in cortex anterior to V2 were focused over layer 5 and the bottom of layer 4.
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PMID:Callosal connectivity of areas V1 and V2 in the newborn monkey. 380 52

The development of protein bodies in proteinoplasts of tobacco (Nicotiana tabacum L. var. Wis. 38) roots was investigated with TEM, HVEM, and enzyme cytochemistry. These plastids contain a three-dimensional network of fenestrated tubules which originate from invaginations of the inner membrane of the plastid envelope. Elaboration of the network occurs in parallel with cell differentiation: slender tubules common to plastids in meristematic cells undergo dilation as protein accumulates during cell differentiation; proteinoplasts of vacuolate and root cap cells usually contain a large protein body. The contents of the peripheral tubules, originating from the inner membrane, are less electron dense than the tubules making up the central network. Localized dilations within the tubular network result in the formation of dense spheroidal structures, protein bodies, apparently as a result of continued protein accumulation via tubules connecting to the central network. Protein might be imported from segments of rough ER attached to or apposed to the outer membrane of the proteinoplast envelope. The presence of catalase (E.C. 1.11.1.6), peroxidase (E.C. 1.11.1.7), and cytochrome oxidase (E.C. 1.9.3.1) was demonstrated by cytochemistry with diaminobenzidine (DAB) as substrate. Oxidized DAB was found in protein bodies after incubation in each of the specific reaction media. While aminotriazole and sodium azide inhibited oxidation of DAB by catalase and peroxidase, respectively, only potassium cyanide completely inhibited oxidation of DAB in protein bodies. We conclude that protein bodies of proteinoplasts in tobacco roots are not sites for storage of protein, rather protein bodies contain heme protein(s) with strong oxidase activity that may convey a specific function to proteinoplasts.
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PMID:Development and enzyme activity of protein bodies in proteinoplasts of tobacco root cells. 404 99

1. The kinetics of ferrocytochrome c peroxidation by yeast peroxidase are described. Kinetic differences between the older and more recent preparations of the enzyme most probably arise from differences in intrinsic turnover rates. 2. The time-courses of cytochrome c peroxidation by the enzyme follow essentially first-order kinetics in phosphate buffer. Deviations from first-order kinetics occur in acetate buffer, and are due to a higher enzymic turnover rate in this medium accompanied by a greater tendency to autocatalytic peroxidation of cytochrome c. 3. The kinetics of ferrocytochrome c peroxidation by yeast peroxidase are interpreted in terms of a mechanism postulating formation of reversible complexes between the peroxidase and both reduced and oxidized cytochrome c. Formation of these complexes is inhibited at high ionic strengths and by polycations. 4. Oxidized cytochrome c can act as a competitive inhibitor of ferrocytochrome c peroxidation by peroxidase. The K(i) for ferricytochrome c is approximately equal to the K(m) for ferrocytochrome c and thus probably accounts for the observed apparent first-order kinetics even at saturating concentrations of ferrocytochrome c. 5. The results are discussed in terms of a possible analogy between the oxidations of cytochrome c catalysed by yeast peroxidase and by mammalian cytochrome oxidase.
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PMID:Complex-formation between cytochrome c and cytochrome c peroxidase. Kinetic studies. 511 58

Basically the DAB-technique localizes 3 enzymes, i.e. peroxidase, catalase, and cytochrome oxidase, but also pseudoperoxidatic activity of hemeenzymes (hemoglobin, myoglobin, etc.). Although at the ultrastructural level, i.e. in cytochemistry, the appropriate conditions for specific identification of each of these enzymatic activities have been extensively studied and reported in the literature, the subject remains open to investigation. In light microscopy DAB staining has been less thoroughly studied. Since DAB histochemistry might have practical interest in daily diagnostic pathology, it appeared worthwhile to work out a method convenient for paraffin embedded tissues. The method consisted of a prolonged incubation 48 h) of small tissue blocks, which had been prefixed for 1 h in 4% formaldehyde. Dehydration and rehydration occurred in graded ethanols; counterstain was obtained by toluidine blue. Although further experiments are needed to specify the physico-chemical conditions for the three enzymatic activities, the results are morphologically superior to that of frozen sections.
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PMID:Diaminobenzidine histochemistry in light microscopy. 617 Nov 31

The organization of the projection from the lateral geniculate body to the striate cortex in the squirrel monkey has been re-examined using the anterograde and retrograde transport of horseradish peroxidase (HRP) and wheat germ agglutinin conjugated to HRP. The results confirm earlier findings that the projections of the magnocellular and parvocellular layers of the lateral geniculate body terminate in separate sublaminae of layer IV of striate cortex; a more superficial projection of the parvocellular layers to a narrow strip at the base of layer III (IVA in Brodmann's terminology) has also been confirmed. In addition to these well characterized pathways, our results show that the projections of the lateral geniculate body terminate in more superficial levels of layer III and sparsely in layer I of striate cortex. The projections to the upper portion of layer III terminate in distinct patches which coincide precisely with patches of cytochrome oxidase activity previously identified in this zone. The projections to the patches originate primarily from small, pale-staining cells of the "intercalated layers" which surround the magnocellular layers of the lateral geniculate body. A comparison of the organization of the geniculo-cortical projections in the squirrel monkey with that of the cat, Galago, and Tupaia suggests that, despite marked species differences in the laminar organization of the lateral geniculate body and striate cortex, there are striking similarities in the pathway which terminates in the most superficial layers of striate cortex.
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PMID:The laminar organization of the lateral geniculate body and the striate cortex in the squirrel monkey (Saimiri sciureus). 618 1

In primate primary visual cortex, staining for cytochrome oxidase reveals a regular array of blob-like structures, most prominent in layers II and III but also present in layers V and VI. In an attempt to learn more about the input to these blobs, we injected the lateral geniculate bodies of macaques and squirrel monkeys with [3H]proline or horseradish peroxidase and looked in the cortex for transported label. As expected, label was present in layers IVa, IVc alpha, IVc beta, and VI. In addition, both methods revealed an array of puffs deep in layer III. Seen in tangential sections, the puffs precisely matched the cytochrome blobs. These results indicate a projection from the lateral geniculate body to the blob regions deep in layer II/III, either indirect via layer IV or more likely direct. In area 18 stained for cytochrome oxidase, we also observed complex banding patterns; these were remarkably similar to the pattern found after [3H]proline or horseradish peroxidase injection and were also similar to the pattern produced with 2-deoxyglucose labeling after stimulation with vertical or horizontal stripes; the proline and peroxidase labels probably represent a projection from the pulvinar to area 18.
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PMID:Thalamic inputs to cytochrome oxidase-rich regions in monkey visual cortex. 619 14

Staining for the mitochondrial enzyme cytochrome oxidase reveals an array of dense regions (blobs) in the primate primary visual cortex. They are most obvious in the upper layers, 2 and 3, but can also be seen in layers 4B, 5, and 6, in register with the blobs in layers 2 and 3. We compared cells inside and outside blobs in macaque and squirrel monkeys, looking at their physiological responses and anatomical connections. Cells within blobs did not show orientation selectivity, whereas cells between blobs were highly orientation selective. Receptive fields of blob cells had circular symmetry and were of three main types, Broad-Band Center-Surround, Red-Green Double-Opponent, and Yellow-Blue Double-Opponent. Double-Opponent cells responded poorly or not at all to white light in any form, or to diffuse light at any wavelength. In contrast to blob cells, none of the cells recorded in layer 4C beta were Double-Opponent: like the majority of cells in the parvocellular geniculate layers, they were either Broad-Band or Color-Opponent Center-Surround, e.g., red-on-center green-off-surround. To our surprise cells in layer 4C alpha were orientation selective. In tangential penetrations throughout layers 2 and 3, optium orientation, when plotted against electrode position, formed long, regular, usually linear sequences, which were interrupted but not perturbed by the blobs. Staining area 18 for cytochrome oxidase reveals a series of alternating wide and narrow dense stripes, separated by paler interstripes. After small injections of horseradish peroxidase into area 18, we saw a precise set of connections from the blobs in area 17 to thin stripes in area 18, and from the interblob regions in area 17 to interstripes in area 18. Specific reciprocal connections also ran from thin stripes to blobs and from interstripes to interblobs. We have not yet determined the area 17 connections to thick stripes in area 18. In addition, within area 18 there are stripe-to-stripe and interstripe-to-interstripe intrinsic connections. These results suggest that a system involved in the processing of color information, especially color-spatial interactions, runs parallel to and separate from the orientation-specific system. Color, encoded in three coordinates by the major blob cell types, red-green, yellow-blue, and black-white, can be transformed into the three coordinates, red, green, and blue, of the Retinex algorithm of Land.
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PMID:Anatomy and physiology of a color system in the primate visual cortex. 619 95

The tracer, wheat germ agglutinin conjugated to horseradish peroxidase (WGA-HRP), was used as a transneuronal marker in the macaque monkey to study retino-geniculo-striate pathway terminals in area 17. Concomitantly, we stained matching sections for metabolic capacity using the cytochrome oxidase staining technique. Terminal labeling by WGA-HRP and cytochrome oxidase activity staining revealed duplicate patterns in layers II and III, IVA, IVC alpha, IVC beta, and VI. The absence of WGA-HRP-labeled neuronal cell bodies in area 17 supports the conclusion that WGA-HRP is a transsynaptic marker in the macaque visual pathways.
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PMID:Intracortical termination of the retino-geniculo-striate pathway studied with transsynaptic tracer (wheat germ agglutinin-horseradish peroxidase) and cytochrome oxidase staining in the macaque monkey. 620 19


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