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M R Celio

Publications and source records attributed to M R Celio.

At least 91 records · Page 5Linked to original sources
PubMed1990

Distribution of parvalbumin immunoreactivity in the visual cortex of Old World monkeys and humans.

The macaque visual system has been frequently used as a model for understanding functional aspects of human vision. There are, however, few studies directly comparing biochemically defined neuronal populations in the visual cortex of the two species. In this study we compared the distribution and morphological features of the parvalbumin-immunoreactive neuronal subpopulation within humans and Old World monkeys (Macaca fascicularis and Macaca mulatta) by using monoclonal antibodies against the Ca2(+)-binding protein parvalbumin (PV), a neuronal marker in the vertebrate cerebral cortex. Characteristic laminar density and distribution of PV is observed, matching that seen with cytochrome C-oxidase and gamma-aminobutyric acid (GABA) immunoreactivity. Thus, parvalbumin is prominent in the layers receiving afferents from the dorsal lateral geniculate nucleus. Terminal fields are rich in layer IVA and IVC and moderate in the blob-region of layer II-III of the monkey cortex. In the human visual cortex only layer IVC displays rich terminal fields. Parvalbumin is present in neurons within all layers of the cortex except layer I. Parvalbumin-immunoreactive (PV-ir) axons occur in different lamellae of the white matter containing axons belonging to association or projection neurons. The estimation of PV-ir neurons, determined for 50 microns-wide columns through the thickness of area 17, shows that the percentage of the total neuron number in area 17 of humans containing PV is 6.8 +/- 2.0%, and in the macaque monkey, 11.5 +/- 2.9%. The perikaryal area of PV-ir neurons varies according to the layer and is comparable in humans (109.3 +/- 40.8 microns2) and monkeys (94.3 +/- 29.5 microns2). However, the relative number of large PV-ir neurons is higher in humans. The immunoreactive product fills the thinnest cell processes and the shape of PV-ir neurons can be easily traced with the aid of a camera lucida. The shape of the neurons is similar in the two species studied, and they probably belong to non-spiny stellate, double-bouquet, chandelier, and basket cell classes. This study shows that parvalbumin acts as a marker for a subpopulation of interneurons in area 17, but it is also present in the geniculocortical as well as in corticocortical pathways. Moreover, the Old World monkey and human visual cortices have a similar, but not identical, distribution of this important calcium-binding protein.

Animals↗
PubMed1990

Ca2(+)-dependent mobility shift of parvalbumin in one- and two-dimensional gel-electrophoresis.

Under Ca2(+)-loaded conditions parvalbumin migrates in one- and two-dimensional gel-systems as a double-band or -spot whereas in Ca2(+)-free condition it appears as one band or spot. Parvalbumin (PV), a member of the family of calcium-binding proteins [1], was first described in 1934 [2] and occurs in fast-contracting muscles and in subpopulations of neurons in vertebrates and humans [3,4,5]. The physical characteristics of molecular weight (Mv 12 KD), isoelectric point (pI 4.9) and Ca2(+)-binding properties are established (PV binds 2 Ca2+ per molecule) [5,6]. Physiological roles discussed for PV range from trigger- to buffer-protein of intracellular Ca2(+)-ions [7]. In this paper we report an as yet not described mobility shift of PV in gel-electrophoresis after manipulation of the Ca2+ concentration, which may have implications for its physiological function.

Animals↗
PubMed1990

Monoclonal antibodies directed against the calcium binding protein Calbindin D-28k.

We have produced 25 clones secreting antibodies directed against chicken Calbindin D-28k. Two of them, 300 and 318, recognize determinants conserved in fish, chicken, mouse, rat, rabbit, monkey and human Calbindin D-28k. We demonstrate their use in the immunohistochemical localization of Calbindin D-28k, and in the detection of Calbindin D-28k on immunoblots.

Animals↗
PubMed1990

Calbindin D-28k and parvalbumin in the rat nervous system.

This paper describes the distribution of structures stained with mono- and polyclonal antibodies to the calcium-binding proteins calbindin D-28k and parvalbumin in the nervous system of adult rats. As a general characterization it can be stated that calbindin antibodies mainly label cells with thin, unmyelinated axons projecting in a diffuse manner. On the other hand, parvalbumin mostly occurs in cells with thick, myelinated axons and restricted, focused projection fields. The distinctive staining with antibodies against these two proteins can be observed throughout the nervous system. Calbindin D-28k is primarily associated with long-axon neurons (Golgi type I cells) exemplified by thalamic projection neurons, strionigral neurons, nucleus basalis Meynert neurons, cerebellar Purkinje cells, large spinal-, retinal-, cochlear- and vestibular ganglion cells. Calbindin D-28k occurs in all major pathways of the limbic system with the exception of the fornix. Calbindin D-28k is, however, also found in some short-axon cells (Golgi type II), represented by spinal cord interneurons in layer II and interneurons of the cerebral cortex. It is also detectable in some ependymal cells and abundantly occurs in vegetative centres of the hypothalamus. The "paracrine core" of the nervous system and its adjunct (1985, Nieuwenhuys, Chemoarchitecture of the Brain. Springer, Berlin) is very rich in calbindin D-28k. The distribution of calbindin D-28k-positive neurons is very similar to that of the dihydroperydine subtype of calcium channels. Most of the cells containing calbindin D-28k are vulnerable to neurodegenerative processes. Parvalbumin-immunoreactive neurons have a different, and mostly complementary distribution compared with those which react with calbindin D-28k antisera, but in a few cases (Purkinje cells of the cerebellum, spinal ganglion neurons), both calcium-binding proteins co-exist in the same neuron. Many parvalbumin-immunoreactive cells in the central nervous system are interneurons (Golgi type II) and, to a lesser extent, long-axon cells (Golgi type I), whereas conditions are vice versa in the peripheral nervous system. Intrinsic parvalbuminic neurons are prominent in the cerebral cortex, hippocampus, cerebellar cortex and spinal cord. Long-axon parvalbumin-immunoreactive neurons are, for example, the Purkinje cells, neurons of the thalamic reticular nucleus, globus pallidus, substantia nigra (pars reticulata) and a subpopulation among large spinal-, retinal-, cochlear- and vestibular ganglion cells. Parvalbumin is rich in cranial nerve nuclei related to eye movements. In addition to nervous elements, parvalbumin immunoreactivity occurs in a few ependymal cells and in some pillar cells of the organ of Corti.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1989

Age-dependent supersensitivity to the glycogenolytic effect of K+ in the cerebral cortex of the spontaneously epileptic quaking mouse mutant.

K+, at concentrations reached in the extracellular space during neuronal activity (5-10 mM), promotes a time- and concentration-dependent hydrolysis of [3H]glycogen newly synthesized by mouse cerebral cortical slices. In the present study, the glycogenolytic action of K+ was examined in the neocortex of the quaking mouse, a spontaneously epileptic mutant characterized by deficient myelination of the CNS. The potency and efficacy of K+ in eliciting glycogen hydrolysis was greatly enhanced in cerebral cortical slices prepared from homozygous quaking mice (qk/qk) older than 7 weeks of age, indicating a supersensitive response to a metabolic action of the ion. A detailed ontogenic analysis showed an evolution of the supersensitive response to K+ which is reminiscent of the previously described increase in the number of alpha 2-adrenoreceptors in the brainstem of this mutant. In contrast to the altered response to K+, the glycogenolytic action of noradrenaline and vasoactive intestinal peptide reported earlier was equally expressed in qk/qk and in their unaffected littermates.

Aging↗
PubMed1989

Parvalbumin increases in the caudate putamen of rats with vitamin D hypervitaminosis.

The influence of chronic vitamin D3 application on the concentration of the four calcium-binding proteins parvalbumin, the 28-kDa calbindin-D, calmodulin, and S-100 was studied in various brain regions and in the kidney. Young rats were administered daily 20,000 international units of vitamin D3 per kg (body weight) over a period of 4 months. This chronic treatment resulted in a clinically mild hypervitaminosis that did not affect the content of calmodulin, the 28-kDa calbindin-D, and S-100. Also the concentration of parvalbumin in the cerebral cortex, hippocampus, and kidney remained unchanged. On the other hand, parvalbumin was increased about 50% in the caudate putamen of hypervitaminotic animals as compared to controls. Our results indicate that the metabolism of parvalbumin in the caudate putamen can be influenced by variations of the blood level of this steroid hormone.

Animals↗
PubMed1988

Monoclonal antibodies directed against the calcium binding protein parvalbumin.

We have produced twelve monoclonal antibodies (McAB) against carp-II parvalbumin. Three of them, designated 235, 239, 267 recognize determinants conserved in fish, chicken, mouse, rat, monkey and human parvalbumin. We show their use in the qualitative detection of parvalbumin (PV) by immunohistochemistry, in the quantitation of parvalbumin by radioimmunoassay and in the detection of parvalbumin on immunoblots.

Animals↗
PubMed1987

Localization of angiotensinogen in multiple cell types of rat brain.

Angiotensinogen was localized in 3 cell types in brain using immunohistochemical methods. These locations included subpopulations of neurons in nuclei that co-stain for angiotensin II, subpopulations of astrocytes that make putative contacts with brain microvessels, and cells of the choroid plexus. These findings are consistent with multiple functions for brain angiotensinogen as a precursor for neuronal angiotensin II and as a potential source for angiotensin II that is locally produced in the brain.

Angiotensin II↗
PubMed1987

Noradrenergic sub-sensitivity in the cerebral cortex of the tottering mouse, a spontaneously epileptic mutant.

The glycogenolytic action of norepinephrine (NE) was examined in the tottering mouse, a spontaneously epileptic mutant which presents a noradrenergic hyperinnervation of various CNS areas, including the cerebral cortex. The potency and efficacy of NE in promoting glycogenolysis were markedly decreased in cerebral cortical slices prepared from homozygous tottering (tg/tg) when compared to control C57BL/6j (+/+) mice, indicating a sub-sensitive response to a cellular action of NE. The metabolic nature of this adaptive change suggests that an impaired capacity of NE in mobilizing energy substrates may be related to the expression of the epileptic symptomatology in this mutant.

Animals↗
PubMed1987

Ontogeny of the calcium binding protein calbindin D-28k in the rat nervous system.

Calbindin D-28k immunoreactivity appeared at embryonal day 14 (E14) in the central nervous system as well as in the sensory organs and at E15 in the peripheral nervous system of the rat. At E14 the infundibular process of the diencephalon, cells of the posterior hypothalamus and of the dorsal thalamus were the only structures strongly immunostained in the brain, whereas neurons of the basal plate of the spinal cord, medulla oblongata and of the outermost layer of the cerebral cortex were only faintly labeled. Calbindin positive cerebellar Purkinje cells could be discerned at E15 together with a few cells in the hippocampus and in ganglia of the cranial nerves. At E19 various mesencephalic and metencephalic structures, spinal ganglion cells and basal ganglia displayed calbindin immunoreactive cells. The adult pattern of calbindin immunoreactivity (Garcia Segura et al. 1984) was reached before birth in most brain regions. In general, cells which displayed calbindin during brain development were also calbindin positive in the adult animal. Exceptions to this rule were cells of deep nuclei of the cerebellum and non-neuronal cells which transiently expressed calbindin during development. Calbindin appeared in a given brain region almost invariably 1 or 2 days after the cessation of cell division and the beginning of neuronal migration and extension of neuronal processes. The calcium binding protein calbindin might influence these Ca2+-dependent processes.

Animals↗
PubMed1986

Parvalbumin in most gamma-aminobutyric acid-containing neurons of the rat cerebral cortex.

gamma-Aminobutyric acid (GABA) is one of the major inhibitory neurotransmitters in the central nervous system. In the cerebral cortex, GABA-containing cells represent a subpopulation of interneurons. With semithin frozen sections, it is possible to demonstrate that most GABA neurons in the rat somatosensory cortex contain the calcium-binding protein parvalbumin and that parvalbumin is found virtually only in GABA neurons. Parvalbumin seems to influence the electrical properties and enzymatic machinery to modulate neuronal excitability and activity. The specific role of parvalbumin in GABA-containing cortical cells may be related to controlling the effectiveness of their inhibitory action.

Animals↗
PubMed1986

Generation of angiotensinogen by cultured neuroblastoma and glioma cells.

Cultured neuroblastoma cells and neuroblastoma-glioma cells have been shown to contain renin activity, angiotensin-converting enzyme activity, and angiotensins. It has been assumed that these cells also produce angiotensinogen as the substrate of an intracellular renin-angiotensin system. However, measurements of angiotensinogen have not been reported in the neuroblastoma or neuroblastoma-glioma cells, and the possibility that the cells generate angiotensins from fetal bovine angiotensinogen has not been eliminated. In this work angiotensinogen was shown to accumulate in the serum-free medium of thoroughly washed neuroblastoma cells (mouse Neuro-2A and rat B103) and glioma cells (rat C6). Separate experiments demonstrated that mouse Neuro-2A cells continue to produce angiotensinogen even after two passages in a defined serum-free culture medium. Further evidence that the angiotensinogen was not a contaminant from fetal bovine serum was obtained by the use of a monoclonal antibody raised against angiotensinogen of rat plasma. The angiotensinogen of Neuro-2A and C6-glioma cells is bound by the monoclonal antibody, whereas fetal bovine angiotensinogen is not bound. These results are consistent with the hypothesis that angiotensinogen is produced locally in the brain and in neuroblastoma cells as a substrate for an intracellular renin-angiotensin system.

Angiotensinogen↗
PubMed1986

Cellular location of 'liver-specific' antigen F.

Three mouse monoclonal antibodies against Type 1 murine 'liver-specific' antigen F and one rat monoclonal antibody against human antigen F were produced. These monoclonals recognize antigenic determinants common to Type 1 and Type 2 mouse and human antigen F. By immunolabelling with beta-galactosidase, antigen F could be demonstrated in the cytoplasm of hepatocytes, tubules of the kidney, and perikarya of neurons of the central nervous system. F antigens isolated from liver, kidney, and brain all have molecular weights of around 40,000.

Animals↗
PubMed1986

Immunoelectronmicroscopy of neural antigens on ultrathin frozen sections.

We have utilized immunocryoultramicrotomy to detect synapsin, somatostatin, parvalbumin, and tubulin at the ultrastructural level. Immunocryoultramicrotomy combines informative identification of morphology with accurate immunolabeling. Moreover, since no detergents or organic solvents are used to enable antibody penetration, and since no enzyme marker diffusion occurs, localization of the antigens should be more accurate. Accordingly, it was possible to localize precisely all four antigens within a well-preserved structure. Application of this method has important advantages for high-resolution localization of molecules relevant to neuronal function.

Animals↗
PubMed1985

Nucleus basalis Meynert neurons contain the vitamin D-induced calcium-binding protein (Calbindin-D 28k).

The neurons of the monkey basal nucleus of Meynert are shown to contain a protein indistinguishable from the chicken intestinal 28kd vitamin D-dependent calcium-binding protein (Calbindin-D 28k; CPB). CBP is thought to shuttle and buffer Ca++-ions, thus regulating the intracellular calcium distribution and concentration. Our observation may engender interest in searching for the role Vitamin D-metabolites, the CBP and calcium-ions in the physiology and pathology of nucleus basalis Meynert neurons.

Animals↗
PubMed1985

Ontogeny of renin immunoreactive cells in the human kidney.

We studied the time of appearance of renin-immunoreactive cells in prenatal human kidneys by immunohistochemistry and transmission electron microscopy (TEM). Renin immunoreactivity was detectable as early as the 5th or 6th gestational week in the mesonephros and appeared at 8 weeks of gestation in the metanephros. In a 8 week old embryo "renin granules" were seen by TEM in the juxtaglomerular epithelioid granular cells of metanephric tissue. In the embryos delivered by prostaglandin-induced abortion, granular renin immunoreactivity was also present in the cells of the proximal convoluted tubule. Our results support the contention that the renin-angio-tension system is active during fetal life and indicates a role for renin even during the embryonic period. In addition, they document a morphologically detectable effect of prostaglandins on the distribution of renin in the kidney.

Abortion, Induced↗