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M Schalling

Publications and source records attributed to M Schalling.

At least 145 records · Page 8Linked to original sources
PubMed1988

A subpopulation of dopaminergic neurons in rat ventral mesencephalon contains both neurotensin and cholecystokinin.

The coexistence of the neuropeptides neurotensin and cholecystokinin and the catecholamine-synthesizing enzyme tyrosine hydroxylase within neurons of the ventral mesencephalon was analyzed using an immunofluorescence triple-labeling technique. Virtually all of the neurotensin-positive cell bodies in the ventral tegmental area, medial substantia nigra pars compacta, retrorubral field, and rostral and caudal linear raphe nuclei were found to contain both cholecystokinin and tyrosine hydroxylase immunoreactivities. The degree of colocalization was lower and more variable in other regions including the ventral and central periaqueductal grey matter and dorsal raphe nucleus. It appeared that immunoreactivities for these 3 neuroactive substances were not contained within the same axonal-like fibers and terminals in the ventral midbrain. These results demonstrate that a subpopulation of dopaminergic neurons, which presumably comprise part of the ascending mesotelencephalic system, contains the two peptides neurotensin and cholecystokinin. Thus, the data suggest a morphological basis for some of the reported functional interactions of these 3 putative neurotransmitters/neuromodulators within this system.

Animals↗
PubMed1988

DARPP-32 as a marker for D-1 dopaminoceptive cells in the rat brain: prenatal development and presence in glial elements (tanycytes) in the basal hypothalamus.

The present article reviews some aspects of the localization of a dopamine- and cyclic AMP-regulated phosphoprotein, DARPP-32, which is assumed to be present in D-1 dopaminoceptive neurons. Its prenatal development starts at day 14 of gestation, is to a large extent complete at birth and seems to be independent of ingrowing dopamine-containing afferents. Rearrangements occur in certain areas, and in some systems DARPP-32 appears to be only transiently expressed. The presence of DARPP-32 in glial structures, the tanycytes, in the arcuate nucleus-median eminence complex in the mediobasal hypothalamus, has given further support to the hypothesis that dopamine, by controlling the shape of the tanycytes and the extension of their processes, can regulate LHRH release by a 'mechanical mechanism'. This hypothesis is now being examined in some experimental paradigms.

Animals↗
PubMed1988

Neuropeptide tyrosine in the rat adrenal gland--immunohistochemical and in situ hybridization studies.

The adrenal gland of the rat was analysed with immunohistochemistry and antisera to neuropeptide tyrosine, to the catecholamine-synthesizing enzymes tyrosine hydroxylase, phenyl-ethanolamine-N-methyltransferase, and to acetylcholinesterase and with in situ hybridization using a nick-translated 280 base pair deoxyribonucleic acid probe coding for exon 2 of the rat neuropeptide tyrosine gene. Neuropeptide tyrosine-like immunoreactivity was observed in three structures: chromaffin cells, medullary ganglion cells and nerve fibers. The chromaffin cells were of both the noradrenaline- and adrenaline-type. The ganglion cells did not seem to contain any catecholamine-synthesizing enzymes but exhibited a strong immunoreaction for acetylcholinesterase. They were thus in all probability cholinergic neurons. In situ hybridization using the nick-translated deoxyribonucleic acid probe to rat neuropeptide tyrosine messenger ribonucleic acid revealed a very high-grain density over the ganglion cells, a moderate density over the chromaffin cells and a low background over cortex, in agreement with the immuno-histochemical demonstration of neuropeptide tyrosine-like immunoreactivity both in chromaffin and ganglion cells. The intense neuropeptide tyrosine-like immunoreactivity and low content of neuropeptide tyrosine messenger ribonucleic acid suggest that the chromaffin cells have fairly large peptide stores but that the peptide turnover is low. In contrast, the ganglion cell bodies seem to contain low amounts of neuropeptide tyrosine-like immunoreactivity but exhibit a high neuropeptide tyrosine synthesis rate. Preliminary studies with the amine-depleting drug reserpine revealed an increase in messenger ribonucleic acid both in ganglion cells and medullary cells. In the chromaffin cells the highest activity was seen 3 and 4 days after injection, and the levels were down to normal after 8 days. The present findings demonstrate neuropeptide tyrosine synthesis and storage in two cell populations in the adrenal medulla. In situ hybridization with its cellular resolution can provide information on possible differential effects of drugs and experimental procedures on these two neuropeptide tyrosine stores.

Acetylcholinesterase↗
PubMed1988

Coexistence and gene expression of phenylethanolamine N-methyltransferase, tyrosine hydroxylase, and neuropeptide tyrosine in the rat and bovine adrenal gland: effects of reserpine.

Expression and regulation of the catecholamine-synthesizing enzymes phenylethanolamine N-methyltransferase (PNMTase; S-adenosyl-L-methionine:phenylethanolamine N-methyltransferase, EC 2.1.1.28) and tyrosine hydroxylase [TyrOHase; tyrosine 3-monooxygenase, L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2] and the coexisting neuropeptide tyrosine (NPY) were studied in rat and bovine adrenal medulla. By using both immunohistochemistry and in situ hybridization, PNMTase- and NPY-positive cells exhibited a close overlap in bovine medulla and were preferentially localized in the outer two-thirds of the medulla. Although TyrOHase and its mRNA were observed in virtually all medullary gland cells, TyrOHase mRNA levels were much higher in the PNMTase- and NPY-positive cells. After administration of the catecholamine-depleting drug reserpine to rats, a brief increase, followed by a dramatic decrease, in the level of PNMTase mRNA was observed in the adrenal medulla. In contrast, mRNA for both TyrOHase and NPY only exhibited an increase, whereby the TyrOHase mRNA peak preceded that of NPY mRNA. Different regulatory mechanisms may thus operate for these three compounds coexisting in the adrenal medulla.

Adrenal Glands↗
PubMed1988

Antiserum raised against residues 159-168 of the guanine nucleotide-binding protein Gi3-alpha reacts with ependymal cells and some neurons in the rat brain containing cholecystokinin- or cholecystokinin- and tyrosine 3-hydroxylase-like immunoreactivities.

Antibodies raised against a synthetic deca-peptide corresponding to a specific sequence of Gi3-alpha protein (an inhibitory guanine nucleotide-binding protein) were used to analyze Gi3-alpha-like immunoreactivity in brain sections from colchicine-treated rats by indirect immunofluorescence histochemistry. Gi3-alpha-peptide-positive cell bodies were found in the ventral tegmental area and substantia nigra, and these cells were also cholecystokinin (CCK)- and tyrosine 3-hydroxylase-positive. Gi3-alpha-peptide staining was observed in perikarya in the hippocampus and in fibers in the nucleus accumbens, tuberculum olfactorium, bed nucleus of stria terminalis, and a spino-thalamic tract, where it coexisted with CCK-like immunoreactivity as well. No coexistence with CCK occurred in Gi3-alpha-peptide-positive ependymal cells outlining the aqueduct and ventricles. Preadsorption of Gi3-alpha antibodies with CCK-8 or CCK-33 did not alter Gi3-alpha-peptide staining. The occurrence of Gi3-alpha-peptide-like immunoreactivity in CCK-containing neurons may indicate the presence of Gi3-alpha protein and in CCK/dopamine neurons may indicate an association of this Gi protein with dopamine autoreceptors.

Animals↗
PubMed1987

Coexistence of peptides with classical neurotransmitters.

In the present article the fact is emphasized that neuropeptides often are located in the same neurons as classical transmitters such as acetylcholine, 5-hydroxy-tryptamine, catecholamines, gamma-aminobutyric acid (GABA) etc. This raises the possibility that neurons produce, store and release more than one messenger molecule. The exact functional role of such coexisting peptides is often difficult to evaluate, especially in the central nervous system. In the periphery some studies indicate apparently meaningful interactions of different types with the classical transmitter, but other types of actions including trophic effects have been observed. More recently it has been shown that some neurons contain more than one classical transmitter, e.g. 5-HT plus GABA, further underlining the view that transfer of information across synapses may be more complex than perhaps hitherto assumed.

Animals↗
PubMed1987

Detection of neuropeptide Y and its mRNA in megakaryocytes: enhanced levels in certain autoimmune mice.

Neuropeptide tyrosine (neuropeptide Y, NPY) is a potent vasoconstrictor with a wide distribution in the central and peripheral nervous systems. Here we show that high levels of rat NPY mRNA are also found in peripheral blood cells, bone marrow, lung, and spleen. Furthermore, radioimmunoassay revealed high levels of NPY-like peptide in these tissues. In mice, the levels of splenic NPY mRNA and immunoreactive peptide differed extensively between strains and were greatly elevated in several strains (NZB, NZBxW, and BXSB) that develop a disease resembling human systemic lupus erythematosus. Like the rat, the NZB mouse showed a high content of NPY mRNA in peripheral blood cells and bone marrow. Immunohistochemical staining revealed NPY-like immunoreactivity in large cells morphologically identifiable as megakaryocytes in rat bone marrow and in the spleen of the NZB mouse strain. Expression of NPY mRNA in megakaryocytes in rat bone marrow and NZB mouse spleen was confirmed by in situ hybridization. These results indicate that NPY is synthesized in megakaryocytes, implying that NPY can be released from platelets and function as a vasoconstrictor during blood-vessel damage. In addition, the increase in splenic NPY in certain autoimmune mouse strains adds to the list of abnormalities associated with these strains.

Animals↗
PubMed1987

Structure and expression of the gene encoding the vasoactive intestinal peptide precursor.

The gene encoding the human vasoactive intestinal peptide (VIP) and the histidine-methionine amide (PHM-27) peptide hormone was isolated from lambda phage libraries. The human gene was found to be composed of seven exons spanning approximately 9 kilobase pairs. The first exon codes for an untranslated leader sequence, and the second exon codes for a putative signal peptide. DNA sequences coding for the VIP and PHM-27 hormones are located in two different exons. Southern blot analysis with genomic DNA suggested that a single copy of the VIP/PHM-27 gene is present in the human haploid genome. The expression of VIP/PHM-27 precursor mRNA in various tissues in the rat was analyzed by RNA gel blot hybridization. In the organs examined, expression was only detected in the brain and duodenum. RNA isolated from various regions of the rat brain--including the cortex, hypothalamus, and hippocampus--hybridized to both VIP- and PHM-27-specific probes. The same pattern of hybridization was found when VIP- and PHM-27-specific probes were used, suggesting that possible differences in the localization of VIP and PHM-27 peptides between different brain regions cannot be accounted for by differential RNA processing.

Amino Acid Sequence↗
PubMed1986

Leukotriene C4 binding sites in the rat central nervous system.

Binding sites for [3H]LTC4 were observed in crude membrane preparations of rat central nervous system tissue. Equilibrium binding studies indicated one high affinity [3H]LTC4 binding site with a KD of 31.4 +/- 3.4 nM for whole brain preparations. The binding was highly specific for [3H]LTC4 and could be inhibited by the SRS-A antagonist FPL 55172. Specific binding was increased with both mono- and di-valent ions. Regional distribution studies revealed a three-fold difference in binding capacity within different regions of the brain with the highest binding capacity in the brainstem (94.1 +/- 6.9 fmol/mg of protein) and the lowest in the hypothalamus (29.6 +/- 12.8 fmol/mg of protein). In addition, weak low capacity binding was observed for [3H]LTB4 and [3H]LTE4, while no saturable binding was observed for [3H]LTD4. The order of selectivity in inhibiting [3H]LTC4 binding was LTC4 much greater than LTD4 = LTE4 greater than LTB4.

Animals↗