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A Tino

Publications and source records attributed to A Tino.

10 recordsLinked to original sources
PubMed2001

Putative glycine receptors in Hydra: a biochemical and behavioural study.

Glycine acts as an inhibitory transmitter in the lower brain stem and spinal cord of vertebrate species, while very few data are yet available to support a similar role in invertebrate nervous systems. Here we report the identification and characterization of glycine receptors in the freshwater polyp Hydra vulgaris (Cnidaria, Hydrozoa) by biochemical and behavioural studies. Saturation experiments revealed the occurrence of one population of binding sites of nanomolar affinity (KD = 33 nm) and low capacity (Bmax = 79 fmol/mg protein) for [(3)H]strychnine. The addition of glycine or taurine (0.1 microm-1 mm) produced a dose-dependent inhibition of [(3)H]strychnine binding. Beta-alanine (0.1-1 mm) did not significantly affect [(3)H]strychnine binding. The pharmacological properties of these receptors compare with those of vertebrate glycine receptors. Stimulation of Hydra polyps by reduced glutathione resulted in a significant increase in the duration of mouth opening in the presence of glycine, taurine or beta-alanine. The enhancement of the response was related both to amino acid (10-100 microm) and to glutathione concentration (1-10 microm). The effects of glycine or its agonists were suppressed by strychnine (1-10 microm). D-serine, a glycine agonist at the vertebrate NMDA receptor, produced opposite effects to those of glycine. The effects of d-serine were suppressed by 5,7-dichlorokynurenic acid but not by strychnine. In vitro, [(3)H]strychnine binding was not displaced by d-serine. These results indicate a dual action of glycine in Hydra tissues. The hypothesis that NMDA receptors may also be present in this elementary nervous system is proposed.

Animals↗
PubMed1999

Neuronal and glial properties coexist in a novel mouse CNS immortalized cell line.

A mes-c-myc A1 (A1) cell line was generated by retroviral infection of cultured embryonic mesencephalic cells and selected by neomycin resistance. A1 cells cease to divide and undergo morphological differentiation after serum withdrawal or addition of c-AMP. Proliferating or morphologically differentiated A1 cells are all positive for vimentin and nestin, a marker of neural precursor, and show neuronal markers such as microtubule-associated protein 1, neuron-specific enolase and peripherin, and the glial marker glial fibrillary acidic protein. Neuronal and glial markers coexist in single cells. Furthermore, A1 cells show presence of glutamic acid decarboxylase 67 mRNA and its embryonic form EP10 and accumulate the neurotransmitter GABA. Electrophysiological studies demonstrate that morphologically differentiated A1 cells display voltage-gated sodium and potassium channels in response to depolarizing stimuli. A1 cells thus represent a novel, bipotent neural cell line useful for studying CNS differentiation and plasticity, as well as the molecular mechanisms underlying development of GABAergic neurotransmission.

Animals↗
PubMed1999

Kelletinin A, from the marine mollusc Buccinulum corneum, promotes differentiation in Hydra vulgaris.

The effects of kelletinin A [ribityl pentakis (p-hydroxybenzoate)] (KA), a natural compound isolated from the marine gastropod Buccinulum corneum, were studied in vivo in Hydra vulgaris during regeneration. KA caused a marked increase of regenerated tentacle numbers (ATN) and promoted transdifferentiation of epithelial cells into battery cells, and nematocyte differentiation. Morphological data were correlated to changes in acid and alkaline phosphatase levels, enzymes that have been described as regeneration markers.

Acid Phosphatase↗
PubMed1998

The Drosophila melanogaster lipase homologs: a gene family with tissue and developmental specific expression.

We report the molecular cloning of Drosophila genes encoding putative lipase homologs, Dm lip1, lip2 and lip3, the definition of their structure and the expression patterns during development. These Drosophila lipases are related to acid lipases, with a common GHSQG motif, within a more general consensus GXSXG, identified as the active site shared by all the members of lipase superfamily. The lip1 and lip3 genes are transcribed in different tissues and developmental stages, suggesting that they have different functions. The lip1 gene, coding for a protein similar to digestive lipases, is expressed in ovaries and early embryos and, with a different sized transcript, in all the other developmental stages. The lip3 gene, whose translation product is more similar to lysosomal acid lipases, is expressed only during the larval period. The lip2 gene seems non-functional. The Drosophila putative lipases do not show similarity with the Drosophila yolk proteins that are reported to have sequence similarity with lipoprotein lipases, but share a consistent similarity with lepidopteran proteins reported as egg specific or yolk proteins, probably corresponding to lipase homologs. The results reported here are discussed in relation to the evolution and functions of lipases within the between species.

Amino Acid Sequence↗
PubMed1997

Functional organization of the promoter region of the mouse F3 axonal glycoprotein gene.

F3 is a developmentally regulated adhesive glycoprotein expressed by subpopulations of central and peripheral neurons which mediates neurite growth and fasciculation via cis- and trans-interactions with cell-surface or matrix components. We previously reported on the characterization of the F3 gene 5' flanking region in which we identified promoter and enhancer elements. Here, we report on the functional organization of the F3 gene regulatory regions. We show that the F3 promoter is built of linearly arranged positive and negative elements scattered through the 5' flanking region of the F3 gene and the 1st exon (exon 0). Neural- and cell type-specific expression of F3 appears to be governed by elements located in the most proximal promoter region which includes a neural-specific enhancer. In retardation assays, all these cis-acting elements bind nuclear proteins, three of which interact with the identified enhancer element while a single species interacts with sequences located within exon 0. Some of these proteins are also specifically expressed within the brain, indicating that they could correspond to neural-specific trans-acting factors. Elements located immediately upstream of the cell type-specific enhancer and within exon 0 are responsible for regulation of F3 expression by cAMP and retinoic acid.

Animals↗
PubMed1996

Dopamine transporter gene expression in rat mesencephalic dopaminergic neurons is increased by direct interaction with target striatal cells in vitro.

By using a semi-quantitative reverse transcriptase-PCR assay (RT-PCR) we have analyzed dopamine transporter (DAT), tyrosine hydroxylase (TH) and synaptic vesicle monoamine transporter (VMAT2) gene expression in rat mesencephalic (MES) primary cultures. Consistent with previous data obtained during rat MES ontogeny, the onset of DAT transcription in vitro is delayed in embryonic day (E)13, but not in E16, MES neurons when compared to that of TH and VMAT2. In co-culture, the addition of target striatal cells (STR) to E13 MES selectively increases DAT mRNA level in DA neurons during the first 3 days in vitro; cortical cells are ineffective. On the contrary, DAT gene does not appear up-regulated in E16 MES co-cultured with target STR cells, indicating that MES DA neurons respond to STR stimulation only at defined developmental stages. Up-regulation of DAT mRNA level by STR in E13 MES seems to require direct cell interactions since target cells do not exert their effect on DAT transcription when are separated from MES cells by a porous barrier, which only allows diffusion of soluble molecules. Thus maturation of DA neurotransmission in vitro appears to follow a developmental program which can be specifically modulated by their target STR cells.

Animals↗
PubMed1994

Target cells modulate dopamine transporter gene expression during brain development.

We have analysed the expression of the dopamine transporter (DAT) gene and compared it with that of tyrosine hydroxylase, neuronal GABA transporter and synaptic vesicle monoamine transporter genes during pre- and post-natal development of rat mesencephalic dopaminergic (DA) neurones. Our results show that DAT transcripts are not detectable until embryonic day (E) 15, whilst those of the other genes analysed are already present at E12. In vitro, the level of DAT gene transcription in mesencephalic E13 DA neurones is increased in coculture with target striatal cells. Thus striatal targets cells regulate, at the transcriptional level, a key step of dopaminergic neurotransmission during DA neurone development.

Animals↗
PubMed1993

A membrane guanylate cyclase Drosophila homolog gene exhibits maternal and zygotic expression.

A putative membrane form of guanylate cyclase gene was identified in region 32 of the second chromosome of Drosophila melanogaster. The Drosophila protein has a single hydrophobic sequence that divides the protein into a putative extracellular region and a cytoplasmic catalytic region which contains tyrosine kinase and cyclase domains showing varying degrees of conservation with other guanylate and adenylate cyclases. The gene shows a very interrupted organization with small exons separated by small introns and a low level of expression. Transcripts have been localized in situ during oogenesis in the germarium and later in stages 10-14 of egg chamber development. The putative maternal transcript can be seen in very early embryos and reappears later as a product of zygotic gene expression.

Amino Acid Sequence↗
PubMed1990

A cDNA clone homologous to Drosophila F elements from an imaginal discs poly(A)+ library.

A cDNA clone (F-id1) homologous to Drosophila F elements has been isolated from a cDNA library prepared from poly(A)+ RNA derived from imaginal discs. The F-id1 insert is identical to the 3' end terminus of Fw, an element inserted at the white locus upon irradiation. The isolation of F-id1 provides the first evidence that F elements are expressed in the fruit fly life.

Animals↗