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F Aniello

Publications and source records attributed to F Aniello.

31 records · Page 2Linked to original sources
PubMed1996

Molecular cloning of a novel mRNA (harderin) specifically and highly expressed in the Harderian gland of the frog, Rana esculenta.

A cDNA clone encoding a novel mRNA (harderin) has been isolated from the cDNA library of frog Rana esculenta Harderian gland. The cDNA is 875 bp long and encodes a novel protein of 218 amino acid residues. The deduced proteins reveals no significant homology to other proteins. The mRNA is a single 0.9 kb transcript detected only in the RNA of frog Harderian gland, highly expressed throughout the year. The constant and exclusive presence of harderin in the frog Harderian gland, suggests a constitutive tissue specific expression for this protein.

Amino Acid Sequence↗
PubMed1995

Cloning of ascidian homeobox genes provides evidence for a primordial chordate cluster.

In order to isolate genes important in controlling embryonic development in Tunicates, a genomic library from the ascidian Ciona intestinalis was screened with a degenerate oligodeoxyribonucleotide encoding the third helix of Antennapedia-type homeoboxes. Fourteen C. intestinalis homeobox genes, corresponding to several classes of homeodomains, have been identified. Five of the isolated homeoboxes show their highest homology to members of the Vertebrate HOX clusters. mRNAs for two of the isolated homeoboxes are present in unfertilized C. intestinalis eggs.

Amino Acid Sequence↗
PubMed1995

DNA methyltransferase activity in the early stages of a sea urchin embryo. Evidence of differential control.

The specific activity of DNA methyltransferase increases in the nuclei of Sphaerechinus granularis sea urchin embryos at increasing stages of development. The activity reaches maximal value at about 20 h of growth, when embryos are at the mesenchyme blastula stage, then abruptly decreases and is essentially zero at about 35 h of development, when embryos are at the early gastrula stage. Both the increase and the drop of the activity are faster than embryonic cell duplication indicating that the enzyme is under strict control during development and that, in the more advanced embryo, a mechanism is activated to specifically block its activity.

Animals↗
PubMed1995

Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase.

A 2935-bp cDNA clone encoding glutamine synthetase (GS) was isolated from a cDNA library prepared from four-blastomere Paracentrotus lividus sea urchin embryos. The sequence consists of a 75-bp 5' untranslated region (5'-UTR) followed by a 1095-bp coding region corresponding to a 365-amino-acid (aa) protein, a 1747-bp 3'-UTR and a terminal 18-bp poly(A) tail. The encoded protein shows about 66% identical residues, as compared with human and lobster class-II GS. The sequence contains the Mn(2+)-binding aa and the highly conserved aa regions observed in other GS. Northern blot analyses show that the GS mRNA is present in the sea urchin egg and is developmentally regulated in the embryo.

Amino Acid Sequence↗
PubMed1994

Isolation of a new H3.3 histone variant cDNA of P. lividus sea urchin: sequence and embryonic expression.

A cDNA encoding a new H3 histone variant has been isolated from a Paracentrotus lividus sea urchin embryo cDNA library. The encoded protein is identical to the H3.3 histone subtype identified in other species, with the difference that E replaces D at position 81. The clone corresponds to a transcript of about 1.6 kb, not dependent on DNA replication, present in the unfertilized egg and at all stages of embryonic development. The coding part of the cDNA cross-reacts also with a 0.5 kb H3 late histone mRNA.

Animals↗
PubMed1993

Amino-acid sequence of the cooperative dimeric myoglobin from the radular muscles of the marine gastropod Nassa mutabilis.

The complete amino-acid sequence of the dimeric and cooperative myoglobin from the radular muscles of Nassa mutabilis, a common edible gastropod mollusc on the Italian coast, has been determined. The molecule is a homodimer. The monomer is composed of 147 amino-acid residues, with a molecular mass of 15,760 Da. Its sequence is homologous with those of the dimeric myoglobins of the gastropod molluscs of the Prosobranchia subclass Busycon canaliculatum (63% conserved residues) and Cerithidea rhizophorarum (46% conserved residues). The rate of autoxidation to met-myoglobin of N. mutabilis oxymyoglobin at 25 degrees C is strongly pH-dependent with relative minimal rate values in the pH range 7 to 8.

Amino Acid Sequence↗
PubMed1992

Thyroid hormone effects on neuronal differentiation during brain development.

Neurite outgrowth and acquisition of neuronal polarity depend on microtubule assembly and this process is impaired when hypothyroidism is established at late fetal stages in the rat. Taking in account these observations the effects of thyroid hormone deficiency in the developing cerebellum were studied with probes for different tubulin isoforms and for two microtubule-associated proteins, tau and MAP2, which are specific for the axons and the dendrites, respectively. The results showed that thyroid hormone deficiency: 1) desynchronizes the spatio-temporal program of axonal and dendritic differentiation in the cerebellum. 2) Modifies the developmental pattern of expression of various tubulin isoforms. 3) Delays replacement of the immature tau variants by the mature forms. The adult variants of tau proteins specify adult and stable axons whereas the juvenile forms are expressed when axons are growing actively. According to these criteria the hypothyroid brain remains immature at stages when proper connectivity is normally established. Thyroid hormone appears therefore as an epigenic signal that synchronizes axonal and dendritic outgrowth, two major parameters of the construction of the neuronal network.

Animals↗
PubMed1991

Splicing of juvenile and adult tau mRNA variants is regulated by thyroid hormone.

The effect of thyroid hormone on the expression of tau transcripts was studied during postnatal brain development. The level of tau mRNA was only slightly changed postnatally in the cerebral hemispheres of hypothyroid rats, whereas the level of tau mRNA in the cerebellum was maintained at a higher level than in the euthyroid controls. As shown by in situ hybridization studies, such an alteration in tau mRNA expression can be ascribed to an effect of thyroid hormone on the rate of migration of the granule cells in the cerebellum; that tau mRNAs remain high in the cerebellum as long as the granule cells are migrating correlates with the observation that hypothyroidism slows the rate of migration of granule cells. RNase protection assays also showed that thyroid hormone deficiency delays the transition between the immature and mature tau transcripts in both brain regions. Thus, one of the effects of thyroid hormone is to regulate the splicing mechanism that allows replacement of the juvenile tau variants by the adult entities during neuronal differentiation.

Animals↗
PubMed1991

Regulation by thyroid hormone of microtubule assembly and neuronal differentiation.

In this review we examine successively: 1) the major effects of thyroid hormone deficiency seen during brain development with special emphasis on the changes in neuronal morphology and migration occurring postnatally in the cerebellum. 2) The effects of this hormone on microtubule assembly during neurite outgrowth and acquisition of neuronal polarity. 3) The changes in expression of the different tubulin isoforms occurring during development in the normal and hypothyroid rat brain. 4) The regulation by thyroid hormone of the transition occurring during development between the juvenile and adult microtubule-associated protein Tau.

Animals↗
PubMed1991

Regulation of five tubulin isotypes by thyroid hormone during brain development.

Nucleic acid probes derived from the 3' noncoding region of five tubulin cDNAs were used to study the effects of thyroid hormone deficiency on the expression of the mRNAs encoding two alpha (alpha 1 and alpha 2)- and three beta (beta 2, beta 4, and beta 5)-tubulin isotypes in the developing cerebral hemispheres and cerebellum. The content of alpha 1, which markedly declines during development in both brain regions, is maintained at high levels in the hypothyroid cerebellum, whereas it is decreased in the cerebral hemispheres. The alpha 2 level also declines during development and is decreased in both regions by thyroid hormone deficiency, but only during the two first postnatal weeks. Thyroid hormone deficiency slightly increases at all stages the beta 2 level in the cerebellum, whereas a decrease is observed at early stages in the cerebral hemispheres. The beta 5 level seems to be independent of thyroid hormone in the cerebral hemispheres, whereas it decreases at early stages in the hypothyroid cerebellum. Finally, the expression of the brain-specific beta 4 isotype is markedly depressed by thyroid hormone deficiency, particularly in the cerebellum. These data suggest that the genes encoding the tubulin isotypes are, directly or not, differently regulated by thyroid hormone during brain development. This might contribute to abnormal neurite outgrowth seen in the hypothyroid brain and therefore to impairment in brain functions produced by thyroid hormone deficiency.

Aging↗
PubMed1989

Histone-lysine methyltransferase activity from sea-urchin embryo nuclei. Changes in substrate specificity upon purification.

The S-adenosylmethionine:histone-lysine methyltransferase (EC 2.1.1.43) enzyme activity, present in the chromatin of sea-urchin embryo nuclei, has been purified about 300-fold with 30% overall yield. The initial activity in the nucleus transfers methyl groups to the epsilon-amino group of lysines and acceptor proteins are chromatin-bound H3 and H4 histones. In contrast, the purified enzyme activity transfers methyl groups to the arginines and acceptor proteins are soluble H3 and H4 histones. The two changes in substrate specificity do not occur at the same time. The variation of acceptor protein from chromatin-bound to soluble histones occurs at the first step, upon nuclei sonication, when no protein fractionation has yet been performed. At that step, lysine is still the only methylated side-chain. The variation of the methylated amino acid from lysine to arginine occurs gradually with increasing enzyme purification. The enzyme activity has a molecular mass of about 200 kDa. Saturation curves for H3 and H4 histones, used as substrate either individually or in total histones, and for AdoMet show no substantial dependence on enzyme purification. Maximal activity for the enzyme, at all purification levels, occurs at about pH 8 for all substrate histones. An increase in the relative concentrations of di- and trimethyllysine derivatives is observed with the more purified enzyme preparations, while the ratio of mono- and dimethylarginine derivatives remains constant. The data are taken as evidence that the same protein molecule is responsible for the two activities.

Animals↗
PubMedDate not supplied

Sea urchin DNA methyltransferases.

DNA methyltransferase activities have been partially purified from unfertilized eggs and blastula nuclei of sea urchin embryos. Comparative studies, using different DNAs as substrates, show that the two preparations are most active on hemimethylated and single-strand DNA, but they methylate, though at a lower rate, also on double-strand DNA. The two activities show distinctive efficiencies in methylating plasmid DNAs and marked differences in the rate of methyl transfer to DNAs in different structural states: linear, relaxed, or supercoiled. The ratio of the apparent specific activity of the two preparations depends on the particular DNA used as substrate and its structure. Methylation analysis of the restriction fragments of methylated plasmid DNAs shows a linear correlation between introduced methyl groups and the percent of CpG of each particular fragment, indicating that methylation is substantially random and sequence is less relevant than conformation in determining enzyme efficiency. The data do not permit us to decide if the two activities are different enzymes or the same enzyme with different modulating factors.

Animals↗