Biomedical subjects

D Maréchal

Publications and source records attributed to D Maréchal.

3 recordsLinked to original sources

PubMed1997

Prominent dendritic localization in forebrain neurons of a novel mRNA and its product, dendrin.

A recently cloned rat brain cDNA derives from a novel gene, termed dendrin (DEN), expressed exclusively in forebrain structures, particularly in neocortex, olfactory bulb, hippocampus, caudate-putamen, and limbic system. In these structures, the cognate mRNA is present in neuronal cell bodies and their dendrites, whereas near exclusive dendritic localization is observed for the polypeptide product. In the hippocamus, DEN mRNA is highly expressed in the cell laminae and dendritic layers of the dentate gyrus and CA1 field, but expression is markedly reduced in the CA3 and CA4 areas. The predicted primary structure of the hydrophilic, highly basic 653-amino-acid polypeptide does not suggest a function. The restricted expression and dendritic location are compatible with a role for DEN in synaptic plasticity of central neocortical forebrain neurons.

Amino Acid Sequence↗

PubMed1993

A subtractive hybridization method to isolate tissue-specific transcripts: application to the selection of new brain-specific products.

A method based on subtractive hybridization of brain complementary DNAs with peripheral messenger RNAs has enabled us to construct an enriched brain-specific cDNA library. Single-stranded cDNAs (ssc DNAs) were synthesized from brain polyadenylated mRNAs and subsequently hybridized with peripheral mRNAs immobilized on nitrocellulose membrane. Unhybridized sscDNAs were converted into double-stranded cDNAs and cloned into plasmid pUC13. The screening of the resulting library showed that a high percentage of the cloned cDNAs corresponded to mRNAs specifically transcribed in the brain.

Animals↗

PubMed1989

The rat-liver microsomal AP endonuclease. The endoplasmic reticulum is presented as a net thrown into the cytosol to capture newly synthesized karyophilic proteins.

Although most of the rat-liver AP (apurinic/apyrimidinic) endonuclease is in chromatin, some activity is found in microsomes. A quantitative assay of the microsomal AP endonuclease is described. The enzyme is a peripheral membrane protein that is located on the outside surface of microsomes. All the binding sites on the microsomes appear to have the same affinity for the AP endonuclease, suggesting the presence of receptors for the enzyme. The AP endonuclease is displaced from its membrane attachment by submicromolar concentrations of the karyophilic signal of SV-40 T antigen. The AP endonuclease receptors are likely to be on the cytosolic side of the endoplasmic reticulum. It is suggested that binding of the protein to these receptors might be the first step of the transport mechanism that enables the AP endonuclease to penetrate into the nucleus. The same mechanism utilizing the same receptors might be used by other karyophilic proteins, including SV-40 T antigen.

Amino Acid Sequence↗