Intrinsic neurons in the rat ovary: an immunohistochemical study

Cell Tissue Res 2000 Apr;300(1):47-56

H D'Albora 1 , P Lombide 1, S R Ojeda 2

1 Laboratory of Biology of Reproduction, Department of Histology and Embryology, School of Medicine, Universidad de la República, Gral. Flores 2125, CP 11800, Montevideo, Uruguay 2 Division of Neuroscience, Oregon Regional Primate Research Center, Beaverton, OR, USA

DOI: 10.1007/s004419900130
PMID: 10805074
Pubmed: https://pubmed.ncbi.nlm.nih.gov/10805074
Texto completo: https://link.springer.com/article/10.1007/s004419900130

Abstract:
Previous studies have shown the presence of neuronal perikarya in the primate ovary, but not in the ovary from Sprague-Dawley rats. We report here that while such intrinsic neurons are indeed absent in this strain of rats, they can be visualized in the ovary from Wistar rats. The neurons, identified by their morphology and by the expression of NeuN (a neuron-specific nuclear protein), were detected at all postnatal intervals examined, from 14 h after birth to 50 days of age. While they were present in the ovarian hilum and medulla at all ages studied, neurons first appeared in the ovarian cortex during the juvenile period (postnatal days 10-20). In all cases, the size of the neuronal soma increased significantly during prepubertal development, reaching maximal values before puberty. Some neurons were catecholaminergic, as indicated by their content of immunoreactive tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis. Some showed neuropeptide Y (NPY) immunoreactivity. TH-positive neurons were seen either in isolation or clustered in ganglion-like structures in both the ovarian cortex and medulla. These results indicate that ovarian neurons are not present in all strains of rats, but when present, the chemical phenotype of some of them is of a sympathetic nature, similar to that described in primates.

Characterization of MARCKS (Myristoylated alanine-rich C kinase substrate) identified by a monoclonal antibody generated against chick embryo neural retina

Biochem Biophys Res Commun 1999 257(2):480-7

F R Zolessi 1 3 , U Hellman 4 , A Baz 2 , C Arruti 1

1 Laboratorio de Cultivo de Tejidos, Sección Biología Celular, Universidad de la República, Montevideo, Uruguay 2 Cátedra de Inmunología, U.A., Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay 3 Departamento de Histología y Embriología, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay 4 Ludwig Institute for Cancer Research, Uppsala, Sweden

DOI: 10.1006/bbrc.1999.0490
PMID: 10198238
Pubmed: https://pubmed.ncbi.nlm.nih.gov/10198238
Texto completo: https://www.sciencedirect.com/science/article/abs/pii/S0006291X99904904?via%3Dihub

Abstract:
To identify molecular markers of cell differentiation in developing nervous tissue, monoclonal antibodies against chick embryo neural retina were made. One of them, 3C3mAb, recognized a developmentally regulated antigen present in several organs of the CNS. Data from MALDI-TOF mass spectrometry and peptide sequencing of the immuno-affinity purified protein indicated identity of the antigen with MARCKS. The immunoreactive material was always found as a unique polypeptide (Mr 71 kDa) in SDS-PAGE, however isoelectrofocusing revealed the existence of several bands (pI ranging from 4.0 to 4.5). Interestingly some retinal cell types, as photoreceptors, exhibited an extremely significant decrease in the intensity of the immunoreactive material during the final phases of terminal differentiation while others, as some retinal neurons, maintained the immunoreactivity when fully differentiated. Taken together these results indicate that MARCKS, a protein susceptible of several posttranslational modifications as myristoylation and phosphorylation at variable extent, may act differently in neural retina cell types.

Analysis of nuclear degradation during lens cell differentiation

Cell Death Differ 1998 5(4):251-61

M F Counis 1 , E Chaudun 1 , C Arruti 2 , L Oliver 3 , M Sanwal 4 , Y Courtois 1 , A Torriglia 1

1 U450 INSERM, développement, vieillissement et pathologie de la rétine, Unité associée CNRS, Association Claude Bernard, 29 rue Wilhem, Paris, 75016, France 2 Laboratorio de Cultivo de Tejidos, Facultad de Medicina, Av General Flores 2125, Montevideo, 11800, Uruguay 3 INSERM U 419, Institut de Biologie, 9 quai Moncousu, Nantes, Cédex 01, 44035, France 4 Department of Biochemistry, University of Western Ontario, London, NGA 5C1, Canada

DOI: 10.1038/sj.cdd.4400351
PMID: 10200471
Pubmed: https://pubmed.ncbi.nlm.nih.gov/10200471
Texto completo: https://doi.org/10.1038/sj.cdd.4400351

Abstract:
Lens cells demonstrate a terminal differentiation process with loss of their organelles including nuclei. Chromatin disappearance is characterised by the same changes as most apoptotic cells, i.e. condensation of chromatin and cleavage into high molecular weight fragments and oligonucleosomes. The endo-deoxyribonucleases (bicationic (Ca2+, Mg2+), mono-cationic (Ca2+ or Mg2+) and acidic non-cationic dependent nucleases) are present in lens fibre cells. Our results suggest that the acidic non-cationic nuclease (DNase II) plays a major role in chromatin cleavage. This nuclease, known to be lysosomal, is found in lens fibre nuclei and only an antibody directed against DNase II inhibits the acidic DNA cleavage of lens fibre nuclei. In addition, there must be another DNase implicated in the process which is not DNase I but appears to be a Ca2+, Mg2+ dependent molecule. Regulation of these DNase activities may be accomplished by the effect of post-translational modifications, acidic pH, mitochondrial release molecules, growth factors or oncogenes. Finally, fibre cells lose organelles without cytoplasmic elimination. The survival of these differentiated cells might be due to the action of survival factors such as FGF 1.

Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta) and pp125(FAK) by glutamate and depolarization in rat hippocampus

J Biol Chem 1996 271(46):28942-6

J C Siciliano 1 2 , M Toutant 1 , P Derkinderen 1 , T Sasaki 3 , J A Girault 1

1 INSERM U 114, Chaire de Neuropharmacologie, Collège de France, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France 2 Departamento de Histología, Facultad de Medicina, 11800 Montevideo, Uruguay 3 Department of Biochemistry, Cancer Research Institute, Sapporo Medical University, S-1 W-17, Sapporo 060, Japan

DOI: 10.1074/jbc.271.46.28942
PMID: 8910543
Pubmed: https://pubmed.ncbi.nlm.nih.gov/8910543
Texto completo: https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(18)35018-X

Abstract:
The mechanisms by which stimuli that raise cytosolic free Ca2+ concentrations in neurons can increase protein tyrosine phosphorylation are not known. Using rat hippocampal slices and cortical synaptosomes, we have examined the regulation of two highly related cytoplasmic tyrosine kinases, pp125 focal adhesion kinase (pp125(FAK)) and proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta). Membrane depolarization increased tyrosine phosphorylation of PYK2/CAKbeta and pp125(FAK). These effects were blocked by EGTA or by protein kinase C inhibitors (RO31-8220; GF109203X) and mimicked by ionomycin or phorbol 12-myristate 13-acetate, in the case of pp125(FAK), or their combination in the case of PYK2/CAKbeta. Glutamate and specific agonists of ionotropic (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate and N-methyl-D-aspartate) or metabotropic (trans-1-aminocyclopentane-1,3, -dicarboxylate) glutamate receptors stimulated the phosphorylation of pp125(FAK), but not of PYK2/CAKbeta. Glutamate effects were prevented by GF109203X. Thus, in hippocampal slices, tyrosine phosphorylation of pp125(FAK) and PYK2/CAKbeta are regulated differentially by pathways involving Ca2+ and protein kinase C. pp125(FAK) and PYK2/CAKbeta may provide specific links between neuronal activity, increases in cytosolic Ca2+ and protein tyrosine phosphorylation, which may be important for neuronal survival, and synaptic plasticity.

Siciliano_1996.pdf