IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
Immunocytochemical Localization of NTPDases1 and 2 in the Neural Retina of Mouse and Zebrafish
Autor/es:
MJ RICATTI, LD ALFIE, EG LAVOIE, J SEVIGNY, PJ. SCHWARZBAUM AND MP FAILLACE
Revista:
SYNAPSE
Editorial:
WILEY-LISS, INC.
Referencias:
Lugar: Nueva York ; Año: 2008 vol. 63 p. 291 - 307
ISSN:
0887-4476
Resumen:
ABSTRACT Ectonucleoside triphosphate diphosphohydrolases (E-NTPDases) are a
family of membrane-bound enzymes that hydrolyze extracellular di- and triphosphate
nucleosides. E-NTPDases have been proposed to control extracellular nucleotide levels
that mediate intercellular communication by binding to specific membrane receptors.
Here we show a detailed immunocytochemical localization of two enzymes of the ENTPDase
family in the retinal layers of two vertebrate species, namely, the mouse and
the zebrafish. In the mouse retina, NTPDase2 was chiefly localized in Mu¨ ller glia and
ganglion cell processes. NTPDase1 was located on neurons as well, since it was
expressed by horizontal and ganglion cell processes, suggesting that nucleotides such as
ATP and ADP can be hydrolyzed at the surface of these cells. NTPDase1 was also
detected in intraretinal blood vessels of the mouse. Regarding zebrafish, NTPDases1
and 2 seem to be differentially localized in horizontal cell processes, photoreceptor segments,
and ganglion cell dendrites and axons, but absent from Mu¨ ller glia. Moreover,
NTPDases1 and 2 appear to be expressed within the germinal margin of the zebrafish
retina that contains proliferative and differentiating cells. Retinal homogenates from
both species exhibited ecto-ATPase activity which might be attributed at least to
NTPDases1 and 2, whose expression is described in this report. Our results suggest a
compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the
retinal layers, supporting a relevant role for extracellular nucleotide mediated-signaling
in vertebrate retinas. Synapse 63:291307, 2009. VVC 2008 Wiley-Liss, Inc.
family of membrane-bound enzymes that hydrolyze extracellular di- and triphosphate
nucleosides. E-NTPDases have been proposed to control extracellular nucleotide levels
that mediate intercellular communication by binding to specific membrane receptors.
Here we show a detailed immunocytochemical localization of two enzymes of the ENTPDase
family in the retinal layers of two vertebrate species, namely, the mouse and
the zebrafish. In the mouse retina, NTPDase2 was chiefly localized in Mu¨ ller glia and
ganglion cell processes. NTPDase1 was located on neurons as well, since it was
expressed by horizontal and ganglion cell processes, suggesting that nucleotides such as
ATP and ADP can be hydrolyzed at the surface of these cells. NTPDase1 was also
detected in intraretinal blood vessels of the mouse. Regarding zebrafish, NTPDases1
and 2 seem to be differentially localized in horizontal cell processes, photoreceptor segments,
and ganglion cell dendrites and axons, but absent from Mu¨ ller glia. Moreover,
NTPDases1 and 2 appear to be expressed within the germinal margin of the zebrafish
retina that contains proliferative and differentiating cells. Retinal homogenates from
both species exhibited ecto-ATPase activity which might be attributed at least to
NTPDases1 and 2, whose expression is described in this report. Our results suggest a
compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the
retinal layers, supporting a relevant role for extracellular nucleotide mediated-signaling
in vertebrate retinas. Synapse 63:291307, 2009. VVC 2008 Wiley-Liss, Inc.
Ectonucleoside triphosphate diphosphohydrolases (E-NTPDases) are a
family of membrane-bound enzymes that hydrolyze extracellular di- and triphosphate
nucleosides. E-NTPDases have been proposed to control extracellular nucleotide levels
that mediate intercellular communication by binding to specific membrane receptors.
Here we show a detailed immunocytochemical localization of two enzymes of the ENTPDase
family in the retinal layers of two vertebrate species, namely, the mouse and
the zebrafish. In the mouse retina, NTPDase2 was chiefly localized in Mu¨ ller glia and
ganglion cell processes. NTPDase1 was located on neurons as well, since it was
expressed by horizontal and ganglion cell processes, suggesting that nucleotides such as
ATP and ADP can be hydrolyzed at the surface of these cells. NTPDase1 was also
detected in intraretinal blood vessels of the mouse. Regarding zebrafish, NTPDases1
and 2 seem to be differentially localized in horizontal cell processes, photoreceptor segments,
and ganglion cell dendrites and axons, but absent from Mu¨ ller glia. Moreover,
NTPDases1 and 2 appear to be expressed within the germinal margin of the zebrafish
retina that contains proliferative and differentiating cells. Retinal homogenates from
both species exhibited ecto-ATPase activity which might be attributed at least to
NTPDases1 and 2, whose expression is described in this report. Our results suggest a
compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the
retinal layers, supporting a relevant role for extracellular nucleotide mediated-signaling
in vertebrate retinas. Synapse 63:291307, 2009. VVC 2008 Wiley-Liss, Inc.Synapse 63:291307, 2009. VVC 2008 Wiley-Liss, Inc.