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Ubiquitous presence of gluconeogenic regulatory enzyme, fructose-1,6-bisphosphatase, within layers of rat retina.

Mamczur P, Mazurek J, Rakus D - Cell Tissue Res. (2010)

Bottom Line: The abundance of the enzyme within the layers of the rat retina suggests that, in mammals in contrast to amphibia, gluconeogenesis is not restricted to one specific cell of the retina.We propose that FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species.Additionally, the nuclear localization of FBPase and of its binding partner, aldolase, in the retinal cells expressing the proliferation marker Ki-67 indicates that these two gluconeogenic enzymes are involved in non-enzymatic nuclear processes.

View Article: PubMed Central - PubMed

Affiliation: Department of Animal Molecular Physiology, Institute of Zoology, Wroclaw University, Cybulskiego 30, 50-205, Wroclaw, Poland.

ABSTRACT
To shed some light on gluconeogenesis in mammalian retina, we have focused on fructose-1,6-bisphosphatase (FBPase), a regulatory enzyme of the process. The abundance of the enzyme within the layers of the rat retina suggests that, in mammals in contrast to amphibia, gluconeogenesis is not restricted to one specific cell of the retina. We propose that FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species. Additionally, the nuclear localization of FBPase and of its binding partner, aldolase, in the retinal cells expressing the proliferation marker Ki-67 indicates that these two gluconeogenic enzymes are involved in non-enzymatic nuclear processes.

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Immunofluorescent localization of aldolase A, FBPase, and Ki-67 in rat neonatal retinal sections. Labeling by antibodies against Ki-67 (b) with propidium-iodide-counterstained nuclei (a) and merged image of a, b (c). Double-labeling with antibodies against muscle aldolase (d) and Ki-67 (e) and merged image of d, e (f). Double-labeling with antibodies against FBPase (g) and Ki-67 (h) and merged image of g, h (i). Merged images reveal co-localization of aldolase and FBPase with Ki-67. Bar 15 μm
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Fig6: Immunofluorescent localization of aldolase A, FBPase, and Ki-67 in rat neonatal retinal sections. Labeling by antibodies against Ki-67 (b) with propidium-iodide-counterstained nuclei (a) and merged image of a, b (c). Double-labeling with antibodies against muscle aldolase (d) and Ki-67 (e) and merged image of d, e (f). Double-labeling with antibodies against FBPase (g) and Ki-67 (h) and merged image of g, h (i). Merged images reveal co-localization of aldolase and FBPase with Ki-67. Bar 15 μm

Mentions: Unexpectedly, FBPase and the muscle, but not brain, isozyme of aldolase was localized in the nuclei of some neonatal retina cells (Fig. 6). Staining with antiserum against proliferation marker Ki-67 revealed the co-localization of aldolase A and FBPase with this marker suggesting that both the enzymes accumulated only within the nuclei of proliferating cells (Fig. 6). Neither FBPase (Fig. 2) nor aldolase exhibited nuclear localization in the adult retina (Fig. 7), but the aldolase A antiserum strongly stained nuclei of cultured proliferating Müller cells (Fig. 8).Fig. 6


Ubiquitous presence of gluconeogenic regulatory enzyme, fructose-1,6-bisphosphatase, within layers of rat retina.

Mamczur P, Mazurek J, Rakus D - Cell Tissue Res. (2010)

Immunofluorescent localization of aldolase A, FBPase, and Ki-67 in rat neonatal retinal sections. Labeling by antibodies against Ki-67 (b) with propidium-iodide-counterstained nuclei (a) and merged image of a, b (c). Double-labeling with antibodies against muscle aldolase (d) and Ki-67 (e) and merged image of d, e (f). Double-labeling with antibodies against FBPase (g) and Ki-67 (h) and merged image of g, h (i). Merged images reveal co-localization of aldolase and FBPase with Ki-67. Bar 15 μm
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Related In: Results  -  Collection

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Fig6: Immunofluorescent localization of aldolase A, FBPase, and Ki-67 in rat neonatal retinal sections. Labeling by antibodies against Ki-67 (b) with propidium-iodide-counterstained nuclei (a) and merged image of a, b (c). Double-labeling with antibodies against muscle aldolase (d) and Ki-67 (e) and merged image of d, e (f). Double-labeling with antibodies against FBPase (g) and Ki-67 (h) and merged image of g, h (i). Merged images reveal co-localization of aldolase and FBPase with Ki-67. Bar 15 μm
Mentions: Unexpectedly, FBPase and the muscle, but not brain, isozyme of aldolase was localized in the nuclei of some neonatal retina cells (Fig. 6). Staining with antiserum against proliferation marker Ki-67 revealed the co-localization of aldolase A and FBPase with this marker suggesting that both the enzymes accumulated only within the nuclei of proliferating cells (Fig. 6). Neither FBPase (Fig. 2) nor aldolase exhibited nuclear localization in the adult retina (Fig. 7), but the aldolase A antiserum strongly stained nuclei of cultured proliferating Müller cells (Fig. 8).Fig. 6

Bottom Line: The abundance of the enzyme within the layers of the rat retina suggests that, in mammals in contrast to amphibia, gluconeogenesis is not restricted to one specific cell of the retina.We propose that FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species.Additionally, the nuclear localization of FBPase and of its binding partner, aldolase, in the retinal cells expressing the proliferation marker Ki-67 indicates that these two gluconeogenic enzymes are involved in non-enzymatic nuclear processes.

View Article: PubMed Central - PubMed

Affiliation: Department of Animal Molecular Physiology, Institute of Zoology, Wroclaw University, Cybulskiego 30, 50-205, Wroclaw, Poland.

ABSTRACT
To shed some light on gluconeogenesis in mammalian retina, we have focused on fructose-1,6-bisphosphatase (FBPase), a regulatory enzyme of the process. The abundance of the enzyme within the layers of the rat retina suggests that, in mammals in contrast to amphibia, gluconeogenesis is not restricted to one specific cell of the retina. We propose that FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species. Additionally, the nuclear localization of FBPase and of its binding partner, aldolase, in the retinal cells expressing the proliferation marker Ki-67 indicates that these two gluconeogenic enzymes are involved in non-enzymatic nuclear processes.

Show MeSH