Subcellular localization of aldolase B

Abstract

The localization of the aldolase B isozyme was determined immunohistochemically in rat kidney and liver using a polyclonal antibody. Aldolase B was preferentially localized in a nuclear region of hepatocytes from the periportal region and was absent in those from the perivenous region. Aldolase B was also preferentially localized in the proximal tubules and was absent in other structures of the renal cortex as well as in the renal medulla. Using reflection confocal microscopy, the enzyme was preferentially localized in a nuclear position in liver and renal cells, which was similar to the cellular and intracellular location found for the gluconeogenic enzyme fructose‐1,6‐bisphosphatase (Sáez et al. [1996] J. Cell. Biochem. 63:453–462). Subcellular fractionation studies followed by enzyme activity assays revealed that aldolase activity was associated with subcellular particulate structures. Overall, the data suggest that different aldolase isoenzymes are needed in the glycolytic and gluconeogenic pathways. J. Cell. Biochem. 78:62–72, 2000. © 2000 Wiley‐Liss, Inc.

A cryptic role of a glycolytic–gluconeogenic enzyme (aldolase) in amino acid transporter turnover in Aspergillus nidulans

“…Previous studies in mammalian cells have shown that FBAs are located also in the nucleus of different cell types Dzugaj, 2004, 2008;Saez and Slebe, 2000). Precisely, it has been shown that aldolase A is located in the cytoplasm as well as in the nuclei of porcine cardiomyocytes and also of porcine and rat smooth muscle cells in heterochromatin regions Dzugaj, 2004, 2008).…”

“…The role of FBAs in cell nuclei remains unknown and is probably related with their involvement in a number of cellular processes unrelated with their primary function (see below). FBAs nuclear localization might be possible to link cellular metabolism with biological processes related with regulation of gene expression (Saez and Slebe, 2000). Moreover, we have shown that targeting of the AgtA aspartate-glutamate transporter in the plasma membrane of A. nidulans is strongly affected by low enzyme levels resulting from the low fbaA transcriptional levels.…”

“…Precisely, it has been shown that aldolase A is located in the cytoplasm as well as in the nuclei of porcine cardiomyocytes and also of porcine and rat smooth muscle cells in heterochromatin regions Dzugaj, 2004, 2008). Additionally, aldolase B is located in the nucleus of rat hepatocytes and renal cells (Saez and Slebe, 2000). The role of FBAs in cell nuclei remains unknown and is probably related with their involvement in a number of cellular processes unrelated with their primary function (see below).…”

“…The subcellular localization of FBP aldolases, similarly to most other glycolytic enzymes such as glyceraldehyde-3-phosphate dehydrogenase (GAPDH), is mainly in the cytoplasm, but some evidence for their presence in the nucleus also exists (Tuinen and Riezman, 1987;Saez and Slebe, 2000). Recent studies have further revealed that certain enzymes of the glycolytic and gluconeogenic systems may be associated with specific subcellular particulate elements, among them F-actin, and that the complexes of sequential metabolic enzymes are often bound to structural elements of the cell (Tuinen and Riezman, 1987;Saez and Slebe, 2000;Benziane et al, 2007).…”

“…Recent studies have further revealed that certain enzymes of the glycolytic and gluconeogenic systems may be associated with specific subcellular particulate elements, among them F-actin, and that the complexes of sequential metabolic enzymes are often bound to structural elements of the cell (Tuinen and Riezman, 1987;Saez and Slebe, 2000;Benziane et al, 2007).…”