REVIEW |
Correspondence to: Albert A.J. Verhofstad, Dept. of Pathology, University Medical Centre Nijmegen, PO Box 9101, 6500 HB Nijmegen, The Netherlands. E-mail: A.Verhofstad@pathol.azn.nl
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Summary |
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Ornithine decarboxylase (ODC) is a key enzyme in polyamine biosynthesis. Increased polyamine levels are required for growth, differentiation, and transformation of cells. In situ detection of ODC in cells and tissues has been performed with biochemical, enzyme cytochemical, immunocytochemical, and in situ hybridization techniques. Different localization patterns at the cellular level have been described, depending on the type of cells or tissues studied. These patterns varied from exclusively cytoplasmic to both cytoplasmic and nuclear. These discrepancies can be partially explained by the (lack of) sensitivity and/or specificity of the methods used, but it is more likely that (sub)cellular localization of ODC is cell type-specific and/or depends on the physiological status (growth, differentiation, malignant transformation, apoptosis) of cells. Intracellular translocation of ODC may be a prerequisite for its regulation and function. (J Histochem Cytochem 50:11431160, 2002)
Key Words: ornithine decarboxylase, polyamines, localization, enzyme cytochemistry, immunocytochemistry, in situ hybridization, green fluorescent protein
Ornithine decarboxylase (ODC, EC 4.1.1.17) converts the amino acid ornithine to the diamine putrescine, which is the obligatory precursor in the biosynthesis of the polyamines spermidine and spermine. Together with the two other polyamine-regulating enzymes, S-adenosylmethionine decarboxylase (AdoMetDC) and spermidine/spermine N1-acetyltransferase (SSAT), ODC controls the cellular balance of polyamines (Fig 1).
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Polyamines are multifunctional organic bases that play an essential role in cell growth, differentiation, and malignant development (
The enzyme exhibits rapid and diverse changes in biological activity as an early response to virtually all growth-promoting stimuli to cells, including those of hormones, drugs, growth factors, mitogens, and tumor promoters (
The native enzyme is active as a homodimer and uses pyridoxal L-phosphate as a co-factor. ODC can exist in multiple forms, but it is not yet clear whether these different forms are isoenzymes, chemically modified enzyme proteins, or mutated ODC proteins (
ODC activity is controlled at the transcriptional, translational, and post-translational levels and is under strict negative feedback control by its polyamine products (
Despite extensive research, the precise role of the ODC/polyamine system in cell physiology remains to be clarified. Insight into the exact cellular and subcellular localization of ODC might provide valuable information on the role of this system in cell physiology. As summarized in Table 1, several approaches have been applied to localize ODC expression or activity in cells using biochemical, enzyme cytochemical, immunocytochemical, and hybridocytochemical methods. In this review, results obtained with the various methods with respect to localization patterns of ODC in cells (Table 2) and tissues in various organ systems (Table 3) in relation to polyamine functions are presented and interpreted.
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Distribution Patterns of ODC in Cells and Tissues |
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Fractionated Cells
Activity of ODC can be determined by measuring production of 14CO2 (
The CO2-trapping technique has been used to determine ODC activity in subcellular fractions of rat prostate (
The results of fractionation studies to localize ODC activity are rather conflicting and show ODC activity present in both cytoplasm and nucleoplasm or nucleoli. Nuclear and cytoplasmic ODC may be differently regulated because ODC activity induced by growth-promoting stimuli is increased in the cytoplasm only. On the other hand, either contamination of the nuclear fraction with cytosolic ODC or leakage of nuclear ODC to the cytoplasm may have occurred during homogenization of tissues, which led to false conclusions.
Cultured Cells
Intracellular localization of ODC in cultured cells was studied for the first time in stimulated murine macrophage-like RAW 264 cells using a polyclonal antiserum against ODC that had been purified from this cell line (
Bachrach and co-workers immunocytochemically detected ODC in transformed mouse fibroblasts, human epithelial carcinoma cells, and lymphoblasts from leukemia patients (
With our monoclonal antibody MP16-2, we examined localization of ODC in various human and murine cell lines (
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We have investigated the subcellular distribution patterns of ODC in more detail by using fusion proteins consisting of ODC and enhanced green fluorescent protein (EGFP). The expression vector pEGFP-N1 was subcloned with or without a human ODC cDNA fragment. Subsequently, EGFP and ODCEGFP were expressed in cultured HeLa cells. Typical results of expression patterns of EGFP alone or the fusion protein are shown in Fig 2B2D and Fig 2G. Expression of EGFP alone in these cells was homogeneous throughout the cytoplasm and nuclei of the cells (Fig 2B). In contrast, expression patterns of ODCEGFP constructs were heterogeneous (Fig 2C and Fig 2D). Confluent cells showed cytoplasmic perinuclear staining, whereas dividing cells showed heterogeneous staining of the nucleus. When cells were treated with polyamines to induce antizyme-regulated ODC degradation, ODC was predominantly localized in the nucleus (Fig 2G). Immunostaining of antizyme in these cells showed that antizyme co-localizes with ODC in the nucleus (Fig 2F and Fig 2G). These results suggest that ODC accumulates in the nucleus after antizyme induction. Further experiments using inhibitors of proteasomal degradation and/or nuclear translocation are needed to clarify the role of ODC translocation to the nucleus in antizyme-induced degradation of ODC.
It is not yet clear whether the distinct changes in ODC expression or localization patterns actually reflect progression through the cell cycle. The ODC gene has been described as a cell cycle-dependent gene that is only weakly expressed in quiescent cells. Its expression is strongly increased in proliferating cells (
In general, higher levels of ODC were detected in most studies in smaller, more rapidly growing cells. ODC expression appears to be correlated with cell proliferation and cell transformation. Translocation of ODC in conjunction with cytoskeletal systems might be an important regulatory event in these cellular processes. In situ detection of ODC may therefore be useful as a biomarker for (malignant) cell proliferation or, conversely, as an indicator for sensitivity to anti-proliferative drugs, as suggested by
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Nervous System |
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Considerable evidence exists for a role of the ODC/polyamine system in neurobiological systems (for review see
In rat and mouse brain, ODC activity is highest during birth and declines after the first week to a low adult level (
A sharp rise in brain ODC activity has also been found in various pathological conditions of the brain (
In conclusion, ODC expression may be closely associated with normal and pathological processes in the brain. However, whether induction of ODC has real pathological consequences or is merely a trophic response to stress or an epiphenomenon remains to be established. During brain maturation, ODC localization is restricted to neurons, which is in agreement with the proposed role of the ODC/polyamine system in neuronal migration, axogenesis, synaptogenesis, and activity of ion channels (
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Urogenital System |
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ODC is particularly active in epithelial cells of rodent kidneys and accessory sex organs and is regulated by sex hormones that induce hyperplastic and hypertrophic responses (
Localization of ODC expression in mouse or rat kidney after testosterone treatment has been studied with use of enzyme cytochemical (
Prostate cells of human and rat origin produce polyamines at high levels. Its apparent functions are related to cell proliferation and secretory activities. ODC has been localized immunocytochemically in rat prostate gland, revealing heterogeneous cytoplasmic staining of acinar cells (
Elevated activity of ODC has been associated with androgen-dependent proliferation of Sertoli cells and germ cells in testis and of principal cells in the epididymal epithelium (
ODC activity is strongly induced in the ovary of rat, hamster, and chicken during the ovalutory cycle (
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Gastrointestinal Tract |
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Cell growth in the gastrointestinal tract, induced by food, hormones, refeeding after starvation, and intestinal adaptation is paralleled by increases in ODC activity (
The liver has been an important organ in the initial studies of regulation of ODC activity. ODC expression was rapidly and strongly elevated during liver regeneration before the onset of nucleic acid and protein synthesis (
The role of the ODC/polyamine system in proliferation of the gastric oxyntic cell is still a matter of debate. An increase in mucosal ODC activity could not be detected biochemically in response to refeeding or gastrin stimulation. Furthermore, treatment with DFMO had no effect on normal gastric epithelial growth and only partially prevented the trophic response to refeeding, but did inhibit the trophic action of gastrin. However, immunocytochemical analysis of stomach epithelium of fasted animals showed that ODC protein was present only in a narrow band of cells at the base of gastric pits and at the top of oxyntic glands, which increased after feeding or gastrin stimulation (
ODC and polyamine levels are increased during rapid growth phases in maturation and recovery of intestinal epithelium during adaptive hyperplasia, during lactation, after intestinal obstruction, during post-starvation refeeding, and after feeding with lectins (
These studies and studies using cultured enterocyte cell lines (
ODC activity is increased in the early stages of cell growth in intestine and pancreas during the neonatal period (
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Malignancies |
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ODC expression is upregulated in cancer cells, resulting in high basal levels of ODC and polyamines in many tumor types. Recent studies show that ODC overexpression coincides with expression of oncogenes during cell transformation (
The role of the ODC/polyamine system in cancer progression has been extensively studied in a murine multistep model of carcinogenesis in the skin (reviewed by
Immunolocalization studies of human skin showed that ODC is present in both basal and corneal layers of normal skin (
Subcellular localization studies of ODC in normal human keratinocytes revealed that ODC is present in the perinuclear/nuclear region (
ODC localization studies have also been performed in some other types of malignancies, i.e., hepatocellular carcinoma (
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On the Subcellular Localization of ODC |
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In the past 30 years, ODC expression has been found in either the cytoplasm, the nucleus, or both. It is difficult to synthesize these rather inconclusive studies into a general concept of ODC localization and its significance in cell physiology. Interpretation of ODC distribution patterns is further hampered by the little knowledge on the exact molecular actions of its products, the polyamines.
One possibility is that these inconsistent results are based on methodological problems with respect to the (lack of) sensitivity and/or specificity of the various methods used for the localization of ODC. Alternatively, the various localization patterns may reflect differences among cell types, their particular biological behavior (proliferation, differentiation, apoptosis), or the onset of ODC expression. Furthermore, (trans)location of ODC may be an important mechanism to control expression of ODC.
These aspects of subcellular localization patterns of ODC in relation to polyamine function are discussed in detail in the next paragraphs.
Methodological Problems
Early studies focused on biochemical measurement of ODC activity in fractionated cell preparations. Activity of the enzyme was found in cytoplasmic as well as nuclear fractions, and particularly in nucleoli. This biochemical method is highly sensitive, but care must be taken lest improper homogenization procedures or storage of frozen supernatants cause artifacts due to the metabolism of ornithine via the mitochondrial pathway (
Development of the highly specific and irreversibly binding ODC inhibitor DFMO enabled cytochemical localization of ODC activity using fluorescent or radioactively labeled derivatives of DFMO. Most of these studies report that ODC is localized in both cytoplasm and nuclear compartments. Because DFMO is highly specific for ODC and does not react with the inactive ODCantizyme complex (
Immunocytochemical detection of ODC revealed different localization patterns, depending on the cell system studied and the antibody used. These patterns varied from cytoplasmic or (peri)nuclear localization to localization in both cytoplasm and nucleus. A problem in ODC immunocytochemistry is that information on the nature or activity of the detected ODC protein cannot be obtained. ODC antibodies may also react with catalytically inactive forms of ODC, e.g., monomeric subunits of ODC or monomers bound to the ODCinhibitory antizyme protein. Furthermore, ODC antibodies may crossreact with the antizyme inhibitor, which shows a high homology with ODC protein but lacks its catalytic activity (
In addition to differences in specificity of antibodies against ODC, effects of cell and tissue preparation procedures, such as fixation, permeabilization, dehydration, and embedding, can greatly affect preservation and/or accessibility of the ODC protein for the antibodies. We recently attempted to systematically develop a reliable method for immunocytochemical detection of ODC (
In contrast to the findings obtained with biochemical and enzyme cytochemical studies, immunocytochemical studies of ODC showed that ODC is present mainly in the cytoplasm. This discrepancy may mean that catalytically active nuclear ODC exists in a complexed or cryptic form or is less accessible for antibodies to bind. On the other hand, cytosolic ODC may exist in an immunologically active but enzymatically inactive form. Immunocytochemical detection of ODC in ODC-overproducing CHO cells showed considerably more ODC in the cytoplasm than in the nucleus. In contrast, ODC detected by autoradiography using radiolabeled DFMO was evenly distributed over the cell (
In situ hybridization studies using a labeled cRNA or cDNA probe specifically hybridizing with ODC mRNA have been performed on mouse, rat, and human tissues (Table 1). The localization patterns of ODC mRNA were, at least partially, consistent with ODC localization patterns obtained in biochemical and immunocytochemical studies. However, many other experiments have provided evidence for translational and post-translational control of ODC (
Cell Physiological Aspects
Technical aspects may be responsible for the variety of staining patterns, but it may also be possible that the localization of ODC in cytoplasm and nucleus varies depending on the physiological state of the cell. ODC may be expressed in a particular cell type or subcellular compartment when its products, the polyamines, are needed there. Although intracellular transport of polyamines cannot be ruled out, targeting of ODC to the functional site of polyamines may be the actual transport mechanism.
Polyamines are implied to have an essential role in mitotic spindle organization and modulation of DNA structure and stability. Therefore, nuclear ODC may be an important source for nuclear polyamines. An argument against this proposition is that, to produce nuclear spermidine and spermine in addition to their precursor putrescine, the other biosynthetic enzymes of the ODC/polyamine system also must be translocated/present in the nucleus, for which no evidence (yet) exists. However, putrescine may not serve solely as a precursor for the production of spermidine and spermine but may exert cellular effects of its own, as found recently in intestinal epithelial cells (
Localization studies of polyamines using autoradiographic, cytochemical, and immunocytochemical techniques have confirmed the presence of polyamines in the nucleus (
The vast majority of the results presented in Table 2 and Table 3 show a cytoplasmic localization of ODC. Furthermore, most studies in which ODC localization was examined before and after stimulation report on a cytoplasmic rather than a nuclear localization of stimulated ODC.
The precise functional role of the ODC/polyamine system in the cytoplasm still needs to be elucidated, but many studies suggest that polyamines play essential roles in the machinery of protein biosynthesis. This hypothesis is further supported by immunoelectron microscopic studies of ODC and polyamines in which the label was closely associated with rough endoplasmic reticulum and polyribosomal structures, respectively (
Recent studies in cultured cells using confocal laser scanning microscopy (
Membrane localization of ODC appeared to be related to structural elements, i.e., actin or keratin cytoskeletal elements (
Translocation of ODC may also have a functional role in its degradation. It is well established that antizyme binds to ODC and targets it to the proteasome for degradation. Antizyme has been localized in the cytoplasm but also in the nucleus, especially in cells with high ODC expression (
The variety of ODC distribution patterns as observed in different tissue types may be explained by the various roles of polyamines in cell metabolism and growth. As expected, ODC expression is prominent in the proliferating fraction of rapidly growing tissues. For example, ODC activity is particularly high in tissues with high cell turnover, e.g., intestinal epithelium, which require a constant supply of polyamines for growth, renewal, and metabolism. In contrast, highest activity of ODC has been found in the prostate, in which polyamines are synthesized for export rather than for intracellular use. In transgenic mice that overexpress human ODC due to a ubiquitous promoter, abnormalities were found only in testis and brain (
ODC distribution patterns may depend not only on the cell type but also on cell kinetic behavior, because ODC activity and polyamine pools change during cell growth, differentiation, and cell death in a transient manner. Therefore, the onset of ODC expression can vary greatly among cells, depending on their physiological status, creating heterogeneous and apparently inconsistent results in cytochemical studies.
In conclusion, intracellular localization of ODC is not static but is subject to highly dynamic processes. Future studies in living cells using real-time analysis of fluorescence-tagged ODC and ODC regulatory proteins (antizyme, antizyme inhibitor) are needed to further unravel the complexity of the regulation and function of the ODC/polyamine system.
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Acknowledgments |
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Supported by the Dutch Cancer Society (grants NKB-93-599, NKB-98-1807) and the Nijbakker Morra Foundation.
We wish to thank Dr Lo Persson and Prof dr Olli Jänne for generously providing us with the human ODC cDNA. We gratefully acknowledge Prof dr Olle Heby and Dr Jonas Nilsson for kindly supplying antizyme antiserum.
Received for publication November 6, 2001; accepted April 1, 2002.
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