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REVIEW |
1 Department of Biochemistry and Molecular Biology, College of Medicine, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA
2 Center for Prostate Disease Research and Department of Surgery, Uniformed Services University, School of Medicine, Bethesda, Maryland 20814, USA
3 Eppley Institute for Cancer Research, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA
(Requests for offprints should be addressed to M-F Lin, Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska 68198-5870, USA; Email: mlin{at}unmc.edu)
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Abstract |
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 Top Abstract IntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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Introduction |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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There are two forms of PAcP in well-differentiated prostate epithelial cells: one remains intracellular, i.e. the cellular form (cPAcP); the other is secreted, i.e. the secretory form (sPAcP). The two forms of PAcP have different isoelectric point (pI) values and exhibit differences in biochemical properties (Vihko 1979, Lad et al. 1984, Boissonneault et al. 1995). Preliminary studies have revealed that they differ in glycosylation and hydrophobicity, as indicated by differential sensitivity to endoglycosidases and detergent effects on their mobility in gel filtration, fast protein liquid chromatography respectively (R Garcia, X Xia and MF Lin, unpublished data). However, the molecular bases for the physicochemical differences remain to be determined. Both forms of PAcP can hydrolyze a broad variety of small organic phosphomonoesters under acidic conditions within the optimal pH range between 4 and 6 (Vihko 1979, Van Etten 1982, Lin et al. 1983). Thus, the enzyme is classically referred to as an acid phosphatase (AcP).
The development of the prostate gland from birth through sexual maturity in the human is mirrored by the changes in cPAcP expression. The expression level of cPAcP is negligible before adolescence in males. After puberty, the cPAcP level increases and reaches a very high level in normal, well-differentiated prostate epithelial cells at approximately 0.5 mg/g wet weight of tissue (Yam 1974, Goldfarb et al. 1986). The sPAcP is predominantly secreted into seminal fluid at a physiological concentration of approximately 1 mg/ml (Ronnberg et al. 1981). Although the serum PAcP level is negligible in healthy individuals, its level is elevated in prostate cancer patients and correlates with the stage of prostate cancer. cPAcP has been a useful marker for the detection of metastatic prostate cancer, due to its cell-specific expression (Sakai et al. 1992). However, the functional role of cPAcP in normal and cancerous prostate epithelial cells was not known until a decade ago. Hence, this review focuses on discussing the role of the cPAcP-mediated signaling in prostate carcinogenesis and progression.
It should be noted that the expression level of cPAcP negatively correlates with prostate carcinogenesis, i.e. its cellular level decreases in prostate cancer cells relative to adjacent non-cancerous cells (Reif et al. 1973, Foti et al. 1977, Loor et al. 1981, Lin et al. 2001). Furthermore, the level of cPAcP corresponds inversely to prostate cancer progression, i.e. the higher the grade, the lower the cPAcP protein (Abrahamsson et al. 1988, Sinha et al. 1988, Sakai et al. 1991), despite an elevated level of sPAcP in circulation. Transcriptome-based tissue microarray analyses using HG U133A GeneChip (Affymetrix, Santa Clara, CA, USA) on 18 laser-captured, micro-dissected, paired normal and cancerous prostate specimens reveal that 100% of advanced prostate cancer specimens of Gleason scores 8 or 9 and 90% of cancer specimens of Gleason scores 6 or 7 have decreased PAcP expression compared with the adjacent normal specimens (Fig. 1
). Interestingly, the PAcP protein isolated from prostate cancer tissues and the circulation of prostate cancer patients exhibits acidic pI values, significantly lower than that of PAcP from non-cancerous tissues (Foti et al. 1977, Chu et al. 1978, Lin et al. 1983). Furthermore, the half-life of cancerous PAcP in the circulation of experimental animals is longer than that of non-cancerous PAcP (Lin et al. 1983). The decreased clearance rate of cancerous PAcP in those animals was found to be due in part to the differences in post-translational modification, including increased sialylation that is consistent with the low pI values (Lin et al. 1980, 1983). Thus, although the level of PAcP in prostate cancer cells is decreased (Fig. 1; Hakalahti et al. 1993), the elevated serum PAcP in prostate cancer patients is apparently contributed by the combined effects of increased tumor mass and the prolonged half-life of serum PAcP. Additionally, the loss of membrane polarity, as seen in advanced prostate cancer (Busch et al. 2002), may also play a significant role in this phenomenon.
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cPAcP: a neutral histidine-dependent protein phosphatase in prostatic epithelium |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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). Collectively, the data indicate that cPAcP indeed functions as a PTP in prostate epithelial cells.
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Even though PAcP uses tyrosine-phosphorylated proteins as a preferred substrate both in vitro (Lin & Clinton 1986, Boissonneault et al. 1995, Vihko et al. 2005) and in vivo (Lin et al. 1993a), recent data show that PAcP also effectively dephosphorylates lysophosphatidic acid and phosphatidylinositol 3-phosphate (PI3P), thus serving additionally as a lipid phosphatase (Tanaka et al. 2004, Vihko et al. 2005). The in vivo significance of PAcP as a lipid phosphatase in prostate carcinogenesis requires further analysis.
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Structural analysis of cPAcP |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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; Ostanin et al. 1994, Porvari et al. 1994). Using site-directed mutagenesis, it was subsequently determined that His12 and Asp258 of PAcP, but not Cys183 or Cys281, are required for its PTP activity (Zhang et al. 2001). The H12A and D258A mutants of human PAcP did not exhibit significant (detectable) AcP or PTP activities, whereas the C183A and C281A mutants essentially retained both activities completely (Zhang et al. 2001). It should be noted that Asp258 is conserved in the PTP family (Ostanin et al. 1994). The side chain of this Asp of PAcP may serve as a proton donor during the dephosphorylation reaction (Porvari et al. 1994), similar to Asp129 of the low-molecular-weight AcP, which has been reclassified as a member of a sub-family in the PTP superfamily (Ostanin et al. 1994, Zhang et al. 1994). Trp106 and His112 residues of PAcP may be responsible for the dimerization of the molecule, which greatly enhances its phosphatase activity (Porvari et al. 1994, Wasylewska et al. 2003). These results indicate that PAcP represents a novel PTP that does not belong to the classical cysteine PTP family, yet uses the same active site as well as the catalytic mechanism of AcP to execute its PTP activity.
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cPAcP: a negative regulator of cell proliferation |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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It could also be argued that the decreased cPAcP expression in poorly differentiated prostate cancer cells is due to the nature of PAcP as a differentiation antigen, i.e. decreased PAcP expression is a consequence of the loss of differentiation of prostate cancer cells. However, existing evidence suggests that this may not be the case. Among different human prostate cancer cell lines, cPAcP level inversely correlates with cell proliferation (Table 1) (Lin et al. 1992). LNCaP and MDA PCa2b cells, which express endogenous cPAcP, grow much more slowly than PC-3 and DU 145 cells, which lack PAcP expression (Table 1; Lin et al. 1992, Meng & Lin 1998, Veeramani et al. 2005). Growth stimulation of LNCaP cells by various factors, including dihydro testosterone (DHT) and epidermal growth factor (EGF) treatment, is accompanied by decreased cPAcP activity (Lin et al. 1992, 1994). Conversely, under non-permissive growth conditions, cPAcP level is elevated and cell growth is diminished (Lin et al. 1992). Furthermore, prolonged passage of LNCaP and MDA PCa2b cells in culture results in a decrease in their cPAcP expression, correlating with an increase in cell proliferation (Fig. 4; Lin et al. 1998, Igawa et al. 2002, Veeramani et al. 2005). Importantly, ectopic expression of cPAcP using a full-length cDNA in PAcP-null prostate cancer cells decreases their growth rate (Fig. 4; Lin et al. 1994, 1998, Zhang et al. 2001). Conversely, transfection of PAcP-positive LNCaP cells with anti-sense PAcP cDNA results in approximately 30% decrease in PAcP activity which correlates with the enhancement of the growth rate of those cells (Fig. 5). The role of PAcP in prostate cell growth has been validated by experiments with PAcP knock-out mice in that they showed increased epithelial cell proliferation within the anterior and dorsolateral lobes of prostate, which later developed into invasive adenocarcinomas (Vihko et al. 2005). Taken together, it is evident that cPAcP plays a critical role in regulating the proliferation of human prostate epithelial cells that leads to the generation of prostate cancer.
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HER-2/ErbB-2/Neu (HER-2): a substrate of cPAcP in prostate cancer cells |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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Studies with canine prostate epithelial cells indicated that PTP inhibitor treatment selectively increased the activity of membrane protein tyrosine kinases by inhibiting PTPs such as cPAcP and PTP-1B, which were found to be membrane-associated (Boissonneault et al. 1995), indicating that cPAcP associates with receptor tyrosine kinases. Data from different prostate cancer cell lines show that an inverse correlation exists between the cPAcP level and the p-Tyr level of a 185 kDa phosphoprotein. For example, PAcP-null prostate cancer cells had a higher p-Tyr level of the 185 kDa phosphoprotein, compared with that of PAcP-positive prostate cancer cells (Table 1
and Fig. 4; Lin & Meng 1996, Meng & Lin 1998). This has been further shown in different passages of cells, i.e. high-passage LNCaP (LNCaP C-81) cells, which have a decreased cPAcP expression, have an increased level of p-Tyr of a 185 kDa phosphoprotein, compared with that of low-passage LNCaP (LNCaP C-33) cells (Fig. 4). Furthermore, in LNCaP C-33 cells that express endogenous PAcP, inhibition of cPAcP activity by L(+)-tartrate, a classical inhibitor to PAcP, leads to increased tyrosine phosphorylation of a 185 kDa phosphoprotein (Lin & Meng 1996, Lin et al. 1998, Meng & Lin 1998). Conversely, liposome-mediated delivery of purified PAcP protein into DU 145 cells leads to a decreased specific activity of tyrosine kinases in cell lysates as well as decreased p-Tyr level of a 185 kDa phosphoprotein (Lin et al. 1993a, Lin & Meng 1996). Ectopic expression of cPAcP in PacP-null prostate cancer cells by cDNA transfection results in decreased tyrosine phosphorylation of a 185 kDa phosphoprotein (Lin et al. 1998, Meng & Lin 1998, Zhang et al. 2001). This 185 kDa phosphoprotein has been identified as HER-2, a member of the ErbB receptor protein tyrosine kinase family (Meng & Lin 1998). Decreased cPAcP expression in LNCaP C-33 cells by means of RNAi-mediated knockdown correlates with increased tyrosine phosphorylation of HER-2 (Fig. 2). Additionally, expression of cPAcP by cDNA transfection correlates with decreased phosphorylation of HER-2 protein at specific tyrosine residues, including Tyr1248, which leads to a decrease in the extracellular signal-regulated kinase/mitogen activated protein kinase (ERK/MAPK) activation as well as a reduction in cell proliferation (Zhang et al. 2001, Lee et al. 2004).
Theoretical and experimental estimates of free energy of binding revealed that PAcP has the most favorable binding towards the synthetic peptide that includes 1197–1203 amino acid residues of rat ErbB-2 when compared with several other phosphotyrosine peptides from rat EGFR and rat ErbB-2; therefore signifying the specific interaction between HER-2 and PAcP (Sharma et al. 2005). Thus, the molecular mechanism by which cPAcP regulates cell proliferation is at least in part through the p-Tyr dephosphorylation of HER-2 protein in prostate cells.
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cPAcP and HER-2 interactions in the regulation of androgen sensitivity |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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Results from several studies collectively indicate that cPAcP in prostate cancer cells is involved in determining their androgen sensitivity, although other mechanisms, e.g. AR mutations and/or gene amplification, may also contribute to this mode of regulation. In prostate cancer archival specimens, the expression level of cPAcP correlates negatively with the grade of prostate cancer, i.e. the higher the grade, the lower the cPAcP expression; it is also well established that hormone-refractory prostate cancers, in general, are of high grades (Abrahamsson et al. 1988, Sinha et al. 1988, Sakai et al. 1991). Our observations from prostate cancer cell lines corroborate the clinical data that androgen-sensitive prostate cancer cells are AR positive and express cPAcP, which correlates with slow growth rates. In contrast, androgen-independent cells, regardless of their AR expression level, usually express low/no cPAcP and have rapid growth rates (Fig. 4 and Table 1; Lin et al. 1992, 1994, 1998). Prolonged passage of androgen-sensitive LNCaP and MDA PCa2b cells in culture is accompanied by a decrease in the endogenous cPAcP expression, but not AR expression, which leads to their androgen-independent growth (Fig. 4; Igawa et al. 2002, Denmeade et al. 2003, Unni et al. 2004, F F Lin & M F Lin, unpublished data). Ectopic cPAcP expression by PAcP cDNA transfection into those AR-positive androgen-independent prostate cancer cells restores their androgen sensitivity (Fig. 4; Lin et al. 1998, 2001, Meng et al. 2000). The correlation between cPAcP expression and androgen sensitivity in culture is also reflected in xenograft animal models in that prostate cancer cells that express lower PAcP readily form subcutaneous tumors in athymic female mice and castrated athymic male mice, which have a very low level of circulating androgens (Table 2; Lin et al. 2001, Igawa et al. 2002, 2003, Denmeade et al. 2003). The molecular mechanism by which cPAcP is involved in regulating androgen-sensitive cell proliferation deserves further investigation.
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; Qiu et al. 1998, Liu et al. 2005). Apparently, activation of HER-2 is required for androgenic stimulation of prostate cancer cell proliferation.
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; Lin et al. 1998, Meng & Lin 1998, Meng et al. 2000). In PAcP cDNA-transfected stable sub-clones of LNCaP C-81 and PC-3 cells, DHT treatment results in decreased exogenous cPAcP and increased HER-2 tyrosine phosphorylation with concurrent stimulation of cell proliferation, but not in the control cells transfected with vector alone (Meng et al. 2000). The hyperactivation of HER-2 by tyrosine phosphorylation in androgen-independent prostate cancer cells is in keeping with the amplification of HER-2 gene in the hormone-refractory growth of breast and ovarian cancer cells (Press et al. 1990, Meden & Kuhn 1997, Press et al. 1997, Menard et al. 2001) as an alternative mechanism for stimulating the growth of steroid hormone-dependent cancers in the absence of ligand. Hence, it is clear that, despite the requirement for AR, the interaction between cPAcP and HER-2 can regulate the androgen sensitivity of the prostate cancer cells. The involvement of HER-2 in hormone-refractory prostate cancer is further supported by similar observations in androgen-independent LAPC4 cells (Craft et al. 1999, Mellinghoff et al. 2004). An aberrant regulation of either molecule can contribute to androgen-independent proliferation of prostate cancer cells.
It is conceivable that in PAcP-null prostate cancer cells, activated HER-2 transmits signals via p52Shc to increase downstream ERK/MAPK activity. Activated ERK/MAPK may increase the ligand-independent activity of AR by phosphorylation that results in elevated androgen-independent prostate cancer proliferation (Fig. 7; Yeh et al. 1999, Meng et al. 2000, Lee et al. 2003, 2004). This activated HER-2 signal can also up-regulate androgen-independent induction of PSA synthesis and secretion in those prostate cancer cells (Yeh et al. 1999, Wen et al. 2000, Lee et al. 2003, 2004). This is particularly evident in HER-2-impaired LNCaP cells, which showed impaired induction of PSA by androgen (Lee et al. 2003, Liu et al. 2005). Taken together, these results provide a mechanistic explanation for the apparent paradox arising from clinical observations in advanced hormone-refractory prostate cancer that they express functional AR, but are nevertheless androgen independent. In those cells, the expression of cPAcP is decreased, indicating that HER-2 is activated by tyrosine phosphorylation (Loor et al. 1981, Lin et al. 2001, Pontes et al. 1981, Solin et al. 1990, Sakai et al. 1993), while the HER-2 gene is not amplified (Table 3; Signoretti et al. 2000, Osman et al. 2001). Furthermore, in prostate cancer specimens, the phosphorylation level of ERK/MAPK is elevated (Gioeli et al. 1999, Price et al. 1999) with the elevation of serum PSA (Chu & Lin 1998). Thus, down-regulation of tyrosine phosphorylation of HER-2 by cPAcP plays a key role in determining the androgen sensitivity of prostate cancer cells.
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). PI3K-Akt is found to be activated in prostate tissue of PAcP knock-out mice (Vihko et al. 2005). Thus, loss of PAcP in prostate epithelial cells might also activate the PI3K-Akt pathway, in addition to the HER-2–MAPK pathway, leading to the tumor progression. Collectively, in the absence or presence of low levels of cPAcP, activated HER-2 by virtue of its increased tyrosine phosphorylation, can transduce its signals through PI3K-Akt to confer androgen-independent cell proliferation (Wen et al. 2000). Alternatively, since PAcP can directly dephosphorylate PI3P, loss of PAcP in prostate cancer cells can lead to the accumulation of PI3P that can activate the downstream Akt (Fig. 7; Vihko et al. 2005). Further investigations are required to clarify whether cPAcP functions independently of phosphatase and tensin homolog (PTEN) or interacts with PTEN in regulating the Akt pathway. PTEN-independent Akt activation by HER-2 and PAcP may thus play an additional role in androgen-independent proliferation of prostate cancer cells, despite the fact that PTEN may be inactivated by mutation leading to the constitutive activation of Akt (Li et al. 1997, Reiss et al. 2000). This notion is supported by observations that LNCaP C-33 cells, which have a mutant, nonfunctional PTEN gene and, hence, express activated Akt, are still androgen sensitive (Lin et al. 1998, 2003, Bastola et al. 2002). Further studies are needed to define the role of Akt in the development of androgen-independent prostate cancer under clinical conditions. It is also important to identify whether other pathways that, in conjunction with the HER-2–MAPK signaling pathway, may further promote AR activation and hormone-refractory prostate cancer proliferation. |
cPAcP: a tumor suppressor phosphatase |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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; Reif et al. 1973, Lin et al. 2001). Furthermore, in cancerous tissue, PAcP mRNA exhibits sequence heterogeneity in the coding and non-coding regions (Vihko et al. 1988, Van Etten et al. 1991, Lin et al. 1993b); and cPAcP protein in cancerous tissue has distinct biochemical properties, such as different pI values, from non-cancerous tissues (Foti et al. 1977, Chu et al. 1978, Lin et al. 1983). Thus, it is tempting to speculate that the molecular and biochemical differences between cPAcP in cancerous versus non-cancerous prostate cells, which can lead to differences in specificity and kinetics of the enzyme as reported for other PTPs (Wishart et al. 1995, Cirri et al. 1996), may make a critical contribution to the development of prostate cancer.
Secondly, among different prostate cancer cell lines, cPAcP level inversely correlates with tumorigenicity and growth rate, both of which are the cellular correlates of cancer and indispensable for tumor progression. It is well known that PAcP-null PC-3 and DU 145 cells are highly tumorigenic, as indicated by higher soft agar colony formation and tumor growth in experimental animals, and are rapidly growing compared with the PAcP-positive LNCaP and MDA PCa2b cells (Table 1). Furthermore, in those PAcP-positive cells, cPAcP level decreases upon passage corresponding to the increase in the tumorigenicity as well as the cell growth rate (Fig. 4). Similarly, decreasing expression of endogenous cPAcP by transfection of its small interfering (si)RNA or PAcP cDNA in the anti-sense orientation into PAcP-positive LNCaP cells increases HER-2 tyrosine phosphorylation and cell proliferation (Figs 2 and 5).
Thirdly, ectopic expression of the wild-type cPAcP by cDNA transfection into rapidly growing, PAcP-null human prostate cancer cells reduces their growth rates and tumorigenicity; as shown in a soft agar anchorage-independence assay and xenograft animal models (Fig. 4) (Lin et al. 1994, 1998, 2001, Zhang et al. 2001). Stable subclones of LNCaP C-81 cells transfected with the wild-type PAcP cDNA are less tumorigenic than cells transfected with vector alone (Table 2) (Igawa et al. 2003). The direct tumor-suppressive activity of cPAcP has been demonstrated in xenograft animal models in that a single intra-tumoral injection of the wild-type PAcP cDNA into established subcutaneous LNCaP C-81 cell-induced tumors results in dephosphorylation of HER-2 in those tumors with concomitant suppression of their growth (Igawa et al. 2003). The expression level of cPAcP in those PAcP cDNA-injected subcutaneous C-81 tumors was high at 1 week post-injection and the level of cPAcP in those tumors gradually dropped almost to the level of controls by 6 weeks, correlating with the tyrosine phosphorylation of HER-2 (Igawa et al. 2003). A PTPase activity-dead mutant of PAcP exhibits dramatically reduced tumor-suppressive activity in these assays, suggesting that the PTP activity of cPAcP, acting via the down-regulation of HER-2 activity, plays a critical role in the tumor suppression (Igawa et al. 2003). Since nude mice were used for the above experiments the influence of other factors, such as T-cell immune response to the injected PAcP, could be overruled. Nevertheless, under clinical conditions, for example, within an intact human body, prostate cancer might be exposed to a variety of factors including immunological responses that could operate along with other mechanisms to influence the outcome of cancer. Thus, PAcP may be involved in prostate cancer suppression via multiple pathways.
Finally, PAcP knock-out mice show increased cell proliferation followed by prostatic intraepithelial neoplasia (PIN) lesions, which later progress into invasive adenocarcinomas (Vihko et al. 2005). These observations are collectively consistent with the notion that cPAcP functions as a tumor suppressor by dephosphorylating HER-2 (Fig. 2) and that decreased cPAcP expression, observed in early stages of prostate cancer, is one of the key determinants for prostate cancer progression.
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Potential applications of cPAcP in prostate cancer therapy |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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PAcP expression exhibits prostate specificity and thus its promoter elements may be used as a tool for targeting prostate cancer cells. The tissue-specific activity of the PAcP promoter has already been reported (Zelivianski et al. 1998, 2002, Shan et al. 2003). For example, deletion analyses of the PAcP promoter revealed that p779 (0 to –779 bp fragment) has the basal promoter activity and p1356 (0 to –1356 bp fragment) exhibits the prostate specificity (Zelivianski et al. 2004). This p1356 promoter fragment is active even in aggressive prostate cancer cells, such as PC-3 and DU 145 cells, although they lack endogenous PAcP expression (Zelivianski et al. 2002, 2004). Despite the fact that the molecular mechanism by which PAcP expression is decreased in prostate cancer remains unknown, one strategy to exploit the tissue specificity of the PAcP promoter for anti-tumor therapy is to use an expression vector that encodes a cytotoxic protein under the transcriptional control of the PAcP promoter element, for example, p1356. This fragment is active even in advanced prostate cancer cells and can drive the expression of the cytotoxic protein in a prostate-specific manner. Alternatively, a mini-gene construct with PAcP cDNA under the transcriptional control of the p1356 fragment may be used to inhibit the growth of prostate cancer cells with minimal side effects. However, further in vitro experiments and xenograft animal studies are needed to determine the efficacy of those elements of the PAcP promoter prior to their application for prostate cancer therapy in human patients.
Another avenue for the therapeutic application of PAcP under clinical conditions is the utilization of the immunogenic property of the PAcP protein in prostate cancer patients. This is supported by the findings of active immunization studies for prostate cancer based on prostatic antigens such as PSA and PAcP (McNeel et al. 2001; for review, see Fong & Small 2003). Patients with metastatic prostate cancer responded to the immunization of dendritic cells pulsed with PAcP protein with more than 50% of the patients developing an immune response (Fong et al. 2001). Phase 1 and phase 2 trials with dendritic cell-based PAcP vaccination for androgen-independent prostate cancer led to a greater than 50% decrease in PSA (Small et al. 2000, Burch et al. 2004). Further clinical trials on a larger scale are required to assess the efficacy of PAcP-based vaccination. Studies are also needed for the potential use of the cancer-associated PAcP isolated from prostate cancer patients as an immunogen designed to improvetheefficacyofprostate cancer immunotherapy.
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Conclusion and perspectives |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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Acknowledgements |
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Funding |
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The project on PAcP is currently supported in part by NIH grants CA88184, P20RR017675 and P20RR018759; and the UNMC Graduate Student Fellowship (T-C Y; S-J C). The authors declare that there is no conflict of interest that would prejudice the impartiality of this scientific work.
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References |
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TopAbstractIntroductioncPAcP: a neutral histidine...Structural analysis of cPAcPcPAcP: a negative regulator...HER-2/ErbB-2/Neu (HER-2): a...cPAcP and HER-2 interactions...cPAcP: a tumor suppressor...Potential applications of cPAcP...Conclusion and perspectivesReferences |
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