Acid Phosphatases

Kaija, Helena; Patrikainen, Lila; Alatalo, Sari L.; Väänänen, H. Kalervo; Vihko, Pirkko

doi:10.1016/b978-012088562-6/50011-x

Cited by 3 publications

(8 citation statements)

References 133 publications

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“…PAP was discovered over 70 years ago and was used as a diagnostic marker for prostate cancer in humans [21] , [22] , [23] , [24] , [25] , [26] . Over time, numerous antibodies were raised against human PAP.…”

Section: Resultsmentioning

confidence: 99%

“…This lack of immunoreactivity could be due to the lower percent identity/similarity between hPAP and rPAP relative to hPAP and mPAP ( Table 1 ). PAP is a glycosylated protein [23] , so differences in glycosylation might also affect immunoreactivity. While our research with PAP was in progress [17] , Biømeda went out of business, making it impossible to obtain this antibody for further studies.…”

Section: Resultsmentioning

confidence: 99%

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Prostatic Acid Phosphatase Is Expressed in Peptidergic and Nonpeptidergic Nociceptive Neurons of Mice and Rats

Taylor-Blake

Zylka

2010

PLoS ONE

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Thiamine monophosphatase (TMPase, also known as Fluoride-resistant acid phosphatase or FRAP) is a classic histochemical marker of small- to medium-diameter dorsal root ganglia (DRG) neurons and has primarily been studied in the rat. Previously, we found that TMPase was molecularly identical to Prostatic acid phosphatase (PAP) using mice. In addition, PAP was expressed in a majority of nonpeptidergic, isolectin B4-binding (IB4+) nociceptive neurons and a subset of peptidergic, calcitonin gene-related peptide-containing (CGRP+) nociceptive neurons. At the time, we were unable to determine if PAP was present in rat DRG neurons because the antibody we used did not cross-react with PAP in rat tissues. In our present study, we generated a chicken polyclonal antibody against the secretory isoform of mouse PAP. This antibody detects mouse, rat and human PAP protein on western blots. Additionally, this antibody detects PAP in mouse and rat small- to medium-diameter DRG neurons and axon terminals in lamina II of spinal cord. In the rat, 92.5% of all PAP+ cells bind the nonpeptidergic marker IB4 and 31.8% of all PAP+ cells contain the peptidergic marker CGRP. Although PAP is found in peptidergic and nonpeptidergic neurons of mice and rats, the percentage of PAP+ neurons that express these markers differs between species. Moreover, PAP+ axon terminals in the rat partially overlap with Protein kinase Cγ (PKCγ+) interneurons in dorsal spinal cord whereas PAP+ axon terminals in the mouse terminate dorsal to PKCγ+ interneurons. Collectively, our studies highlight similarities and differences in PAP localization within nociceptive neurons of mice and rats.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Prostatic Acid Phosphatase Is Expressed in Peptidergic and Nonpeptidergic Nociceptive Neurons of Mice and Rats

Taylor-Blake

Zylka

2010

PLoS ONE

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“…The catalytic activity of these enzymes target phosphoesters in acidic environments. 5 TRACP is a cationic ferric glycoprotein with a molecular mass of about 35 kDa and a monomeric peptide structure. 6 TRACP expression is found in cells of the mononuclear phagocyte system, most abundantly in bone-resorbing osteoclasts, alveolar macrophages and dendritic cells.…”

Section: Introductionmentioning

confidence: 99%

“… 6 TRACP expression is found in cells of the mononuclear phagocyte system, most abundantly in bone-resorbing osteoclasts, alveolar macrophages and dendritic cells. 5 …”

Section: Introductionmentioning

confidence: 99%

Optimization of the tartrate-resistant acid phosphatase detection by histochemical method

Galvão

Santos²,

Ribeiro³

et al. 2011

Eur J Histochem

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According to the new kidney disease improving global outcomes (KDIGO) guidelines, the term of renal osteodystrophy, should be used exclusively in reference to the invasive diagnosis of bone abnormalities. Due to the low sensitivity and specificity of biochemical serum markers of bone remodelling, the performance of bone biopsies is highly stimulated in dialysis patients and after kidney transplantation. The tartrate-resistant acid phosphatase (TRACP) is an iso-enzyme of the group of acid phosphatases, which is highly expressed by activated osteoclasts and macrophages. TRACP in osteoclasts is in intracytoplasmic vesicles that transport the products of bone matrix degradation. Being present in activated osteoclasts, the identification of this enzyme by histochemistry in undecalcified bone biopsies is an excellent method to quantify the resorption of bone. Since it is an enzymatic histochemical method for a thermolabile enzyme, the temperature at which it is performed is particularly relevant. This study aimed to determine the optimal temperature for identification of TRACP in activated osteoclasts in undecalcified bone biopsies embedded in methylmethacrylate. We selected 10 cases of undecalcified bone biopsies from hemodialysis patients with the diagnosis of secondary hyperparathyroidism. Sections of 5 µm were stained to identify TRACP at different incubation temperatures (37°, 45°, 60°, 70° and 80°C) for 30 minutes. Activated osteoclasts stained red and trabecular bone (mineralized bone) was contrasted with toluidine blue. This approach also increased the visibility of the trabecular bone resorption areas (Howship lacunae). Unlike what is suggested in the literature and in several international protocols, we found that the best results were obtained with temperatures between 60°C and 70°C. For technical reasons and according to the results of the present study, we recommended that, for an incubation time of 30 min, the reaction should be carried out at 60°C. As active osteoclasts are usually scarce in a bone section, the standardization of the histochemistry method is of great relevance, to optimize the identification of these cells and increase the accuracy of the histomosphometric results. Our results, allowing an increase in osteoclasts contrast, also support the use of semi-automatic histomorphometric measurements.

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“…In addition, there are no small molecules that selectively and potently inhibit PAP. While non-selective inhibitors like L-(+)-tartrate exist, these molecules inhibit other acid phosphatases [ 3 ]. The only other known PAP inhibitor, α-benzylaminobenzylphosphonic acid (BABPA), has a much lower IC 50 , in the nanomolar range [ 4 , 5 ].…”

Section: Introductionmentioning

confidence: 99%

A High Throughput Assay to Identify Small Molecule Modulators of Prostatic Acid Phosphatase

Larsen¹,

Zylka

Scott³

2009

Curr Chem Genomics

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Prostatic acid phosphatase (PAP) is expressed in nociceptive neurons and functions as an ectonucleotidase. Injection of the secretory isoform of PAP has potent antinociceptive effects in mouse models of chronic pain. These data suggested that a small molecule activator of PAP may have utility as a novel therapeutic for chronic pain, while inhibitors could be used to acutely inhibit PAP in vitro and in vivo. To identify small molecule modulators of PAP activity, we validated a high throughput, fluorescence-based biochemical assay and then used this assay to screen a compound library. We decreased the frequency of false positive activators by subtracting compound fluorescence from the final assay fluorescence. This approach significantly reduced the number of false positive activators found in the screen. While no activators were confirmed, seven novel inhibitors of PAP were identified. Our results suggest this high throughput assay could be used to identify small molecule modulators of PAP activity.

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Acid Phosphatases

Cited by 3 publications

References 133 publications

Prostatic Acid Phosphatase Is Expressed in Peptidergic and Nonpeptidergic Nociceptive Neurons of Mice and Rats

Prostatic Acid Phosphatase Is Expressed in Peptidergic and Nonpeptidergic Nociceptive Neurons of Mice and Rats

Optimization of the tartrate-resistant acid phosphatase detection by histochemical method

A High Throughput Assay to Identify Small Molecule Modulators of Prostatic Acid Phosphatase

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