Topic
Tartrate-resistant acid phosphatase
About: Tartrate-resistant acid phosphatase is a research topic. Over the lifetime, 1115 publications have been published within this topic receiving 45937 citations. The topic is also known as: HPAP & SPENCDI.
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Journal Article•
TL;DR: Tartrate resistant acid phosphatase is a useful marker of metastatic bone disease and response to treatment in breast cancer patients and was significantly higher in patients with progressive disease.
Abstract: BACKGROUND Tartrate resistant acid phosphatase (TRACP) is exclusively localized in osteoclasts and has been suggested to be a unique marker of bone metastasis. PATIENTS AND METHODS TRACP activity using an improved spectrophotometric assay was measured in 56 healthy volunteers and 113 breast cancer patients, including 35 with bone metastases (BM). RESULTS TRACP activities (IU/l, mean +/- SD) of normal subjects in pre- and post-menopausal women were 5.7 +/- 1.3 and 6.6 +/- 1.2, respectively (p < 0.02). The specificity, sensitivity, and accuracy of TRACP in patients, were 91.0%, 65.7%, and 83.2%, respectively. TRACP was significantly higher in patients with BM than in patients without BM (p < 0.01). In patients with BM, TRACP increased in proportion to the number of BM. Regarding clinical assessment of treatment of BM, TRACP was significantly higher in patients with progressive disease. CONCLUSION TRACP is a useful marker of metastatic bone disease and response to treatment in breast cancer patients.
21 citations
15 Dec 2011
TL;DR: The active-site structure of the homodimeric 111-kDa kbPAP is consistent with proposals on the mechanism of phosphate ester hydrolysis by nucleophilic attack on the phosphate by an Fe(III)-coordinated hydroxide ion.
Abstract: Purple acid phosphatases (PAPs) hydrolyzing activated phosphoric acid esters and anhydrides have in common a two-metal center with a tyrosine-Fe(III) charge transfer transition responsible for the color. In the mammalian enzymes from the spleen, macrophages, osteoclasts, and uterine fluids, the second metal in the active site is Fe(II); whereas, the plant enzyme kidney bean PAP (kbPAP) has an Fe(III)–Zn(II) active center. The structure of the homodimeric 111-kDa kbPAP shows the active site at the carboxy end of two sandwiched β–α–β–α–β motifs. The two metal ions are bridged monodentately by Asp164. The iron is further coordinated by Tyr167, His325, and Asp135, and the zinc by His286, His323, and Asn201. The active-site structure is consistent with proposals on the mechanism of phosphate ester hydrolysis by nucleophilic attack on the phosphate by an Fe(III)-coordinated hydroxide ion. Protein isolation, biological functions, sequences, activity, comparison of mammalian and plant PAPs, and the functional aspects of both types are discussed extensively.
3D Structure
Keywords:
purple acid phosphatase;
tartrate-resistant acid phosphatase;
uteroferrin;
iron protein;
zinc protein;
X-ray structure
21 citations
TL;DR: An acid phosphatase, which was immunochemically identical to splenic purple acid phosphate, was purified to homogeneity from rat bone and hydrolyzed aryl phosphates, nucleoside di- and triphosphates, thiamine pyrophosphate, phosphoenolpyruvic acid and acidic phosphoproteins.
Abstract: 1. 1. An acid phosphatase, which was immunochemically identical to splenic purple acid phosphatase, was purified to homogeneity from rat bone. 2. 2. The enzyme was a two iron-containing monomeric glycoprotein with a mol. wt of 36,000. 3. 3. The enzyme hydrolyzed aryl phosphates, nucleoside di- and triphosphates, thiamine pyrophosphate, phosphoenolpyruvic acid and acidic phosphoproteins. 4. 4. The enzyme was inhibited by ammonium molybdate, NaF and CuSO4 but not by tartrate and SH-reagents.
21 citations
TL;DR: Results suggest that TRAP-marks are vestiges of proteins secreted by polarized osteoclasts, and treatment of osteoclast cultures with alendronate suppressed the formation of TR AP-marks and resorption pits without affecting the cell viability.
21 citations
Journal Article•
TL;DR: The data demonstrate that chronic lymphocytic leukemia and prolymphocyticukemia cells can be induced to realize a common genetic program which bears characteristics of HCL, indicating that these three entities are much more closely related than previously thought.
Abstract: In vitro maturation was induced with 12- O -tetradecanoylphorbol-13-acetate in leukemic cell samples from patients with chronic lymphocytic leukemia ( n = 10) and prolymphocytic leukemia ( n = 4). The cells were studied for morphology, for immunological markers using the fluorescence activated cell sorter, and for acid phosphatase isoenzymes using both cytochemistry and isoelectrofocusing.
Morphologically the induced changes included appearance of cells with an excentric nucleus and basophilic cytoplasm and eventually of cells with many fine cytoplasmic projections (“hairs”). Analysis of immunological markers by flow cytometry revealed that the monoclonal antibody defined cell surface molecule HD6 (CD22), which is strongly expressed on hairy cell leukemia (HCL) but absent from plasmacytoma and plasma cells, can be induced or enhanced in the leukemic samples. In the study of acid phosphatase isoenzymes using cytochemistry we observed the induction of the tartrate resistant isoenzyme. Further, using isoelectrofocusing we could demonstrate the induction of the same band of tartrate resistant acid phosphatase with an isoelectric point of 9.0–9.7 as detected also in HCL. This particular isoenzyme is considered characteristic of HCL but is absent in plasmacytoma. Our data demonstrate that chronic lymphocytic leukemia and prolymphocytic leukemia cells can be induced to realize a common genetic program which bears characteristics of HCL, indicating that these three entities are much more closely related than previously thought.
21 citations