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.

Isolation and characterization of a homogeneous acid phosphatase from catfish liver

Abstract: 1. 1. A homogeneous, tartrate-inhibitable acid phosphatase (AcPase) was obtained from the liver of channel catfish ( Ictalurus punctatus ) by the use of Affi Gel-10-coupled aminohexyltartramic acid affinity chromatography. 2. 2. The enzyme has a molecular weight of 82,500 and is a dimer consisting of two apparently equivalent subunits with subunit weights of 35,000 ± 3000. Amino acid composition data are presented and compared with those of mammalian acid phosphatases. 3. 3. Data suggest that the enzyme is a metalloacid phosphatase. 4. 4. Catfish liver AcPase exhibits two molecular forms with pI 5.66 and 5.37 which were separated by chromatofocusing. 5. 5. A spontaneous conversion of the less acidic form to a more acidic form was observed and this conversion was accompanied by a decreased sensitivity towards tartrate inhibition.

Serum creatine kinase isoenzyme BB in mammalian osteopetrosis.

Abstract: In mammalian osteopetrosis the different mutations exemplify reduced bone resorption leading to net accumulation of bone. Recently, high blood levels of creatine kinase-BB have been reported in some human forms, suggesting it as a marker of osteopetrosis. In the current study serum creatine kinase-BB was evaluated in relation to known osteoclastic pathophysiology in two human types of autosomal dominant osteopetrosis at baseline and after stimulation with triiodothyronine and in four different rodent mutations. Creatine kinase-BB was increased markedly in Type 2 autosomal dominant osteopetrosis and in the incisors absent rat, both characterized by large numbers of giant osteoclasts, and did not change significantly after stimulation. Although creatine kinase-BB was unchanged in Type 1 autosomal dominant osteopetrosis at baseline and after stimulation, the rodent counterparts characterized by small osteoclasts, microphthalmic and osteopetrotic mice and toothless rats, had significantly decreased levels. Similar differences were observed in both types of autosomal dominant osteopetrosis compared with controls concerning tartrate resistant acid phosphatase. Creatine kinase-BB in mammalian osteopetrosis is related to osteoclastic number and size, where it probably reflects the differentiation and maturation of inactive bone resorbing cells. The isoenzyme does not seem to be a valuable screening marker for osteopetrosis.

Cytochemistry of hairy cells.

Abstract: The peripheral blood of 24 patients with bone marrow biopsy-proven hairy cell leukemia was examined with histochemical methods. Periodic acid-Schiff, acid phosphatase, acid phosphatase with tartrate, alpha naphthyl butyrate esterase, alpha naphthyl acetate esterase, and alpha naphthyl acetate esterase with sodium fluoride inhibition were among the reactions utilized. Reactivity was graded on a scale of 0 to +++. All patients had circulating hairy cells, ranging from 2 to 88% of the leukocyte count. Sequential studies (2 – 7 times) were performed in 9 of the patients. A finely granular, ± to ++ reaction product with periodic acid-Schiff (PAS) was present in 22 patients; in 3, however, the PAS was negative at one time in sequential studies. Acid phosphatase activity was present in more than 50% of the hairy cells in 21 patients; in only one was the reaction present in less than 25% of the leukemia cells. The reaction consisted of formation of granules which were small to medium in size with diffuse and irregular cytoplasmic distribution. Tartrate resistant acid phosphatase activity was present in 1 – 100% of the hairy cells in 23 of the 24 patients. One patient with 35% circulating cells showed acid phosphatase reactivity in 58% of these, but tartrate-resistant acid phosphatase reactivity was totally absent; the intensity of these two reactions varied between patients and within the same patient. Alpha naphthyl butyrate esterase reactivity ranged from ± to + in 16 of the 20 patients examined. In 19 of 20 patients, the alpha naphthyl acetate esterase reaction was ± to ++ positive, consisting of diffusely scattered granules in at least a few and, in some cases, in as many as 95% of the cells. This activity was inhibited by sodium fluoride in 16 of 19 patients. These findings are compared to those in 17 patients with various lymphoproliferative and myeloproliferative disorders who were studied by the same methods. Our results indicate that the cytochemical properties of hairy cells differ from those of any established cell group.

Transcription From the Tartrate-resistant Acid Phosphatase Promoter Is Negatively Regulated by the Myc Oncoprotein

Abstract: TRAP, a characteristic marker of osteoclast differentiation, is an enzyme that plays an active role in the process of bone resorption. Despite the importance of TRAP in osteoclast biology, the components involved in the transcriptional regulation of this gene are largely unknown. This study investigated the regulation of TRAP transcription by the Myc oncoprotein in three different cell types. A series of nested TRAP promoter deletion constructs were cotransfected into P388D1 murine macrophages and C3H10T1/2 murine embryonic fibroblasts along with a backbone plasmid control or expression plasmids containing v-Myc, c-Myc, or an inactive v-Myc protein construct (delta84/NLS). Both v-Myc and c-Myc negatively regulated transcription from the TRAP promoter in P388D1 and C3H10T1/2 cells, 90% and 50%, respective to cell type and amount of endogenous Myc protein, and delta84/NLS had no effect. The functional Myc-responsive element(s) within the TRAP promoter was localized to a region between -436 and +1 bp, which contains two putative Myc-inhibitory binding sites coincident with an initiator element (Inr) at -116 bp and -18 bp. Conversely, in the HD-11EM chicken v-Myc transformed preosteoclast cell line, the full-length TRAP promoter transcription was increased when endogenous v-Myc levels were decreased in response to pretreatment of these cells with 1alpha,25-dihydroxyvitamin D3 [1alpha,25(OH)2D3]. This report provides the first evidence of the specific regulation of TRAP at the transcriptional level by Myc, a transcription factor that is normally expressed at relatively high levels in preosteoclasts and other myelomonocytic cells and suggests that Myc plays an active role in suppressing the transcription of a mature osteoclast selective gene.