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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 ArticleDOI
TL;DR: The changes in IL-6 production induced by the hormones could not be the sole determinant for the extent of TRAP+ MNC formation, however, the stimulatory effect of 1α,25(OH)2D3 on osteoclastogenesis nevert...
Abstract: In mouse bone marrow primary cultures, the formation of osteoclast-like, i.e. tartrate-resistant acid phosphatase (TRAP)- and calcitonin receptor-positive multinucleated cells (MNC), when induced by 1α,25-dihydroxyvitamin D3 (1α,25(OH)2D3), can be suppressed by 17β-estradiol (17β-E2), whereas 17α-E2 is without any effect. 17β-E2, above 10−11 m, significantly reduced 1α,25(OH)2D3-mediated TRAP+ MNC formation in cultured bone marrow cells from both female and male mice. The estrogen at 10−8 m suppressed the peak response to the vitamin D sterol by 50%. 17β-E2 significantly suppressed basal and 1α,25(OH)2D3-stimulated cellular production of interleukin (IL)-6. IL-6 alone, although bone marrow cells in hormone-free culture produced appreciable amounts of the cytokine, did not induce any TRAP+ MNC. Therefore, the changes in IL-6 production induced by the hormones could not be the sole determinant for the extent of TRAP+ MNC formation. However, the stimulatory effect of 1α,25(OH)2D3 on osteoclastogenesis nevert...

55 citations

Journal ArticleDOI
TL;DR: It is suggested that sTr-AcP could be a useful marker for bone loss and consequently, for the measure of bone resorption rate in postmenopausal women.
Abstract: Serum tartrate-resistant acid phosphatase (sTr-AcP) and bone mineral content (BMC) were measured in 29 women with postmenopausal osteoporosis and in 12 control women. Serum Tr-AcP was higher in osteoporotic patients than in controls and a negative linear correlation was found between sTr-AcP and BMC in osteoporotic women. These results suggest that sTr-AcP could be a useful marker for bone loss and consequently, for the measure of bone resorption rate in postmenopausal women.

55 citations

Journal ArticleDOI
01 May 1998-Bone
TL;DR: The expression of IL-6R and gp130 in bone marrow cells during osteoclast differentiation and TRAP-positive multinucleated cells during tartrate-resistant acid phosphatase (TRAP) formation are investigated to suggest that gp130 and IL- 6R, as well asIL-6, are involved in the formation and activation of osteoclasts.

55 citations

Journal Article
01 Mar 1994-Leukemia
TL;DR: The high degree of sequence homology indicated that TRAP and PAP enzymes represent a single entity belonging to the class of metalloproteins.
Abstract: Acid phosphatase (AcP, EC 3.1.3.2) is represented by a number of enzymes that can be differentiated according to structural and immunological properties, tissue distribution, subcellular location and other features; these AcP isoenzymes share similar catalytic activity toward phosphoesters in an acidic medium. Classically, AcPs have been divided into four types according to their sensitivity to tartrate and to their origin: erythrocytic, lysosomal, prostatic AcP, and an AcP enzyme that was first identified in hairy cell leukemia (HCL). This latter AcP was termed isoenzyme 5 (based on its electrophoretic mobility) or human type 5, tartrate-resistant acid phosphatase (TRAP). Differences in various physicochemical properties, lack of amino acid sequence similarity and different chromosomal locations of the respective genes showed that the four AcP isoenzymes are not related. The biochemical properties of TRAP are unique: resistance to inhibition by tartrate, but inhibition by molybdate; glycoprotein of 30-40 kDa occurring as two similar isoforms with different carbohydrate content, each composed of dissimilar subunits of 16 and 23 kDa in disulfide linkage; active at acid pH (optimum at 5-6) with basic pI (8.5-9.0); presence of an iron active site giving the purified protein a purple color. The TRAPs of different human sources (HCL spleen, osteoclastoma, Gaucher's spleen, placenta) have an 85-94% homology in their amino acid sequences. Full-length TRAP cDNAs (1.4 kb) have been cloned from human placenta and Gaucher's spleen. Variations in TRAP structure appear to result from post-translational modifications and not from the existence of a multigene family as only a single TRAP gene and a single mRNA species have been reported. This notion of a single TRAP gene is supported by the substantial sequence homology found among the various TRAPs from human tissues and from animal sources (e.g. bovine spleen and bone; rat spleen, bone and epidermis; pig uterus). The latter enzyme preparations of animal origin have been described for many years as the purple acid phosphatase (PAP). However, the high degree of sequence homology indicated that TRAP and PAP enzymes represent a single entity belonging to the class of metalloproteins. The human TRAP gene was assigned to chromosome 15 and to chromosome 19 by two groups. TRAP protein is localized in lysosomes or similar organelles and is not secreted. The serum level of TRAP was found to be increased during physiological bone growth, in Gaucher's disease, and in malignancies metastasized to bone (resulting from increased osteoclastic activity).(ABSTRACT TRUNCATED AT 400 WORDS)

55 citations

Journal ArticleDOI
TL;DR: Since osteoclasts cannot function properly without multinucleation, selective CRAC inhibitors may have utility in management of hyperresorptive states.
Abstract: Osteoclasts are specialized macrophage derivatives that secrete acid and proteinases to mobilize bone for mineral homeostasis, growth, and replacement or repair Osteoclast differentiation generally requires the monocyte growth factor m-CSF and the TNF-family cytokine RANKL, although differentiation is regulated by many other cytokines and by intracellular signals, including Ca(2+) Studies of osteoclast differentiation in vitro were performed using human monocytic precursors stimulated with m-CSF and RANKL, revealing significant loss in both the expression and function of the required components of store-operated Ca(2+) entry over the course of osteoclast differentiation However, inhibition of CRAC using either the pharmacological agent 3,4-dichloropropioanilide (DCPA) or by knockdown of Orai1 severely inhibited formation of multinucleated osteoclasts In contrast, no effect of CRAC channel inhibition was observed on expression of the osteoclast protein tartrate resistant acid phosphatase (TRAP) Our findings suggest that despite the fact that they are down-regulated during osteoclast differentiation, CRAC channels are required for cell fusion, a late event in osteoclast differentiation Since osteoclasts cannot function properly without multinucleation, selective CRAC inhibitors may have utility in management of hyperresorptive states

55 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20239
202238
202126
202025
201913
201821