Isolation and phenotypic characterization of a multinucleated tartrate-resistant acid phosphatase–positive bone marrow macrophage

2011 ◽  
Vol 39 (3) ◽  
pp. 339-350.e3 ◽  
Author(s):  
Erik Karlström ◽  
Barbro Ek-Rylander ◽  
Mikael Wendel ◽  
Göran Andersson
2009 ◽  
Vol 1176 (1) ◽  
pp. 124-134 ◽  
Author(s):  
Hans-Jörg Bühring ◽  
Sabrina Treml ◽  
Flavianna Cerabona ◽  
Peter De Zwart ◽  
Lothar Kanz ◽  
...  

1977 ◽  
Vol 23 (1) ◽  
pp. 89-94 ◽  
Author(s):  
K W Lam ◽  
L T Yam

Abstract A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.


2009 ◽  
Vol 10 (4) ◽  
pp. 601-606 ◽  
Author(s):  
S.V. Reddy ◽  
J.E. Hundley ◽  
J.J. Windle ◽  
O. Alcantara ◽  
R. Linn ◽  
...  

Hybridoma ◽  
2006 ◽  
Vol 25 (6) ◽  
pp. 358-366 ◽  
Author(s):  
Tatsuya Ohashi ◽  
Toshihide Miura ◽  
Yoshihiko Igarashi ◽  
Iwao Kiyokawa ◽  
Yasuhito Sato ◽  
...  

1995 ◽  
Vol 41 (10) ◽  
pp. 1495-1499 ◽  
Author(s):  
P Chamberlain ◽  
J Compston ◽  
T M Cox ◽  
A R Hayman ◽  
R C Imrie ◽  
...  

Abstract We have characterized four monoclonal antibodies (mAbs) to the purple ("tartrate-resistant," band 5) acid phosphatase of the human osteoclast (TRAP) and used these to develop a specific serum immunoassay. All four mAbs are of high affinity (Ka = 1-5 x 10(8) L/mol) with a very fast Kassoc (0.2-2.0 x 10(5) L mol-1 s-1) and a moderate Kdissoc (1-3 x 10(-3) s). Two of the mAbs were selected to develop a time-resolved fluorescence immunoassay to measure serum concentrations of TRAP. The mean serum immunoreactive TRAP in a group of healthy premenopausal women and men was 3.7 +/- 1.8 micrograms/L (mean +/- SD) and 3.5 +/- 1.6 micrograms/L, respectively. Significantly higher concentrations of TRAP were found in postmenopausal women (6.3 +/- 2.3 micrograms/L) and in eight patients with Gaucher disease (19.3 +/- 4.7 micrograms/L). Further studies are required to investigate the value of serum TRAP as a marker of bone resorption.


1986 ◽  
Vol 34 (10) ◽  
pp. 1317-1323 ◽  
Author(s):  
F P van de Wijngaert ◽  
E H Burger

Fixed, undecalcified mouse long bones were embedded in glycol methacrylate (GMA), sectioned, and incubated for acid phosphatase in the presence or absence of tartrate, to investigate the feasibility of tartrate-resistant acid phosphatase as a histochemical marker for osteoclast identification. Naphthol AS-BI phosphate was used as the substrate and hexazonium pararosanaline as coupler. Cytocentrifuge preparations of mouse, rat, and quail bone marrow or frozen and GMA sections of mouse splenic tissue were used as controls to specify acid phosphatase activity. After adequate fixation, acid phosphatase activity sensitive to tartrate inhibition (TS-AP) was demonstrated in macrophages from spleen, bone marrow, and loose connective tissue surrounding bone rudiments. Acid phosphatase activity resistant to tartrate inhibition (TR-AP), was detected in multi-nuclear osteoclasts and in some mononuclear cells from bone marrow and periosteum. In cytocentrifuge preparations and frozen sections of mouse spleen, TR-AP was demonstrated after simultaneous incubation with substrate and tartrate. In GMA sections, however, TR-AP could only be demonstrated after pre-incubation with tartrate before application of substrate. We suggest that histochemical demonstration of TR-AP versus TS-AP on GMA-embedded bone sections by means of a pre-incubation method can be used as an identification marker of (pre)osteoclasts. Plastic embedding is recommended for its excellent preservation of morphology and enzyme activity.


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