Acid phosphatase activity and intracellular collagen degradation by fibroblasts in vitro

1986 ◽  
Vol 245 (2) ◽  
Author(s):  
Toshihiko Yajima
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Collagen Degradation ◽  
Intracellular Collagen

scholarly journals Chick osteoblasts contain fluoride-sensitive acid phosphatase activity.

1988 ◽  
Vol 36 (9) ◽  
pp. 1175-1180 ◽  
Author(s):  
M W Lundy ◽  
K H Lau ◽  
H C Blair ◽  
D J Baylink
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Bone Matrix ◽  
Competitive Inhibitor ◽  
Cellular Origin ◽  
Embryonic Chicken ◽  
Low Concentrations

We used histological and biochemical methods to determine the cellular origin of bone matrix fluoride-sensitive acid phosphatase in chicken bone. Embryonic chicken calvariae were embedded in plastic and sections stained for acid phosphatase at various concentrations of substrate and fluoride. Acid phosphatase activity was observed in osteoblasts and osteoclasts but not in fibroblasts. Striking inhibition of osteoblastic acid phosphatase occurred at 100 microM fluoride, a concentration that had no apparent effect on osteoclastic acid phosphatase. Inhibition of osteoblastic and osteoclastic acid phosphatase by fluoride was also examined using extracts of embryonic chicken calvarial cells, mouse osteoblasts (MC3T3-El cell line), and purified chick osteoclasts, respectively. Fluoride is a partial competitive inhibitor of both chicken and mouse osteoblastic acid phosphatases, with apparent inhibition constants of 10-100 microM. These concentrations of fluoride correspond to those that increase bone formation in vitro and in vivo. In contrast, the apparent inhibition constant for fluoride of osteoclastic acid phosphatase was much higher (i.e., 0.5 mM). In summary, this study demonstrates that chicken osteoblasts contain an acid phosphatase that is sensitive to inhibition by low concentrations (i.e., microM) of fluoride.

IODINATED PARTICLES IN THE RAT THYROID

1975 ◽  
Vol 79 (3) ◽  
pp. 459-473 ◽  
Author(s):  
J. Dang ◽  
R. Miquelis ◽  
P. Bastiani ◽  
C. Simon
Keyword(s):  
Acid Phosphatase ◽  
Thyroid Gland ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
High Turnover ◽  
Secondary Lysosomes ◽  
Rat Thyroid ◽  
Tsh Stimulation

ABSTRACT In a previous study (Simon et al. 1971) a procedure for the preparation and separation of iodinated particles was described in the rat. The present paper deals with further investigations on the nature of these particles. Acid phosphatase and iodine are conjointly sedimentable and display a latency that is unmasked on dilution in a hypo-osmotic medium and under acidification to pH 5.0. These properties together with the sensitivity to Triton X-100 are best accounted for by assuming that iodinated particles of the thyroid gland are lysosomes. Part of the particulate iodine is soluble in n-butanol (BEI fraction). The existence of this BEI fraction demonstrates that hydrolysis of thyroglobulin occurs within the particles which thus exhibit an acid protease activity. Both the sedimentable iodine pool and acid phosphatase are increased under TSH stimulation and decreased after thyroxine treatment. In addition, the general activity of the iodinated particles is dependent on the daily iodine intake as shown by the variation of their iodine pool, acid phosphatase activity and BEI fraction with the iodine diet. It is concluded that iodinated particles of the thyroid gland are secondary lysosomes which participate in iodine secretion under TSH control. By in vitro treatment with destabilizing media or after in vivo treatment with thyroxine, iodinated particles exhibit a parallel loss of iodine and acid phosphatase. After a short-term TSH treatment in vivo, their iodine pool is more increased than their acid phosphatase activity. It is concluded that, at least in the normal rat thyroid, iodinated particles are essentially secondary lysosomes; true colloid droplets actually accumulate only after sufficient TSH stimulation. After ultracentrifugation, 3 main subpopulations are separated for which iodine and acid phosphatase patterns are superimposed. In addition, they all exhibit properties characteristic of secondary lysosomes. Finally, the presence of a fourth sedimentable iodinated fraction with a high turnover rate is postulated.

Cytochemical distribution of acid phosphatase activity in gliomas cultured in vitro

1968 ◽  
Vol 11 (2) ◽  
pp. 113-121 ◽  
Author(s):  
A. Głuszcz ◽  
A. Drab ◽  
K. Sejmicka ◽  
J. Alwasiak
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity

Effects of Hebeloma arenosa and phosphorus fertility on root acid phosphatase activity of red pine (Pinus resinosa) seedlings

1991 ◽  
Vol 69 (2) ◽  
pp. 380-383 ◽  
Author(s):  
Janet MacFall ◽  
Steven A. Slack ◽  
Jaya Iyer
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Fungal Growth ◽  
Pinus Resinosa ◽  
Ectomycorrhizal Fungus ◽  
Red Pine ◽  
Nitrophenyl Phosphate

The ectomycorrhizal fungus Hebeloma arenosa Burdsall, MacFall & Albers was assayed for surface-accessible acid phosphatase activity in vitro on roots of red pine (Pinus resinosa Ait.) seedlings. Hebeloma arenosa was grown in defined liquid media containing 0, 17, 34, 68, or 136 mg/L phosphorus for 4 weeks. When assayed for acid phosphatase activity with p-nitrophenyl phosphate, 7.3 μmol of orthophosphate were released per gram dry weight of fungal tissue. There was no effect of added P on enzyme activity, excluding the treatment with no added P in which there was negligible fungal growth. Red pine seedlings were grown in Sparta loamy fine sand amended with 0, 17, 34, 68, or 136 mg/kg P as superphosphate, with and without H. arenosa inoculum. Mycorrhizal roots had greater enzyme activity than nonmycorrhizal roots of seedlings grown in similarly P-amended soil. This was determined by the following three assays: orthophosphate release from two salts of myoinosital hexaphosphate (Na and KMg) and from p-nitrophenyl phosphate. It is suggested that greater acid phosphatase activity by roots mycorrhizal with H. arenosa is one mechanism for improved P nutrition through the formation of a pool of P released from sources unavailable for direct intake.

Acid phosphatase activity of six ectomycorrhizal fungi

1979 ◽  
Vol 57 (11) ◽  
pp. 1203-1205 ◽  
Author(s):  
Iwan Ho ◽  
Bratislav Zak
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Test Methods ◽  
Starch Gel Electrophoresis ◽  
Tree Roots ◽  
Nitrophenyl Phosphate ◽  
Starch Gel

Six ectomycorrhizal fungi commonly associated with Douglas-fir were tested in vitro for acid phosphatase activity by measuring the amount of p-nitrophenyl phosphate converted to p-nitrophenol and by examining their production of isoenzymes detectable by starch gel electrophoresis. Both test methods showed acid phosphatase activity to be highest in Hebeloma crustuliniforme, followed by progressively lower activity in Laccaria laccata, Amanita muscaria, and Thelephora terrestris. Rhizopogon vinicolor and Piloderma bicolor showed low activity. We discuss the significance of these fungi in the utilization of complex phosphates by tree roots.

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