scholarly journals Exploring the role of a glycine cluster in cold adaptation of an alkaline phosphatase

2002 ◽  
Vol 269 (9) ◽  
pp. 2330-2335 ◽  
Author(s):  
Konstantinos Mavromatis ◽  
Iason Tsigos ◽  
Maria Tzanodaskalaki ◽  
Michael Kokkinidis ◽  
Vassilis Bouriotis
Keyword(s):  
Alkaline Phosphatase ◽  
Cold Adaptation

First repeated bone scan in the observation of patients with operable breast cancer.

1986 ◽  
Vol 4 (3) ◽  
pp. 389-394 ◽  
Author(s):  
A Pedrazzini ◽  
R Gelber ◽  
M Isley ◽  
M Castiglione ◽  
A Goldhirsch
Keyword(s):  
Breast Cancer ◽  
Alkaline Phosphatase ◽  
Bone Scan ◽  
Serum Alkaline Phosphatase ◽  
Clinical Situation ◽  
Operable Breast Cancer ◽  
First Relapse ◽  
Bone Scans ◽  
First Recurrence

Data on 1,601 patients with node-positive operable breast cancer who were randomized in four different prospective adjuvant therapy trials were analyzed to evaluate the role of routine bone scans and the alkaline phosphatase value at regular intervals in screening for bone involvement. Bone scan was a prerequisite for randomization and was repeated within the first 12 months in 90% (1,441) of the patients. Abnormal or doubtful scan findings had to be verified by x-ray examination. The repeated scan results were normal in 1,263 (87.8%) patients, doubtful but with no radiologic evidence of bone metastasis in 161 (11%), and abnormal (radiologically confirmed) in 17 (1.2%). After a median observation of 4 years bone metastases as the first relapse developed in 136 (8.5%) patients. This occurred in 87 of 1,263 (6.9%) of the patients with normal repeated scan results and in 18 of 161 (11.2%) of those with doubtful repeated scan findings. Based on the results of the first repeated scan, early detection of a first recurrence in bone might have been possible for 2.4% of the population. Serum alkaline phosphatase levels were also without clinical use. Bone scan in the observation of patients with operable breast cancer should be performed only as dictated by the clinical situation.

scholarly journals Pathophysiological Role of Vascular Smooth Muscle Alkaline Phosphatase in Medial Artery Calcification

2015 ◽  
Vol 30 (5) ◽  
pp. 824-836 ◽  
Author(s):  
Campbell R Sheen ◽  
Pia Kuss ◽  
Sonoko Narisawa ◽  
Manisha C Yadav ◽  
Jessica Nigro ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Pathophysiological Role ◽  
Medial Artery Calcification ◽  
Medial Artery

Role of alkaline phosphatase in colitis in man and rats

Gut ◽  
2008 ◽  
Vol 58 (3) ◽  
pp. 379-387 ◽  
Author(s):  
A Tuin ◽  
K Poelstra ◽  
A de Jager-Krikken ◽  
L Bok ◽  
W Raaben ◽  
...  
Keyword(s):  
Alkaline Phosphatase

Acidosis inhibits osteoblastic and stimulates osteoclastic activity in vitro

1992 ◽  
Vol 262 (3) ◽  
pp. F442-F448 ◽  
Author(s):  
N. S. Krieger ◽  
N. E. Sessler ◽  
D. A. Bushinsky
Keyword(s):  
Alkaline Phosphatase ◽  
Metabolic Acidosis ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Collagen Synthesis ◽  
Calcium Flux ◽  
Osteoclastic Activity ◽  
Glucuronidase Activity

Metabolic acidosis induces net calcium flux (JCa) from cultured neonatal mouse calvariae through physicochemical and cell-mediated mechanisms. To determine the role of osteoblasts in acid-induced JCa, collagen synthesis and alkaline phosphatase activity were assessed in calvariae incubated in reduced pH and bicarbonate medium, a model of metabolic acidosis (Met), and compared with controls (Ctl). Collagen synthesis fell from 30.5 +/- 1.1 in Ctl to 25.1 +/- 0.4% with Met, and alkaline phosphatase decreased from 403 +/- 25 in Ctl to 298 +/- 21 nmol Pi.min-1.mg protein-1 with Met. During acidosis JCa was correlated inversely with percent collagen synthesis (r = -0.743, n = 11, P = 0.009) and with alkaline phosphatase activity (r = -0.453, n = 22, P = 0.034). To determine the role of osteoclasts in acid-induced JCa, osteoclastic beta-glucuronidase activity was determined in Ctl and Met in the absence or presence of the osteoclastic inhibitor calcitonin (CT, 3 x 10(-9) M). Met increased beta-glucuronidase (5.9 +/- 0.2) compared with Ctl (4.6 +/- 0.3 micrograms phenolphthalein released.bone-1.h-1), whereas CT inhibited beta-glucuronidase in both Ctl and Met (3.1 +/- 0.2 and 3.5 +/- 0.3, respectively). During acidosis JCa was correlated directly with beta-glucuronidase activity (r = 0.683, n = 42, P less than 0.001). Thus the cell-mediated component of JCa during acidosis in vitro appears to result from a combination of inhibited osteoblastic and stimulated osteoclastic activity.

scholarly journals THE ROLE OF ALKALINE PHOSPHATASE IN OSTEOGENESIS

1951 ◽  
Vol 93 (5) ◽  
pp. 415-426 ◽  
Author(s):  
Robert S. Siffert
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Bone Matrix ◽  
Living Cells ◽  
Alkaline Solutions ◽  
Human Beings ◽  
Acid Media ◽  
Weakly Acid

The role of alkaline phosphatase in osteogenesis has been investigated by histochemical techniques with particular attention to its relationship to phosphate metabolism and matrix elaboration. The upper tibial epiphysis mainly, and other epiphyses as well of growing rabbits, and the costochondral junctions of newborn human beings were studied, as were bone grafts in growing rabbits. The findings in the newborn human beings were identical with those in the rabbits. Phosphatase activity and free phosphate localization do not universally coincide. The enzyme appears to be intimately related to preosseous cellular metabolism and to the elaboration of a bone matrix that is chemically calcifiable. It remains possible, however, that phosphatase may be in some way involved in making inorganic salts available to the calcifiable matrix. If this function does exist it is a secondary one, since the elaboration of bone matrix, which is always associated with phosphatase activity, can and does occur in the absence of calcification. Calcification may occur later, in the absence of the enzyme. There is evidence to suggest that cartilage matrix is utilized in the formation of bone matrix. Phosphatase is physiologically active only in the presence of living cells. Where it is demonstrable in the absence of living cells, as in the cartilage remnants of the metaphysis, it appears to be physiologically inactive. Since phosphatase is temporarily inactivated in weakly acid media, and readily reactivated by alkaline solutions it is possible that the enzyme might survive in a physiologically inactive state in weakly acid tissues, and yet remain capable of histochemical demonstration in vitro in an alkaline medium. Phosphatase is not related to the disappearance of chondroitin sulfate.

An Evaluation of the Greiner Selective Analyzer and its Role in the Clinical Laboratory

1975 ◽  
Vol 12 (1-6) ◽  
pp. 182-191 ◽  
Author(s):  
Andrew G. Skinner ◽  
Peter Wilding
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Creatinine ◽  
Total Protein ◽  
Total Bilirubin ◽  
Clinical Laboratory ◽  
Comparison Of Results ◽  
Operation Temperature ◽  
Accuracy And Precision ◽  
Analytical Range

The Greiner Selective Analyzer (GSA II) was evaluated over a period of six months. The evaluation assessed the reliability, accuracy, and precision of the analyser for six determinations. The methods evaluated were for glucose, urea, creatinine, total protein, total bilirubin, and alkaline phosphatase. Comparison of results was also made with those obtained for the same specimens using the Technicon SMA 12/60 Analyzer. Correlation and comparison of results indicate that the Greiner Selective Analyzer performed better for three of the methods but worse for serum creatinine determination. The role of the analyser as a routine tool in the clinical laboratory was also evaluated during analyses of approximately 900 patient specimens. Other features evaluated were analytical range of the six methods under study, the economics of operation, temperature control, and electrical and mechanical safety.

Role of β-GP-derived pi in mineralization via ecto-alkaline phosphatase in cultured fetal calvaria cells

1996 ◽  
Vol 62 (2) ◽  
pp. 262-274 ◽  
Author(s):  
Fani Anagnostou ◽  
Christiane Plas ◽  
Jean-Raphaël Nefussi ◽  
Nadine Forest
Keyword(s):  
Alkaline Phosphatase

RICKETS, DEFICIENCY OF "ALKALINE" PHOSPHATASE ACTIVITY AND PREMATURE LOSS OF TEETH IN CHILDHOOD

PEDIATRICS ◽  
1953 ◽  
Vol 11 (4) ◽  
pp. 309-322
Author(s):  
EDNA H. SOBEL ◽  
LELAND C. CLARK ◽  
R. PHYLLIS FOX ◽  
MEINHARD ROBINOW
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Enzyme Treatment ◽  
Deciduous Teeth ◽  
Local Factor ◽  
Plasma Alkaline Phosphatase ◽  
Serum Inorganic Phosphate ◽  
Genetically Determined

A child, studied between the ages of 1½ and 3½ years, presented an abnormally low plasma alkaline phosphatase activity (0.8-1.64 Bessey-Lowry u.), a deformed skeleton and the loss of most of her deciduous teeth. The serum Ca was normal; the serum inorganic phosphate remained at the normal relatively high levels of infancy as the child grew older Roentgenograms demonstrated deficient mineralization of the skeleton and teeth. Biopsies of the liver and the costochondral junction displayed a deficiency of tissue alkaline phosphatase activity. The architecture of the rib was consistent with rickets. There was no evidence for the presence of an inhibitor of alkaline phosphatase, such as beryllium, or for an excessive excretion of the enzyme. Treatment with purified growth hormone, ascorbic acid and thiamin chloride had no effect, while vitamin D 500 thousand u. caused little change in the enzyme activity in a 10 day period. The father had low plasma alkaline phosphatase activity and a number of similar patients are mentioned, for whom there was also evidence that the deficiency in alkaline phosphatase activity may be genetically determined. While the precise role of alkaline phosphatase activity in the metabolism of bone is not clear, the findings in this patient suggest that growing bone may require the presence of alkaline phosphatase for normal calcification, and that the skeletal disorder, which could not be distinguished from rickets, may be related to a disturbance in the local factor.

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