scholarly journals Mouse ovarian alkaline phosphatase activities that respond to gonadotropins: histochemical and biochemical studies.

1976 ◽  
Vol 24 (10) ◽  
pp. 1101-1109 ◽  
Author(s):  
T A Bramley ◽  
J Kent

Alkaline phosphatase activity was measured in whole ovarian homogenates from pre-pubertal mice of different ages, with and without prior injection of human chorionic gonadotropin. Alkaline phosphatase activity was also scored in the different cell types in sections of similar ovaries, using two distinct histochemical procedures. The results from those methods differed. Biochemical studies indicated the presence of three distinct alakaline phosphatase activities: I and Ib, both optimal at pH 10.4 and with similar substrate requirements and inhibitor sensitivities (phosphatase I being characteristic of unstimulated ovaries and Ib of ovaries stimulated with human luteinizing hormone or human chorionic gonadotropin), and phosphatase II, optimal at pH 9.4, with different substrate requirements and inhibitor sensitivities. The differences observed using the histochemical procedures can probably be accounted for by the effects of different incubation conditions on the activities of these three enzymes.

2007 ◽  
Vol 342-343 ◽  
pp. 85-88 ◽  
Author(s):  
Hyun Sook Baek ◽  
Young Hwan Park ◽  
Ki Chang Seok ◽  
Jong Chul Park ◽  
Don Kyun Rah

Attachment and viability of different cell types(fibrioblast, chondrocyte and osteoblast ) was observed on two forms of silk (mat & Three-dimensional scaffolds). The osteoblasts behaviors cultured on silk mat were significantly higher than that found on 3-D silk fibroin scaffold (3-D SF scaffold). In the MTT assay, the cell viability of fibroblasts, chondrocyte and osteoblasts seeded on 2-D nanofiber mat was (2-D mat) significantly higher than that found on 3-D SF scaffold. Similar result could be seen from SEM observation and cell attachment study. However, alkaline phosphatase activity was significantly increased on 3-D SF scaffold than on2-D nanofiber


Author(s):  
H. J. W. Cleeve

Summary Samples from 260 non-jaundiced patients with elevated plasma alkaline phosphatase activities were analysed for γ-glutamyltransferase and 5′-nucleotidase activity, and for alkaline phosphatase isoenzyme pattern. The plasma γ-glutamyltransferase activity was found to be a more sensitive index than that of plasma 5′-nucleotidase in confirming the presence of a liver component of the elevated plasma alkaline phosphatase. If the γ-glutamyltransferase level is normal it is probable that the increase in plasma alkaline phosphatase activity is of bone origin. However, an elevated γ-glutamyltransferase result does not exclude a bone component; in this situation plasma alkaline phosphatase isoenzymes should be estimated. The causes of elevated activities of plasma alkaline phosphatase, 5′-nucleotidase and γ-glutamyltransferase, found in this investigation were generally the same as those found by other workers. The effect of treatment by drugs on γ-glutamyltransferase, an inducible enzyme, needs more investigation.


Blood ◽  
1955 ◽  
Vol 10 (11) ◽  
pp. 1120-1131 ◽  
Author(s):  
E. WILTSHAW ◽  
W. C. MOLONEY

Abstract (1) In a large series of individuals alkaline phosphatase activity in the leukocyte was studied by biochemical and histochemical methods. (2) The value of combined histochemical and biochemical measurements is demonstrated in this report. (3) In chronic myelogenous leukemia the neutrophil contain very little alkaline phosphatase activity while in myeloid metaplasia and pyogenic infections morphologically similar cells exhibit a great increase in this enzyme. (4) Various factors which might influence alkaline phosphatase activity in See PDF for Figure See PDF for Table leukocytes were investigated and it was found that on incubation in serum or saline the cell alkaline phosphatase activity increased. However, this in vitro rise was unrelated to the source of the serum menstrum.


2019 ◽  
Author(s):  
Takenori Kanai ◽  
Yoshihiko Sawa ◽  
Kenyo Takara ◽  
Koichiro Kajiwara ◽  
Takahiro Fujita ◽  
...  

AbstractPodoplanin is the only counter-receptor of platelet CLEC-2 and is expressing on mature osteoblast, but there is no report on the role of podoplanin and CLEC-2 in calcification. This study aimed to investigate the role of podoplanin binding to CLEC-2 in the calcification of osteoblasts carrying homozygously deleted Pdpn alleles (PdpnΔ/Δ) by heterozygously expressing collagen type I alpha 1 promoter (Col1a)-driven Cre recombinase. There were no macroscopic abnormalities in the bone and dentin of Col1a11-Cre;PdpnΔ/Δ mice but the coccygeal bone medullary cavity was very narrow. In the quantitative analysis for alizarin red-stained products and alkaline phosphatase activities on the cultured calvarial osteoblasts, the amounts of calcified products and alkaline phosphatase activity of calvarial osteoblasts of both Pdpnfl/fl and Col1a11-Cre;PdpnΔ/Δ mice were significantly higher in the calcification medium than in the α-mem. Both the amounts of calcified products and alkaline phosphatase activity of calvarial osteoblasts from Pdpnfl/fl mice were significantly lower in the calcification medium with CLEC-2 than without CLEC-2 while there were no significant differences in the amounts of calcified products and alkaline phosphatase activities of calvarial osteoblasts from Col1a11-Cre;PdpnΔ/Δ mice with CLEC-2. Platelet CLEC-2 may play a role in regulating the calcification via binding to podoplanin on mature osteoblasts expressing podoplanin in the medullary cavity of a part of the bone.


1960 ◽  
Vol XXXV (IV) ◽  
pp. 575-584 ◽  
Author(s):  
C. Borel ◽  
J. Frei ◽  
A. Vannotti

ABSTRACT Enzymatic studies, on leucocytes of pregnant women, show an increase of the alkaline phosphatase activity and a decrease of the glucose consumption and lactate production, as well as of proteolysis. The oxygen consumption, with succinate as substrate, does not vary.


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