The alkaline phosphatase activity of the tissues and the primordial germ cells during the embryonic development of the mouse

1959 ◽  
Vol 48 (4) ◽  
pp. 1271-1274
Author(s):  
S. M. Tsiper
1950 ◽  
Vol s3-91 (13) ◽  
pp. 89-105
Author(s):  
T. YAO

1. The localization of alkaline phosphatase during the post-embryonic development of Drosophila melanogaster has been described. 2. In the larvae, nuclear phosphatase is always demonstrable, but cytoplasmic phosphatase shows a more restricted distribution. Salivary glands, mid-gut, Malpighian tubes, and pericardial cells are richest in cytoplasmic phosphatase. 3. The larva prior to puparium formation is characterized by a decrease of alkaline phosphatase in the internal organs with a simultaneous increase in the hypodermis. 4. The phosphatase data support the view that the prepupa is actually an intrapuparial larval instar. 5. Pupation is accompanied, by a very noticeable increase of alkaline phosphatase which is mainly confined to the cytoplasm. The high enzyme activity is maintained for the first day and a half after head eversion: there is a subsequent decline until at the time of emergence most organs are inactive. However, certain organs retain their alkaline phosphatase activity. 6. As in embryogenesis, alkaline phosphatase seems to be more concerned with histo-differentiation than with chemo-differentiation. 7. Alkaline phosphatase (and also acid phosphatase) actively participates in the process of histolysis or cellular degeneration. 8. The alkaline phosphatase activity of the pericardial cells, together with other morphological evidence, indicates that these cells are endocrine organs which play important roles in Drosophila metamorphosis. 9. Cytochemical evidence suggests that alkaline phosphatase in Drosophila is probably playing a part in the carriage of organic substances across the membrane barrier.


1968 ◽  
Vol 100 (6) ◽  
pp. 649-655 ◽  
Author(s):  
S. N. H. Naqvi ◽  
Shahid H. Ashrafi ◽  
M. A. H. Qadri

AbstractThe acid and alkaline phosphatase activity was measured in the developing egg and in the alimentary canal of aging nymphs as well as adult males and females of different ages. Para-nitrophenol was used as colorimetric standard and disodium p-nitrophenyl phosphate as substrate. Activity was measured in terms of micromoles of p-nitrophenol liberated from the substrate as a result of enzyme action.Acid phosphatase activity was noticed to increase with the embryonic development and was higher than in the case of alkaline phosphatase. The alkaline phosphatase activity was lowest in the freshly laid egg, but increased more sharply than acid phosphatase during embryonic development.The activity of both the acid and alkaline phosphatases was highest in the first instar and declined gradually to the fifth instar. The activity of acid phosphatase was higher than alkaline phosphatase in all stages except the first instar where it was almost equal. The activity of both the enzymes was higher during the intermoulting period and declined at each moult indicating a hormone–enzyme relationship.In adults, activity of both the enzymes increased up to the maturation period after which the activity gradually decreased. Acid phosphatase activity was generally higher in males whereas alkaline phosphatase activity was generally higher in females. In almost all cases, the acid phosphatase activity was found to be higher than the alkaline phosphatase.


2020 ◽  
Author(s):  
Ida Marie Boisen ◽  
John Erik Nielsen ◽  
Ireen Kooij ◽  
Jovana Kaludjerovic ◽  
Peter J. O’Shaughnessy ◽  
...  

AbstractTesticular microcalcifications consist of hydroxyapatite and their demonstration by ultrasound has been associated with increased risk of testicular germ cell cancer (TGCT). Here, we show that fibroblast growth factor 23 (FGF23), a bone-specific regulator of phosphate homeostasis, is expressed in testicular germ cell neoplasia in situ (GCNIS), embryonal carcinoma (EC), and human embryonic stem cells. FGF23 is not glycosylated in TGCTs and thus rapidly cleaved into a C-terminal fragment that serves as a competitive antagonist for full-length FGF23. High levels of C-terminal FGF23 occupy the receptor formed by Klotho and FGF receptor 1 (FGFR1) in the germ cells facilitating a shift in the expression of phosphate transport proteins from SLC34A2 to SLC34A1 in seminiferous tubules adjacent to GCNIS. Fgf23 knockout mice have a marked epididymal deposition of hydroxyapatite, while the testicular phenotype is milder with spermatogenic arrest and focal germ-cell-specific expression of the bone-like markers runt-related transcription factor 2 (RUNX2) and bone gamma-carboxyglutamic acid-containing protein (BGLAP). In accordance, mice with no functional androgen receptor and lack of circulating gonadotropins develop microcalcifications in 94% of cases and have lower Slc34a2, and higher Slc34a1 and Bglap expression. In accordance, human testicular specimens with microcalcifications also have lower SLC34A2, and focally germ cells express SLC34A1, BGLAP, and RUNX2. Importantly, calcium or phosphate induced osteogenic transdifferentiation of a spermatogonial cell line in vitro demonstrated by induction of alkaline phosphatase activity and deposition of hydroxyapatite, which could be fully rescued by pyrophosphate (PPi). Severe microcalcifications were also found in a mouse model with Sertoli-cell ablation particularly when Sertoli-ablation was conducted prepubertally where the germ cells retain stem cell potential. In conclusion, cancer-related microcalcifications may arise secondary to gonadal mineral alterations, which in combination with impaired Sertoli cell function and reduced PPi due to high alkaline phosphatase activity in GCNIS and TGCTs, facilitates osteogenic transdifferentiation of testicular germ cells and deposition of hydroxyapatite.


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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