Effect of Alkaline and Acid Phosphatases on Clotting:

1966 ◽  
Vol 15 (03/04) ◽  
pp. 365-380 ◽  
Author(s):  
P. G Iatridis ◽  
J. H Ferguson

SummaryAlkaline phosphatase is found to enhance the activation of factor IX by SF. The correlation of the distribution of alkaline phosphatase in electrophoretic fractions with the clotting tests suggest that the “beta” fraction contains the responsible factor for the acceleratory effect of alkaline phosphatase on clotting.Acid phosphatase, while not exerting a direct inhibitory effect on SF, does enhance the plasmatic anti-SF activity. The “beta” and “F-gamma” fractions seem to contain the responsible factor of acid phosphatase for the plasmatic anti-SF enhancement.SF preparation has no acid or alkaline phosphatase activity.A tentative schema is proposed to explain the effects of acid and alkaline phosphatase on clotting.

Blood ◽  
1950 ◽  
Vol 5 (3) ◽  
pp. 267-277 ◽  
Author(s):  
W. F. HAIGHT ◽  
R. J. ROSSITER

Abstract 1. The acid and alkaline phosphatase activity has been determined on a series of suspensions of white cells obtained from both man and the rabbit by several different methods. 2. A statistical analysis of the results shows that for both species the alkaline phosphatase of white cell suspensions is confined chiefly to the polymorphonuclear leukocyte and the acid phosphatase is chiefly in the lymphocyte, although the polymonphonuclear leukocyte contains lesser concentrations of this enzyme also. 3. Although this qualitative distribution was the same for both species studied, quantitatively the rabbit differed from man. The activity of the alkaline phosphatase of the rabbit polymorphonuclear leukocyte was eight times that of the corresponding human cell, while the activity of the acid phosphatase of the human lymphocyte was more than twice that of rabbit lymphocyte.


2019 ◽  
Vol 71 (2) ◽  
pp. 509-520
Author(s):  
A.M.S. Reis ◽  
K.P. Oliveira ◽  
I.H.F. Paula ◽  
A.P. Silva ◽  
J.F. Tarragô ◽  
...  

ABSTRACT The aim of this study was to evaluate the effect of concentrations of caffeine on the viability, synthesis activity and gene expression in cultures of chondrocytes. Extracted articular cartilage from the femurs and tibias of 15 Wistar rats at three days old to isolate chondrocytes. Chondrocytes were cultured in chondrogenic medium (control) or supplemented with caffeine (0.5, 1.0, 2.0mM). Cell viability, alkaline phosphatase activity and collagen synthesis were assessed using colorimetric assays at 7, 14, 21 days. The chondrocyte cultures of all groups grown under coverslips were stained with hematoxylin-eosin to determine the percentage of cells/field and with PAS, safranin O, alcian blue to determine the percentage of matrix chondrogenic/field at 21 days. The expressions of gene transcripts for aggrecan, collagen-II, Sox-9, Runx-2 and alkaline phosphatase were also evaluated by RT-PCR at 21 days. The means were compared using Student-Newman-Keuls. Caffeine significantly reduced the conversion of MTT to formazan, percentage of cells/field, collagen synthesis, alkaline phosphatase activity, synthesis of PAS+, safranin O+ and alcian blue+ chondrogenic matrix, and the expression of aggrecan, Sox-9 and II collagen. It is concluded that caffeine at concentrations of 0.5, 1.0, 2.0mM has a direct inhibitory effect on chondrogenesis in cultures of chondrocytes from rats.


1969 ◽  
Vol 17 (12) ◽  
pp. 799-806 ◽  
Author(s):  
JON E. WERGEDAL ◽  
DAVID J. BAYLINK

The distribution of acid and alkaline phosphatase activity in the rat tibia has been studied in transverse sections sawed from fresh undemineralized diaphyses. The endosteal resorbing surfaces had the highest acid phosphatase activity as demonstrated with 50 mM α-naphthol phosphate as the substrate. Strong activity was present not only in osteoclasts and adjacent osteocytes but extracellularly lining Howship's lacunae. In areas of bone formation, moderate acid phosphatase activity was present in osteoblasts and young osteocytes. In addition, a zone of activity was found at the mineralizing front where mineralization is initiated. This active zone ( a) was separated from the active periosteal cell layer by a zone of inactive osteoid and ( b) in formol-calcium-fixed demineralized sections extended into young bone. The identity of the mineralizing front was confirmed by tetracycline labeling. The activity at the mineralizing front had the properties of an enzyme. Alkaline phosphatase activity demonstrated with naphthol ASTR phosphate was largely associated with the osteoblasts and other mesenchymal cells at forming surfaces.


Author(s):  
Luciana de Oliveira Franco ◽  
Thayza Christina Montenegro Stamford ◽  
Marcos Antônio Barbosa de Lima ◽  
Rita de Cassia Carvalho Maia ◽  
Tânia Lúcia Montenegro Stamford ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document