Alkaline-phosphatase and adenosine-triphosphatase histochemical reactions in the salivary glands of cat, dog and man, with particular reference to the myoepithelial cells

Histochemie ◽  
1970 ◽  
Vol 24 (3) ◽  
pp. 214-229 ◽  
Author(s):  
J. R. Garrett ◽  
J. D. Harrison
Keyword(s):  
Alkaline Phosphatase ◽  
Salivary Glands ◽  
Adenosine Triphosphatase ◽  
Myoepithelial Cells

scholarly journals Inhibition studies of alkaline phosphatase in hard tissue-forming cells.

1975 ◽  
Vol 23 (5) ◽  
pp. 342-347 ◽  
Author(s):  
A Linde ◽  
B C Magnusson
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Adenosine Triphosphatase ◽  
Ruthenium Red ◽  
Inorganic Pyrophosphatase ◽  
Alkaline Ph ◽  
Hard Tissue ◽  
Assay Condition ◽  
Phosphatase Inhibitors ◽  
Inhibition Studies

The effects of the alkaline phosphatase inhibitors levamisole and R 8231 on p-nitro-phenylphosphatase, inorganic pyrophosphatase and adenosine triphosphatase (ATPase) activities in dentingenically active odontoblasts were studied. The p-nitrophenylphosphatase and inorganic pyrophosphatase activities were inhibited, while 40% of the ATP-splitting enzyme activity remained under the assay condition used. This finding, togeather with earlier studies, indicates that at least two different phosphatase are active at alkaline pH in hard tissue-forming cells; on nonspecific alkaline phosphatase and one specific ATPase. The ATPase activity is uninfluenced by ouabain and ruthenium red and is activated by Ca-2+ ions.

scholarly journals Histological and certain histochemical observations on the labial salivary glands of the buffalo , bubalus bubalis.

2010 ◽  
Vol 9 (1) ◽  
pp. 17
Author(s):  
A. I. Jabbar
Keyword(s):  
Salivary Glands ◽  
Bubalus Bubalis ◽  
Myoepithelial Cells ◽  
Ductal System ◽  
Labial Glands

Histological, morphometric and histochemical investigations were carried out on the labial salivary glands of the buffalo. Both the upper and lower labial glands of the buffalo are branched tubuloacinar type and composed of serous acini surrounded by myoepithelial cells. Histochemically it showed seromucous character, they secrete neutral mucopolysaccharides, mucopolysaccharides acid, and few sulfated mucopolysaccharides. The labial salivary glands of buffalo posses ductal system of both the intralobular ductules and interlobular ducts.

Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases

1979 ◽  
Vol 53 (1) ◽  
pp. 45-49 ◽  
Author(s):  
T. K. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Functional Significance ◽  
Adenosine Triphosphatase ◽  
Vas Deferens ◽  
Gland Cells ◽  
Vitelline Gland ◽  
Receptaculum Seminis ◽  
Almost All

ABSTRACTCertain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; tsetes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.

Oxytocin receptors in rat involuting mammary gland

1983 ◽  
Vol 61 (7) ◽  
pp. 631-635 ◽  
Author(s):  
Melvyn S. Soloff ◽  
Michael H. Wieder
Keyword(s):  
Alkaline Phosphatase ◽  
Mammary Gland ◽  
Fold Increase ◽  
Myoepithelial Cells ◽  
Oxytocin Receptor ◽  
Secretory Cells ◽  
Specific Marker ◽  
Oxytocin Receptors ◽  
Pregnancy And Lactation ◽  
Receptor Number

Oxytocin-receptor concentrations in the rat mammary gland were determined by Scatchard analyses with [3H]oxytocin. There was about a 100-fold increase in the number of receptors per mammary gland between the 1st day of pregnancy and late lactation. The number of receptors then fell markedly during postweaning mammary regression, but rose again during a second pregnancy and lactation cycle. The changes in oxytocin-receptor number corresponded to changes in alkaline phosphatase activity per mammary gland. These results strongly support data suggesting that alkaline phosphatase, like oxytocin receptors, is a specific marker for mammary myoepithelial cells. Despite the fall in oxytocin-receptor number per mammary gland during postweaning regression, the concentration of receptors, expressed per milligram of protein, increased 10-fold over lactating levels on the 6th day of regression. Thereafter, receptor concentrations declined, but were still elevated about fivefold over lactating levels on the 15th day of regression. It is likely that the increased concentration of receptors was due to a decrease in the relative amount of nontarget secretory cells. The factors that regulate the concentration of oxytocin receptors on mammary myoepithelial cells are presently unknown; however, the involuting mammary system may be practical for obtaining enriched populations of oxytocin-sensitive myoepithelial cells.

scholarly journals The tegument ofSchistosoma mansoni: a histochemical investigation

Parasitology ◽  
1976 ◽  
Vol 72 (1) ◽  
pp. 99-109 ◽  
Author(s):  
P. R. Wheater ◽  
R. A. Wilson
Keyword(s):  
Alkaline Phosphatase ◽  
Adenosine Triphosphatase ◽  
Hydrolytic Enzymes ◽  
Mitochondrial Enzymes ◽  
Biosynthetic Activity ◽  
Histochemical Investigation ◽  
Enzyme Content ◽  
Dorsal Tegument ◽  
Main Components

The main components of the schistosome tegument were found to be neutral glycoprotein and phospholipid; a small quantity of glycolipid was observed in the male dorsal tegument. The tegument can be differentiated from other schistosome tissues on the basis of enzyme content; three hydrolytic enzymes were shown to be specifically localized in the tegument: alkaline phosphatase, adenosine triphosphatase and indoxyl esterase. It is suggested that these enzymes could be used as intrinsic markers for tegument structures. The subtegumental cells appear to be the major sites of biosynthetic activity since they contain large amounts of RNA and mitochondrial enzymes.

scholarly journals Histochemical localization of potassium-stimulated P-nitrophenylphosphatase activity in the somatosensory cortex of the rat.

1976 ◽  
Vol 24 (6) ◽  
pp. 731-739 ◽  
Author(s):  
W L Stahl ◽  
S H Broderson
Keyword(s):  
Alkaline Phosphatase ◽  
Enzymatic Activity ◽  
Somatosensory Cortex ◽  
Adenosine Triphosphatase ◽  
Large Diameter ◽  
Cortical Layers ◽  
Outer Portion ◽  
Cacodylate Buffer ◽  
Neuronal Processes ◽  
Rat Somatosensory Cortex

Potassium-stimulated p-nitrophenylphosphatase (K+-pNPPase) activity was investigated in rat somatosensory cortex where 64-88% of enzymatic activity survived 5-10 min of fixation with 3% formaldehyde in 0.1 M cacodylate buffer, pH 7.4. Potassium-stimulated activity was inhibited by 1-10 mM ouabain. Levamisole (1.7 mM) inhibited brain alkaline phosphatase activity, facilitating the detection of K+-pNPPase activity. Strontium (10-20 mM) inhibited enzymatic activity by 38-75%. In parallel histochemical studies reaction product was found in strata, with cortical layers 2, 3, 4 and the outer portion of 5 containing the heaviest deposits. Highly reactive, vertically oriented, large diameter fibers were seen as groups between the outer portion of layer 5 and the pail surface. These fibers apparently arborize in the superficial layers. Smaller fibers were also positive and were oriented in various planes. The highest density of smaller, positive fibers occurred in layers 2 through 5. All positive fibers appeared to be axons or dendrites. Reaction product was not heavily concentrated in neuron perikarya or in glial elements. Sections did not contain reaction product when incubated in media lacking K+ or containing ouabain. The convergence of data from parallel histochemical and biochemical approaches supports the conclusion that the reactivity localized in the cerebral cortex represented the site of K+-pNPPase, a known component of the Na+,K+-adenosine triphosphatase complex. Neuronal processes demonstrated the highest enzymatic activity and may be most important in the active transport of Na+ and K+ in somatosensory cortex.

scholarly journals The Melanocyte System of Cattle Skin I. Amelanotic Dendritic Cells of Epidermis

1973 ◽  
Vol 26 (4) ◽  
pp. 973 ◽  
Author(s):  
AV Schleger ◽  
KG Bean
Keyword(s):  
Alkaline Phosphatase ◽  
Dendritic Cells ◽  
Adenosine Triphosphatase ◽  
Epidermal Cells ◽  
Specific Alkaline Phosphatase

The amelanotic dendritic cells of cattle skin have been studied using the histochemical reactions for non-specific alkaline phosphatase and specific cholinesterase. These epidermal cells in cattle skin show no reaction for adenosine triphosphatase.

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