Localization of alkaline phosphatase in eccrine and apocrine sweat glands

1993 ◽  
Vol 6 (1) ◽  
pp. 22
Author(s):  
Kenji Saga ◽  
Yousuke Morimoto ◽  
Makoto Takahashi
Keyword(s):  
Alkaline Phosphatase ◽  
Sweat Glands

Histochemical studies on bovine sweat glands

1952 ◽  
Vol 42 (1-2) ◽  
pp. 155-158 ◽  
Author(s):  
S. H. Yang
Keyword(s):  
Alkaline Phosphatase ◽  
Chemical Composition ◽  
Sweat Glands ◽  
Zebu Cattle ◽  
Limited Extent ◽  
Sebaceous Glands ◽  
Histochemical Tests

1. Histochemical tests have been applied to the socalled sweat glands and their secretions of Zebu and Ayrshire cattle, the former to only a limited extent.2. For skin specimens of Ayrshire cattle positive reactions were obtained for ribonucleoprotein, arginine and alkaline phosphatase. Negative reactions were obtained for desoxyribonucleoprotein and acid glycerophosphatase.3. Neither the sweat glands of Ayrshire cattle nor those of Zebu cattle gave positive reactions for fats, lipids or cholesterol and its esters, although these were all present in the sebaceous glands of both breeds. Detectable amounts of phospholipid were not found in the sweat glands of the Ayrshire cattle and their secretions.4. The chemical composition of the secretion of bovine sweat glands differs markedly from that of human eccrine or apocrine sweat glands in not containing detectable amounts of glycogen, lipids and associated compounds or iron.

Ultrastructural localization of alkaline phosphatase activity in human eccrine and apocrine sweat glands.

1995 ◽  
Vol 43 (9) ◽  
pp. 927-932 ◽  
Author(s):  
K Saga ◽  
Y Morimoto
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Membranes ◽  
Ultrastructural Localization ◽  
Sweat Glands ◽  
Secretory Cells ◽  
Electron Microscopic ◽  
Enzyme Cytochemistry ◽  
Alp Activity ◽  
Eccrine Sweat Glands ◽  
Eccrine Sweat

Alkaline phosphatase (ALP) is a membrane-bound enzyme that catalyzes the hydrolysis of inorganic and organic monophosphate esters at alkaline pH. Although the functions of ALP are poorly understood, it is believed to be involved in membrane transport. Because little is known about the functions and distribution of ALP in the sweat glands, we studied the localization of ALP in human sweat glands with light and electron microscopic enzyme cytochemistry. In eccrine sweat glands, ALP was restricted to the cell membranes of intercellular canaliculi. Luminal cell membranes of secretory cells that are in continuity with intercellular canaliculi did not show ALP activity. These results suggest that ALP participates in the production of primary sweat at intercellular canaliculi. In apocrine sweat glands, basal cell membranes of secretory cells and myoepithelial cell membranes that were in apposition with each other showed ALP activity, where as no activity was seen in eccrine sweat glands. These differences in the distribution of ALP in myoepithelial cells between eccrine and apocrine sweat glands might be related to the functional differences of these sweat glands. ALP histochemistry could help to diagnose and to determine the direction of differentiation in sweat gland tumors.

scholarly journals The Skin of the Sheep: a Comparision of Body Regions

1968 ◽  
Vol 21 (3) ◽  
pp. 499 ◽  
Author(s):  
AG Lyne ◽  
DE Hollis
Keyword(s):  
Alkaline Phosphatase ◽  
Light Microscope ◽  
Sweat Glands ◽  
Body Region ◽  
Sebaceous Glands ◽  
Distinctive Features ◽  
Body Regions ◽  
Eccrine Glands ◽  
Asymmetrically Distributed ◽  
Dermal Papillae

Light-microscope studies reveal distinctive features in the hair- and woolgrowing skin of adult sheep. The epidermis is variable in thickness-usually thin on wool-growing regions and thicker on haired regions. The follicles are mostly in groups containing one, two, or three primary (P) follicles and a number of secondary (S) follicles. The SIP follicle ratios vary from zero to about 30, depending on the breed and body region. The capillaries, myoepithelium of sweat glands, and dermal papillae of the follicles are often reactive for alkaline phosphatase. This enzyme is also asymmetrically distributed in some follicle bulbs and here it might be related in some way to the segmentation of the fibre cortex and perhaps to the formation of crimped wool. The dermal and follicle nerve networks contain cholinesterases. The latter may also contain alkaline phosphatase. Encapsulated end-organs and tactile disks are occasionally present in both hair- and wool-growing skin. Melanocytes, most common near the dermo-epidermal junction, may also be present in the outer root sheaths of the follicles, sebaceous glands, sweat glands, and dermis. Acetylcholinesterase-positive branched cells are invariably present in the epidermis in all regions where there are follicles. Sebaceous glands are associated with all follicles and apocrine sweat glands with the P follicles only. The P follicles also possess erector muscles that react for cholinesterases. Both the subaceous glands and sweat glands are usually larger in haired regions than in wool-growing regions. Large "eccrine" glands open on the naked part of the muzzle.

The diagnosis of metabolic storage disease in skin biopsies (a light-, electronmicroscopic, and analytical study)

1978 ◽  
Vol 36 (2) ◽  
pp. 648-649
Author(s):  
W. Jurecka ◽  
W. Gebhart ◽  
H. Lassmann
Keyword(s):  
Storage Disease ◽  
Hunter Syndrome ◽  
Histochemical Demonstration ◽  
Sweat Glands ◽  
Type I ◽  
Storage Material ◽  
Scheie Syndrome ◽  
Storage Products ◽  
Skin Biopsies ◽  
Type V

Diagnosis of metabolic storage disease can be established by the determination of enzymes or storage material in blood, urine, or several tissues or by clinical parameters. Identification of the accumulated storage products is possible by biochemical analysis of isolated material, by histochemical demonstration in sections, or by ultrastructural demonstration of typical inclusion bodies. In order to determine the significance of such inclusions in human skin biopsies several types of metabolic storage disease were investigated. The following results were obtained.In MPS type I (Pfaundler-Hurler-Syndrome), type II (Hunter-Syndrome), and type V (Ullrich-Scheie-Syndrome) mainly “empty” vacuoles were found in skin fibroblasts, in Schwann cells, keratinocytes and macrophages (Dorfmann and Matalon 1972). In addition, prominent vacuolisation was found in eccrine sweat glands. The storage material could be preserved in part by fixation with cetylpyridiniumchloride and was also present within fibroblasts grown in tissue culture.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

In Situ Localization of PPAR Gamma and Uncoupling Protein in Mouse Embryo Sections Using Digoxigenin-Labeled Riboprobes

1996 ◽  
Vol 54 ◽  
pp. 32-33
Author(s):  
C. Jennermann ◽  
S. A. Kliewer ◽  
D. C. Morris
Keyword(s):  
Alkaline Phosphatase ◽  
Room Temperature ◽  
Uncoupling Protein ◽  
Ppar Gamma ◽  
Nuclear Hormone Receptor ◽  
Full Length ◽  
Northern Analysis ◽  
Peroxisome Proliferator

Peroxisome proliferator-activated receptor gamma (PPARg) is a member of the nuclear hormone receptor superfamily and has been shown in vitro to regulate genes involved in lipid metabolism and adipocyte differentiation. By Northern analysis, we and other researchers have shown that expression of this receptor predominates in adipose tissue in adult mice, and appears first in whole-embryo mRNA at 13.5 days postconception. In situ hybridization was used to find out in which developing tissues PPARg is specifically expressed.Digoxigenin-labeled riboprobes were generated using the Genius™ 4 RNA Labeling Kit from Boehringer Mannheim. Full length PPAR gamma, obtained by PCR from mouse liver cDNA, was inserted into pBluescript SK and used as template for the transcription reaction. Probes of average size 200 base pairs were made by partial alkaline hydrolysis of the full length transcripts. The in situ hybridization assays were performed as described previously with some modifications. Frozen sections (10 μm thick) of day 18 mouse embryos were cut, fixed with 4% paraformaldehyde and acetylated with 0.25% acetic anhydride in 1.0M triethanolamine buffer. The sections were incubated for 2 hours at room temperature in pre-hybridization buffer, and were then hybridized with a probe concentration of 200μg per ml at 70° C, overnight in a humidified chamber. Following stringent washes in SSC buffers, the immunological detection steps were performed at room temperature. The alkaline phosphatase labeled, anti-digoxigenin antibody and detection buffers were purchased from Boehringer Mannheim. The sections were treated with a blocking buffer for one hour and incubated with antibody solution at a 1:5000 dilution for 2 hours, both at room temperature. Colored precipitate was formed by exposure to the alkaline phosphatase substrate nitrobluetetrazoliumchloride/ bromo-chloroindlylphosphate.

Electron microscopic study of the membrane glycoproteins in the rat kidney after cisplatin treatment

1989 ◽  
Vol 47 ◽  
pp. 912-913
Author(s):  
S.K. Aggarwal
Keyword(s):  
Alkaline Phosphatase ◽  
Rat Kidney ◽  
Light And Electron Microscopy ◽  
Kidney Tissue ◽  
Membrane Glycoproteins ◽  
Electron Microscopic ◽  
Before And After ◽  
Interstrand Cross Links ◽  
Cross Links

The proposed primary mechanism of action of the anticancer drug cisplatin (Cis-DDP) is through its interaction with DNA, mostly through DNA intrastrand cross-links or DNA interstrand cross-links. DNA repair mechanisms can circumvent this arrest thus permitting replication and transcription to proceed. Various membrane transport enzymes have also been demonstrated to be effected by cisplatin. Glycoprotein alkaline phosphatase was looked at in the proximal tubule cells before and after cisplatin both in vivo and in vitro for its inactivation or its removal from the membrane using light and electron microscopy.Outbred male Swiss Webster (Crl: (WI) BR) rats weighing 150-250g were given ip injections of cisplatin (7mg/kg). Animals were killed on day 3 and day 5. Thick slices (20-50.um) of kidney tissue from treated and untreated animals were fixed in 1% buffered glutaraldehyde and 1% formaldehyde (0.05 M cacodylate buffer, pH 7.3) for 30 min at 4°C. Alkaline phosphatase activity and carbohydrates were demonstrated according to methods described earlier.

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