scholarly journals Demonstration of anionic sites in human eccrine and apocrine sweat glands in post-embedded ultra-thin sections with cationic colloidal gold: effect of enzyme digestion on these anionic sites.

1993 ◽  
Vol 41 (8) ◽  
pp. 1197-1207 ◽  
Author(s):  
K Saga ◽  
M Takahashi
Keyword(s):  
Colloidal Gold ◽  
Dermatan Sulfate ◽  
Sweat Glands ◽  
Secretory Cells ◽  
Anionic Sites ◽  
Chondroitinase Abc ◽  
Dark Cell ◽  
Luminal Membrane ◽  
Cationic Colloidal Gold ◽  
Eccrine Sweat Glands

We localized anionic sites ultrastructurally in human eccrine and apocrine sweat glands with a poly-L-lysine-gold complex (cationic colloidal gold). Anionic sites were labeled by incubating Lowicryl K4M-embedded sections on droplets of cationic colloidal gold. In eccrine sweat glands, colloidal gold particles were restricted to the basolateral membrane of the secretory cells at low pH, whereas the luminal membrane did not react with the gold particles. Chondroitinase ABC digested these anionic sites. This indicates that chondroitin sulfate and/or dermatan sulfate constitutes anionic sites in the basal labyrinth of eccrine sweat glands. In apocrine sweat glands, the luminal membrane of the secretory cells showed strong reaction at low pH, whereas the contraluminal membrane did not show any reaction. Neuraminidase completely digested these anionic sites, which indicated that the anionic charge of the apocrine lumen was due to sialic acid. Differences in distribution and susceptibility to enzymes of anionic sites in cell membranes between eccrine and apocrine sweat glands may reflect functional differences between these glands. Dark cell granules in eccrine secretory cells were negative for the anionic sites when sections were labeled without any pre-treatment. However, pre-incubation of the grids on EGTA or deionized water unmasked the anionic sites on the dark cell granules. The positive staining after EGTA treatment was greatly decreased by reincubation with CaCl2. These results suggested that Ca blocked anionic sites in dark cell granules. Exposed anionic sites were digested with chondroitinase ABC. This indicated that chondroitinase ABC and/or dermatan sulfate composed the anionic sites in dark cell granules.

scholarly journals Proliferating cells in human eccrine and apocrine sweat glands.

1995 ◽  
Vol 43 (12) ◽  
pp. 1217-1221 ◽  
Author(s):  
Y Morimoto ◽  
K Saga
Keyword(s):  
Proliferating Cell Nuclear Antigen ◽  
Myoepithelial Cells ◽  
Nuclear Antigen ◽  
Sweat Glands ◽  
Secretory Cells ◽  
Proliferating Cells ◽  
Peripheral Cells ◽  
Proliferating Cell ◽  
Eccrine Sweat Glands

Morphological observations of sweat glands showed degenerated debris of secretory cells in the secretory lumen in both apocrine and eccrine sweat glands. This suggested that dead secretory cells of human eccrine and apocrine sweat glands were released into the lumen and replaced by other cells. However, we did not know which type of cells replaced lost secretory cells. Therefore, we studied the proliferating cells in human eccrine and apocrine sweat glands by labeling S-phase cells in vitro with 5-bromo-2'-deoxyuridine (BrdUrd) and by immunostaining proliferation-associated proliferating cell nuclear antigen (PCNA) with anti-PCNA monoclonal antibody. BrdUrd and anti-PCNA antibody labeled a few secretory cells in eccrine and apocrine sweat glands, but neither method labeled myoepithelial cells. Luminal and peripheral cells of the eccrine and apocrine coiled duct were labeled with both BrdUrd and PCNA. However, we could not find any highly proliferative germinative cells in coiled ducts. Our results suggest that lost secretory cells could be replaced by proliferation of secretory cells themselves rather than by proliferation of myoepithelial cells or duct cells.

Anti-D47: a monoclonal antibody reacting with the secretory cells of human eccrine sweat glands*

1983 ◽  
Vol 109 (5) ◽  
pp. 509-513 ◽  
Author(s):  
J. KANITAKIS ◽  
D. SCHMITT ◽  
A. BERNARD ◽  
L. BOUMSELL ◽  
J. THIVOLET
Keyword(s):  
Monoclonal Antibody ◽  
Sweat Glands ◽  
Secretory Cells ◽  
Eccrine Sweat Glands ◽  
Eccrine Sweat

Visualization of the anionic sites in the cell wall of apple fruit using a cationic colloidal gold probe

1993 ◽  
Vol 51 ◽  
pp. 320-321
Author(s):  
Stéphane Roy ◽  
William S. Conway ◽  
Alley E. Watada ◽  
Christopher D. Pooley ◽  
William P. Wergin
Keyword(s):  
Cell Wall ◽  
Colloidal Gold ◽  
Apple Fruit ◽  
Gold Complex ◽  
Anionic Sites ◽  
Wall Strength ◽  
Anionic Binding Sites ◽  
Cationic Colloidal Gold ◽  
Softening Process ◽  
Gold Probe

The ripening of fleshy fruits involves a softening process that consists of biochemical changes in the cell wall and leads to cell separation. Calcium is an important constituent of the cell wall and plays roles in maintaining the firmness of fruit and in reducing postharvest decay. The modification of cell wall strength is believed to be influenced by calcium that interacts with acidic pectic polymers to form crossbridges. This study examined how the frequency and distribution of anionic binding sites in the cell walls of apple fruit were influenced by calcium infiltration.Mature “Golden Delicious” apple fruits were pressure infiltrated with either H2O or a 4% solution of CaCl2 and the pericarp was sampled and processed according to standard procedures. Cationic poly-Llysine colloidal gold complex was used in a one-step procedure to visualize anionic sites in muro. Observations were performed with light microscopy, following silver intensification, and with transmission electron microscopy.

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 FINE STRUCTURE OF THE MYOEPITHELIUM OF THE ECCRINE SWEAT GLANDS OF MAN

1965 ◽  
Vol 27 (3) ◽  
pp. 551-563 ◽  
Author(s):  
Richard A. Ellis
Keyword(s):  
Endoplasmic Reticulum ◽  
Striated Muscle ◽  
Myoepithelial Cells ◽  
Sweat Glands ◽  
Secretory Cells ◽  
Apical Surface ◽  
Dense Granules ◽  
Dense Zone ◽  
Eccrine Sweat Glands ◽  
Eccrine Sweat

The secretory coils of glutaraldehyde-osmium tetroxide-fixed and Epon-Araldite-embedded eccrine sweat glands from the palms of young men were studied with the electron microscope. The myoepithelial cells lie on the epithelial side of the basement membrane and abut other epithelial elements directly. The irregularly serrated base of the cell has dense thickenings along the plasma membrane which alternate with zones bearing pits; the smooth apical surface lacks dense thickenings, is studded with pits, and conjoined to secretory cells by occasional desmosomes. Masses of myofilaments, 50 A in diameter, fill most of the cell and are associated with irregular dense zones. In cross-section the arrangement of the myofilaments seems identical with that of the I band of striated muscle, and the dense zone has typical Z band structure. A few microtubules and cytoplasmic cores bearing profiles of the endoplasmic reticulum, filamentous mitochondria, and glycogen granules penetrate the fibrillar masses and run parallel to the oriented myofilaments. In the perinuclear zone, Golgi membranes, rough- and smooth-surfaced elements of the endoplasmic reticulum, mitochondria, glycogen, microtubules, lipid, pigment, and dense granules are variable components in the cytoplasm. The interrelationships of the myoepithelial cells with the secretory cells suggest that the former may act as regulators, controlling the flow of metabolites to the secretory epithelium.

scholarly journals Immunoelectron microscopic localization of epidermal growth factor in the eccrine and apocrine sweat glands.

1992 ◽  
Vol 40 (2) ◽  
pp. 241-249 ◽  
Author(s):  
K Saga ◽  
M Takahashi
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Immunoelectron Microscopy ◽  
Secretory Granules ◽  
Myoepithelial Cells ◽  
Sweat Glands ◽  
Secretory Cells ◽  
Epidermal Growth ◽  
Eccrine Sweat Glands ◽  
Eccrine Sweat

We studied the localization of the epidermal growth factor (EGF) in eccrine and apocrine sweat glands with light microscopic and electron microscopic immunohistochemistry. Anti-human EGF (anti-hEGF) polyclonal antiserum and anti-hEGF monoclonal antibody (MAb) were used for the study. Light microscopic immunohistochemistry with monoclonal and polyclonal antibodies showed that hEGF-like immunoreactivity was strongly positive in the myoepithelial cells and weakly positive in the secretory cells of eccrine sweat glands. In apocrine sweat glands, it was strongly positive in the secretory cells as well as in the myoepithelial cells. Immunoelectron microscopy with polyclonal antibody showed that hEGF-like immunoreactivity was present in secretory granules of apocrine secretory cells. These granules had mitochondrion-like internal structure. No reactivity was observed on the eccrine secretory cells by immunoelectron microscopy. Neither dark cell granules nor mitochondria in eccrine secretory cells were labeled with anti-hEGF antibody. In both eccrine and apocrine sweat glands, hEGF-like immunoreactivity was diffusely present in the cytoplasm of myoepithelial cells. However, nuclei and mitochondria of myoepithelial cells were devoid of immunoreactivity for hEGF. Our observations indicate that apocrine sweat glands may secrete more hEGF in the sweat than eccrine sweat glands.

scholarly journals Detection of glomerular anionic sites in post-embedded ultra-thin sections using cationic colloidal gold.

1991 ◽  
Vol 39 (7) ◽  
pp. 965-972 ◽  
Author(s):  
N P Goode ◽  
M Shires ◽  
D M Crellin ◽  
A M Davison
Keyword(s):  
Hyaluronic Acid ◽  
Chondroitin Sulfate ◽  
Colloidal Gold ◽  
Endothelial Glycocalyx ◽  
Computer Assisted ◽  
Nuclear Staining ◽  
Anionic Sites ◽  
Thin Sections ◽  
Cationic Colloidal Gold ◽  
Influence Of Ph

We detected glomerular anionic sites in fixed, LR Gold-embedded ultra-thin tissue sections using cationic colloidal gold. Manual and computer-assisted quantitation were compared, and the influence of pH and glycosaminoglycan-degrading enzymes on site expression was examined. Both quantitation methods produced similar results. Alteration of pH within a narrow range (pH 2.5-3.0) markedly affected the staining pattern. At pH 2.5, epithelial and endothelial glycocalyx and regular sites restricted to the lamina rara externa were stained. At pH 3.0 and above, glycocalyx was unstained but intracellular and nuclear staining was present; glomerular basement membrane (GBM) and mesangial matrix sites were abundant. After chondroitinase ABC or hyaluronidase digestion, GBM staining was eliminated at pH 2.0 and reduced at pH 7.0 (p less than 0.001), suggesting that degraded sites are associated with chondroitin sulfate or hyaluronic acid. By contrast, prolonged heparitinase I digestion was ineffective at either pH. Digestion of purified substrates revealed crossreactivity of heparitinase towards chondroitin sulfate and of chondroitinase towards hyaluronic acid. Since tissue sites were reduced by chondroitinase but not heparitinase, we suggest that degradation is due to hyaluronidase activity of chondroitinase and the anionic sites are associated with hyaluronic acid. However, the influence of pH indicates that lamina rara externa sites are structurally distinct from other GBM anionic sites.

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