scholarly journals FINE STRUCTURAL LOCALIZATION OF CHOLINESTERASE ACTIVITY IN THE RAT SUBMANDIBULAR GLAND

1970 ◽  
Vol 18 (10) ◽  
pp. 730-739 ◽  
Author(s):  
BRUCE I. BOGART

The innervation of the rat submandibular gland was investigated by means of electron microscopy and cytochemical techniques. Axonal swellings partially depleted of their Schwann cell investment were observed in relationship to myoepithelial cells, acinar cells, ducts, capillaries and smooth muscle cells of arterioles. No direct contacts were found to exist between these elements and the nerve fibers. Axonal swellings containing mitochondria and vesicles fell into two distinct types: those characterized by small agranular vesicles and larger vesicles with pale cores and those characterized by small agranular vesicles and small vesicles with dense cores. Reaction product due to acetylcholinesterase activity was observed to be associated with the axolemma and the Schwann cell membrane at the axon-Schwann cell interface of many unmyelinated nerves found in relationship to both the vascular and parenchymal elements of the gland. Activity was found in association with the surface pits and vesicles of myoepithelial cells and arteriolar smooth muscle cells and with the rough endoplasmic reticulum and the nuclear envelope of the myoepithelial cells. Axonal swellings devoid of activity were observed particularly in relationship to arterioles. Reaction product was found only at the axon-Schwann cell interface when sections were incubated in medium for the demonstration of butyrylcholinesterase activity, while no reaction product was found upon addition of eserine sulfate to any of the media. The possibility that the reaction product due to acetylcholinesterase activity observed in association with the axolemma and the surface vesicles and pits of the myoepithelial cells and the arteriolar smooth muscle cells may define the autonomic cholinergic junction in the rat submandibular gland was explored.

1967 ◽  
Vol 33 (1) ◽  
pp. 93-102 ◽  
Author(s):  
Peter M. Robinson ◽  
Christopher Bell

Acetylcholinesterase has been localized at the autonomic neuromuscular junction in the bladder of the toad (Bufo marinus) by the Karnovsky method. High levels of enzyme activity have been demonstrated in association with the membranes of cholinergic axons and the adjacent membranes of the accompanying Schwann cells. The synaptic vesicles stained in occasional cholinergic axons. After longer incubation times, the membrane of smooth muscle cells close to cholinergic axons also stained. Axons with only moderate acetylcholinesterase activity or with no activity at all were seen in the same bundles as cholinergic axons, but identification of the transmitter in these axons was not possible.


1980 ◽  
Vol 84 (3) ◽  
pp. 633-654 ◽  
Author(s):  
W W Franke ◽  
E Schmid ◽  
C Freudenstein ◽  
B Appelhans ◽  
M Osborn ◽  
...  

Myoepithelial cells from mammary glands, the modified sweat glands of bovine muzzle, and salivary glands have been studied by electron microscopy and by immunofluorescence microscopy in frozen sections in an attempt to further characterize the type of intermediate-sized filaments present in these cells. Electron microscopy has shown that all myoepithelial cells contain extensive meshworks of intermediate-sized (7--11-nm) filaments, many of which are anchored at typical desmosomes or hemidesmosomes. The intermediate-sized filaments are also intimately associated with masses of contractile elements, identified as bundles of typical 5--6-nm microfilaments and with characteristically spaced dense bodies. This organization resembles that described for various smooth muscle cells. In immunofluorescence microscopy, using antibodies specific for the various classes of intermediate-sized filaments, the myoepithelial cells are strongly decorated by antibodies to prekeratin. They are not specifically stained by antibodies to vimentin, which stain mesenchymal cells, nor by antibodies to chick gizzard desmin, which decorate fibrils in smooth muscle Z bands and intercalated disks in skeletal and cardiac muscle of mammals. Myoepithelial cells are also strongly stained by antibodies to actin. The observations show (a) that the epithelial character, as indicated by the presence of intermediate-sized filaments of the prekeratin type, is maintained in the differentiated contractile myoepithelial cell, and (b) that desmin and desmin-containing filaments are not generally associated with musclelike cell specialization for contraction but are specific to myogenic differentiation. The data also suggest that in myoepithelial cells prekeratin filaments are arranged--and might function--in a manner similar to the desmin filaments in smooth muscle cells.


1985 ◽  
Vol 33 (5) ◽  
pp. 439-445 ◽  
Author(s):  
A Topilko ◽  
B Caillou

Using the indirect thiocholine method, the ultrastructural localization of acetylcholinesterase (AChE) activity in the normal rat submandibular gland was studied. Cytochemical demonstration of AChE is based on coupling the hydrolysis of acetylthiocholine iodide to the precipitation of heavy metal salts. AChE-associated reaction product was selectively revealed in the perinuclear space and in the endoplasmic reticulum of the intercalated duct cells, in some cells of granular convoluted tubules, and in the striated duct epithelium, as well as in the myoepithelial cells. Although AChE activity generally occurred inside the cells, electron-dense precipitates were shown in intercellular space and in the stroma of the gland. Fine localization of AChE activity was also found in nerve bundles, predominantly between axons and between axons and Schwann cell. Our observations indicate that AChE is synthesized in the epithelium of the ducts and in the myoepithelial cells of the salivary gland. It is not known yet whether this enzyme is released from the intracytoplasmic membrane system into the extracellular space and then transported to the regions of the gland innervation. Conceivably AChE synthesized in the submandibular gland cells could also be considered an inhibitory modulator of the regulatory functions of biologically active polypeptides.


1976 ◽  
Vol 55 (4) ◽  
pp. 628-632
Author(s):  
Leon A. Leonard ◽  
Mohamed Sharawy

A histochemical technique has been used to demonstrate myosin and myosinlike substances in muscle, endothelium, cilia, and myoepithelial cells. When this technique was applied to human dental pulp, similar nzyosinlike substances were demonstrated in smooth muscle cells, fibroblasts, endothelium, and odontoblastic processes.


Author(s):  
J.M. Minda ◽  
E. Dessy ◽  
G. G. Pietra

Pulmonary lymphangiomyomatosis (PLAM) is a rare disease occurring exclusively in women of reproductive age. It involves the lungs, lymph nodes and lymphatic ducts. In the lungs, it is characterized by the proliferation of smooth muscle cells around lymphatics in the bronchovascular bundles, lobular septa and pleura The nature of smooth muscle proliferation in PLAM is still unclear. Recently, reactivity of the smooth muscle cells for HMB-45, a melanoma-related antigen has been reported by immunohistochemistry. The purpose of this study was the ultrastructural localization of HMB-45 immunoreactivity in these cells using gold-labeled antibodies.Lung tissue from three cases of PLAM, referred to our Institution for lung transplantation, was embedded in either Poly/Bed 812 post-fixed in 1% osmium tetroxide, or in LR White, without osmication. For the immunogold technique, thin sections were placed on Nickel grids and incubated with affinity purified, monoclonal anti-melanoma antibody HMB-45 (1:1) (Enzo Diag. Co) overnight at 4°C. After extensive washing with PBS, grids were treated with Goat-anti-mouse-IgG-Gold (5nm) (1:10) (Amersham Life Sci) for 1 hour, at room temperature.


Sign in / Sign up

Export Citation Format

Share Document