scholarly journals THE FINE STRUCTURE OF VON EBNER'S GLAND OF THE RAT

1970 ◽  
Vol 44 (2) ◽  
pp. 340-353 ◽  
Author(s):  
Arthur R. Hand
Keyword(s):  
Fine Structure ◽  
Cell Membrane ◽  
Golgi Complex ◽  
Secretory Granules ◽  
Myoepithelial Cells ◽  
Duct Cells ◽  
Golgi Region ◽  
Granule Membrane ◽  
Cytological Features ◽  
Basal Portion

The fine structure of von Ebner's gland was studied in untreated rats and rats stimulated to secrete by fasting-refeeding or injection of pilocarpine. Cytological features were similar to those reported for pancreas and parotid gland. Abundant granular endoplasmic reticulum filled the basal portion of the cell, a well-developed Golgi complex was located in the vicinity of the nucleus, and the apical portion of the cell was filled with dense secretory granules. Dense heterogeneous bodies resembling lysosomes were closely associated with the Golgi complex. Coated vesicles were seen in the Golgi region and also in continuity with the cell membrane. Granule discharge occurred by fusion of the granule membrane with the cell membrane at the secretory surface. Successive fusion of adjacent granules to the previously fused granule formed a connected string of granules in the apical cytoplasm. Myoepithelial cells were present within the basement membrane, and nerve processes were seen adjacent to acinar and myoepithelial cells. Duct cells resembled the intercalated duct cells of the major salivary glands.

scholarly journals Distribution of basal lysosomes in exocrine acinar cells.

1987 ◽  
Vol 35 (5) ◽  
pp. 565-570 ◽  
Author(s):  
C Oliver ◽  
Y Yuasa
Keyword(s):  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Guinea Pig ◽  
Secretory Granules ◽  
Acinar Cells ◽  
The Other ◽  
Basal Region ◽  
Golgi Region ◽  
Basal Portion ◽  
Two Populations

We examined the distribution of trimetaphosphatase (TMPase)-positive basal lysosomes in pancreas, parotid, submandibular, sublingual, and exorbital lacrimal glands from rats, rabbits, and guinea pigs. The location of the basal lysosomes was compared to that of the acid phosphatase (AcPase)-positive lysosomes. In all of the tissues examined from rat and rabbit, AcPase activity was localized primarily to the Golgi region. Reaction product was localized in GERL, immature secretory granules, and lysosomes lying adjacent to the Golgi apparatus. TMPase activity was found in basal lysosomes and in occasional elongated lysosomes adjacent to the Golgi apparatus. In guinea pig, the distribution of TMPase activity was identical to that seen in the other two species, but a significant number of lysosomes in the basal region of the cells also contained AcPase activity. These results confirm and extend our previous finding (J Histochem Cytochem 31:1209, 1983) that exocrine acinar cells possess two distinct populations of lysosomes. The lysosomes in the Golgi region contain both AcPase and TMPase activity, whereas those in the basal portion of the cells are reactive predominantly for TMPase. The functional significance of the two populations of lysosomes is not understood at present.

Fine Structure of the Ultimobranchial Gland in the Chick

1971 ◽  
Vol 29 ◽  
pp. 510-511
Author(s):  
A. S. Chan
Keyword(s):  
Fine Structure ◽  
Epithelial Cells ◽  
Cell Membrane ◽  
Electron Density ◽  
Osmium Tetroxide ◽  
Secretory Granules ◽  
Parenchymal Cell ◽  
Cell Types ◽  
Dark Cells ◽  
Ultimobranchial Gland

Although the ultimobranchial gland of the chick has been shown to contain large amounts of calcitonin relatively few reports have been published on its fine structure. In the present study, the ultrastructure of the chick ultimobranchial gland, with emphasis on the cells which appear to be the producers of the hormone, will be examined. Ultimobranchial glands were obtained from twenty 2-week-old chicks and fixed in glutaraldehyde followed by osmium tetroxide.The gland is composed of aggregate of cords and clusters of cells interspersed with variable numbers of cyst-like cavities. Two parenchymal cell types, namely, light and dark cells can be recognized (Figs. 1,2,3). Epithelial cells, varying from columnar to cuboidal, line the cavities of the cysts.Light cells form the majority of the cell types (Fig. 1). The cytoplasm is characterized by the presence of membrane-limited secretory granules, measuring from 100 to 350 mμ in diameter. The contents of the secretory granules vary in electron density from moderate to extreme (Figs. 1,2). Secretory granules are distributed randomly in the cytoplasm although some are lined near the cell membrane.

scholarly journals Coexistence of renin and cathepsin B in secretory granules of granular duct cells in male mouse submandibular gland.

1993 ◽  
Vol 41 (3) ◽  
pp. 433-438 ◽  
Author(s):  
K Sano ◽  
S Waguri ◽  
N Sato ◽  
E Kominami ◽  
Y Uchiyama
Keyword(s):  
Submandibular Gland ◽  
Golgi Complex ◽  
Cathepsin B ◽  
Cysteine Proteinase ◽  
Secretory Granules ◽  
Interstitial Cells ◽  
Double Immunostaining ◽  
Duct Cells ◽  
Cathepsin H ◽  
Rat Pituitary

Cathepsin B, a representative lysosomal cysteine proteinase, has been demonstrated to coexist with renin in secretary granules of rat pituitary LH/FSH cells and renal juxtaglomerular cells. We investigated immunocytochemically the localization of cathepsins B, H, and L in the submandibular gland of male mice, in which active renin is also produced. By light microscopy, granular immunodeposits for cathepsin B were detected in epithelial cells of the gland, particularly in granular duct cells and interstitial cells. Immunoreactivity for cathepsins H and L was mainly found in interstitial cells, although that for cathepsin H was weakly seen in acinar cells. By electron microscopy, immunogold particles indicating cathepsin B intensely labeled small granules near the Golgi complex of granular duct cells and weakly labeled large secretory granules, whereas those showing renin labeled both granules. Double immunostaining co-localized immunogold particles showing renin and cathepsin B in small perinuclear granules near the Golgi complex. Some immunopositive granules seemed to be closely associated with the Golgi elements. These results indicate that the co-localization of renin and cathepsin B is also seen in secretory granules of granular duct cells in the mouse submandibular gland, as seen in rat juxtaglomerular and LH/FSH cells. This suggests that cathepsin B is one of the possible candidates for the renin-processing enzyme.

scholarly journals FURTHER STUDIES ON THE THETA CELL OF THE MOUSE ANTERIOR PITUITARY AS REVEALED BY ELECTRON MICROSCOPY, WITH SPECIAL REFERENCE TO THE MODE OF SECRETION

1962 ◽  
Vol 15 (1) ◽  
pp. 85-97 ◽  
Author(s):  
Masao Sano
Keyword(s):  
Cell Membrane ◽  
Anterior Pituitary ◽  
Amorphous Materials ◽  
Distal Part ◽  
Secretory Granules ◽  
Complete Loss ◽  
Low Density ◽  
Cell Type ◽  
Golgi Vesicles ◽  
Golgi Region

Theta cells reported previously as a new cell type in the anterior pituitary of the mouse were examined with the electron microscope. This type of cell is distinguished by the presence of pleomorphic secretory granules, a characteristic arrangement of the rough surfaced variety of endoplasmic reticulum, a well developed Golgi complex, and an eccentrically located nucleus. The secretory granules are seen at first as small granules of low density within the Golgi vesicles. While they are within the Golgi vesicles they become larger and denser. Simultaneously they move from the proximal to the distal part of the Golgi region and finally emerge from the Golgi area as mature granules in the cytoplasm. Thus, secretory granules are always enveloped by a limiting membrane which originates from the wall of the Golgi vesicle. At the stage of granule-extrusion, the cell membrane fuses with the limiting membrane of the granules and openings in the cell membrane appear at the place of extrusion. The granules then appear to lie within inpocketings of the cell membrane. They lose their density within these inpocketings or within the cytoplasm and occasionally show fragmentation. After complete loss of density, the granules are extruded as amorphous materials to the territory outside of the cell.

Pituitary Follicular Cells: Their Origin, Possible Function and Fate

1974 ◽  
Vol 32 ◽  
pp. 34-35
Author(s):  
E. Horvath ◽  
K. Kovacs ◽  
G. Penz ◽  
C. Ezrin
Keyword(s):  
Fine Structure ◽  
Secretory Granules ◽  
Follicular Cells ◽  
Human Pituitary ◽  
Rat Pituitary ◽  
Pituitary Glands ◽  
Junctional Complexes

Follicular structures, in the rat pituitary, composed of cells joined by junctional complexes and possessing few organelles and few, if any, secretory granules, were first described by Farquhar in 1957. Cells of the same description have since been observed in several species including man. The importance of these cells, however, remains obscure. While studying human pituitary glands, we have observed wide variations in the fine structure of follicular cells which may lead to a better understanding of their morphogenesis and significance.

Ultrastructural Aspects of Golgi Complex Function in Parathyroid Cells of Winter Frogs

1973 ◽  
Vol 31 ◽  
pp. 680-681
Author(s):  
William J. Dougherty
Keyword(s):  
Golgi Complex ◽  
Secretory Granules ◽  
Complex Function ◽  
Secretory Activity ◽  
Secretory Proteins ◽  
Perivascular Spaces ◽  
Pituitary Cells ◽  
Electron Microscopic ◽  
Ca Ions ◽  
Regulation Of Secretion

The regulation of secretion in exocrine and endocrine cells has long been of interest. Electron microscopic and other studies have demonstrated that secretory proteins synthesized on ribosomes are transported by the rough ER to the Golgi complex where they are concentrated into secretory granules. During active secretion, secretory granules fuse with the cell membrane, liberating and discharging their contents into the perivascular spaces. When secretory activity is suppressed in anterior pituitary cells, undischarged secretory granules may be degraded by lysosomes. In the parathyroid gland, evidence indicates that the level of blood Ca ions regulates both the production and release of parathormone. Thus, when serum Ca is low, synthesis and release of parathormone are both stimulated; when serum Ca is elevated, these processes are inhibited.

Further Studies on the Ultrastructure of Harderian Gland in Adult Rats

1974 ◽  
Vol 32 ◽  
pp. 288-289
Author(s):  
Alfredo Feria-Velasco ◽  
Guadalupe Tapia-Arizmendi
Keyword(s):  
Fine Structure ◽  
Domestic Fowl ◽  
Animal Species ◽  
Acinar Cells ◽  
Harderian Gland ◽  
Myoepithelial Cells ◽  
The Other ◽  
Albino Rats ◽  
Adult Rats ◽  
Cell Components

The fine structure of the Harderian gland has been described in some animal species (hamster, rabbit, mouse, domestic fowl and albino rats). There are only two reports in the literature dealing on the ultrastructure of rat Harderian gland in adult animals. In one of them the author describes the myoepithelial cells in methacrylate-embbeded tissue, and the other deals with the maturation of the acinar cells and the formation of the secretory droplets. The aim of the present work is to analize the relationships among the acinar cell components and to describe the two types of cells located at the perifery of the acini.

Fine structure of the rectal papillae of the oriental fruuit fly, Dacus dorsalis Hendel (Tephritidae, Diptera Insecta)

1990 ◽  
Vol 48 (3) ◽  
pp. 498-499
Author(s):  
Len Wen-Yung ◽  
Mei-Jung Lin
Keyword(s):  
Fine Structure ◽  
Cell Membrane ◽  
Intercellular Space ◽  
Anterior Part ◽  
Apical Cell ◽  
Posterior Part ◽  
Apical Cell Membrane ◽  
Dacus Dorsalis ◽  
Radial Cell ◽  
Circular Base

Four cone-shaped rectal papillae locate at the anterior part of the rectum in Dacus dorsalis fly. The circular base of the papilla protrudes into the haemolymph (Fig. 1,2) and the rest cone-shaped tip (Fig. 2) inserts in the rectal lumen. The base is surrounded with the cuticle (Fig. 5). The internal structure of the rectal papilla (Fig. 3) comprises of the cortex with the columnar epithelial cells and a rod-shaped medulla. Between them, there is the infundibular space and many trabeculae connect each other. Several tracheae insert into the papilla through the top of the medulla, then run into the cortical epithelium and locate in the intercellular space. The intercellular sinuses distribute in the posterior part of the rectal papilla.The cortex of the base divides into about thirty segments. Between segments there is a radial cell (Fig. 4). Under the cuticle, the apical cell membrane of the cortical epithelium is folded into a regular border of leaflets (Fig. 5).

Ultrastructural studies of the relationship between actin filaments and secretory granules

1990 ◽  
Vol 48 (3) ◽  
pp. 458-459
Author(s):  
Ellen Holm Nielsen
Keyword(s):  
Electron Microscopy ◽  
Colloidal Gold ◽  
Actin Filaments ◽  
Secretory Granules ◽  
Secretory Cells ◽  
Ultrastructural Studies ◽  
Transmission Electron ◽  
Granule Membrane ◽  
Ultrathin Sections ◽  
Lowicryl K4m

In secretory cells a dense and complex network of actin filaments is seen in the subplasmalemmal space attached to the cell membrane. During exocytosis this network is undergoing a rearrangement facilitating access of granules to plasma membrane in order that fusion of the membranes can take place. A filamentous network related to secretory granules has been reported, but its structural organization and composition have not been examined, although this network may be important for exocytosis.Samples of peritoneal mast cells were frozen at -70°C and thawed at 4°C in order to rupture the cells in such a gentle way that the granule membrane is still intact. Unruptured and ruptured cells were fixed in 2% paraformaldehyde and 0.075% glutaraldehyde, dehydrated in ethanol. For TEM (transmission electron microscopy) cells were embedded in Lowicryl K4M at -35°C and for SEM (scanning electron microscopy) they were placed on copper blocks, critical point dried and coated. For immunoelectron microscopy ultrathin sections were incubated with monoclonal anti-actin and colloidal gold labelled IgM. Ruptured cells were also placed on cover glasses, prefixed, and incubated with anti-actin and colloidal gold labelled IgM.

scholarly journals Redistribution of a rab3-like GTP-binding protein from secretory granules to the Golgi complex in pancreatic acinar cells during regulated exocytosis

1994 ◽  
Vol 124 (1) ◽  
pp. 43-53 ◽  
Author(s):  
BP Jena ◽  
FD Gumkowski ◽  
EM Konieczko ◽  
GF von Mollard ◽  
R Jahn ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Golgi Complex ◽  
Binding Protein ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Apical Plasma Membrane ◽  
Gtp Binding Protein ◽  
Regulated Exocytosis ◽  
Gtp Binding

Regulated secretion from pancreatic acinar cells occurs by exocytosis of zymogen granules (ZG) at the apical plasmalemma. ZGs originate from the TGN and undergo prolonged maturation and condensation. After exocytosis, the zymogen granule membrane (ZGM) is retrieved from the plasma membrane and ultimately reaches the TGN. In this study, we analyzed the fate of a low M(r) GTP-binding protein during induced exocytosis and membrane retrieval using immunoblots as well as light and electron microscopic immunocytochemistry. This 27-kD protein, identified by a monoclonal antibody that recognizes rab3A and B, may be a novel rab3 isoform. In resting acinar cells, the rab3-like protein was detected primarily on the cytoplasmic face of ZGs, with little labeling of the Golgi complex and no significant labeling of the apical plasmalemma or any other intracellular membranes. Stimulation of pancreatic lobules in vitro by carbamylcholine for 15 min, resulted in massive exocytosis that led to a near doubling of the area of the apical plasma membrane. However, no relocation of the rab3-like protein to the apical plasmalemma was seen. After 3 h of induced exocytosis, during which time approximately 90% of the ZGs is released, the rab3-like protein appeared to translocate to small vesicles and newly forming secretory granules in the TGN. No significant increase of the rab3-like protein was found in the cytosolic fraction at any time during stimulation. Since the protein is not detected on the apical plasmalemma after stimulation, we conclude that recycling may involve a membrane dissociation-association cycle that accompanies regulated exocytosis.

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