scholarly journals THE CYTOLOGY OF THE NORMAL PARATHYROID GLANDS OF MAN AND VIRGINIA DEER

1963 ◽  
Vol 16 (2) ◽  
pp. 379-400 ◽  
Author(s):  
Bryce L. Munger ◽  
Sanford I. Roth
Keyword(s):  
Golgi Apparatus ◽  
Secretory Granules ◽  
Light And Electron Microscopy ◽  
Blood Stream ◽  
Chief Cells ◽  
Cytoplasmic Organelles ◽  
Golgi Region ◽  
Capillary Endothelial Cells ◽  
Transitional Cells ◽  
Two Phases

The normal parathyroids of six humans and a Virginia deer were studied by light and electron microscopy. The parenchyma of the deer parathyroid is composed of uniform chief cells, which contained 100 to 400 mµ electron-opaque, membrane-limited granules, presumed to be secretory granules, in addition to the usual cytoplasmic organelles. Desmosomes are present between adjacent cells, and rare cilia are observed protruding from the chief cells into the intercellular space. The human parathyroids contain chief cells in two phases—active and inactive—as well as oxyphil cells. Active chief cells have a large Golgi apparatus, sparse glycogen, numerous secretory granules, and rare cilia. Inactive chief cells contain a small Golgi apparatus, abundant glycogen, and few secretory granules. Both forms have the usual cytoplasmic organelles and, between adjacent cells, desmosomes. Oxyphil cell cytoplasm is composed of tightly packed mitochondria and glycogen granules, with rare secretory granules. Cells with cytoplasmic characteristics intermediate between chief and oxyphil cells, possibly representing transitional cells, have been observed. Secretory granules of both man and deer are composed of 100 to 200 A particles and short rods, and the granules develop from prosecretory granules in the Golgi region of the cell. The human secretory granules are smaller and more variable in shape than those of the deer. The granules are iron and chrome alum hematoxylin-positive, argyrophilic, and aldehyde fuchsin-positive, permitting light microscopic identification. They are also found in the capillary endothelial cells of the parathyroid and in its surrounding connective tissue. The secretory granules of the parathyroid cells can thus be followed from their formation in the Golgi apparatus almost to their extrusion into the blood stream.

scholarly journals CYTOCHEMICAL STUDIES OF LYSOSOMES, GOLGI APPARATUS AND ENDOPLASMIC RETICULUM IN SECRETION AND PROTEIN UPTAKE BY ADRENAL MEDULLA CELLS OF THE RAT

1968 ◽  
Vol 16 (5) ◽  
pp. 320-336 ◽  
Author(s):  
ERIC HOLTZMAN ◽  
REGINA DOMINITZ
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Adrenal Medulla ◽  
Secretory Granules ◽  
Light And Electron Microscopy ◽  
Multivesicular Bodies ◽  
Frozen Sections ◽  
Protein Uptake ◽  
Thiamine Pyrophosphatase

The adrenalin-producing cells of the rat adrenal medulla have been studied by light and electron microscopy. Frozen sections of glutaraldehyde-perfused material were incubated for demonstration of "marker" enzymes for lysosomes (acid phosphatase, aryl sulfatase) and Golgi apparatus (thiamine pyrophosphatase). In addition, the uptake and fate of intravenously administered horseradish peroxidase was followed. Acid phosphatase activity is demonstrable in secretory granules, Golgi saccules, vesicles in the Golgi area and in the agranular tubules and cisternae (GERL) from which secretory granules appear to form at the inner surface of the Golgi apparatus. Endoplasmic reticulum with ribosomes on only one surface is closely apposed to both inner and outer aspects of the Golgi apparatus. Peroxidase is taken up in vesicles, tubules and "cup-like" bodies. The latter apparently transform into multivesicular bodies. A possible source of the acid phosphatase found in multivesicular bodies is the small vesicles from the Golgi apparatus or GERL.

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.

scholarly journals Effects of secretory stimulation on the Golgi apparatus and GERL of rat parotid acinar cells.

1984 ◽  
Vol 32 (4) ◽  
pp. 403-412 ◽  
Author(s):  
A R Hand ◽  
C Oliver
Keyword(s):  
Golgi Apparatus ◽  
Functional Relationship ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Dynamic Nature ◽  
Parotid Acinar Cells ◽  
Golgi Region ◽  
Thiamine Pyrophosphatase ◽  
Rat Parotid

The structure and cytochemistry of the Golgi apparatus and GERL of rat parotid acinar cells was studied after in vivo secretory stimulation with isoproterenol. Discharge of mature secretory granules was complete within 1 hr after isoproterenol injection, but immature granules in the Golgi region or near the lumen were not released. At early times (1-5 hr) after isoproterenol, acid phosphatase (AcPase) activity was markedly increased in GERL and immature secretory granules compared to uninjected controls. GERL appeared increased in extent and numerous continuities with immature granules were observed. Reaccumulation of mature secretory granules was first evident at 5 hr, and was almost complete by 16 hr after isoproterenol. Thiamine pyrophosphatase (TPPase) activity, normally restricted to the trans Golgi saccules, was frequently present in immature granules during this time. Narrow cisternae resembling GERL, occasionally in continuity with immature granules, also contained TPPase reaction product. By 16-24 hr after stimulation, the activity and distribution of AcPase and TPPase were similar to control cells. These results demonstrate the dynamic nature of the Golgi apparatus and GERL in parotid acinar cells, and emphasize the close structural and functional relationship between these two structures.

scholarly journals ELABORATION OF THE MATRIX GLYCOPROTEIN OF ENAMEL BY THE SECRETORY AMELOBLASTS OF THE RAT INCISOR AS REVEALED BY RADIOAUTOGRAPHY AFTER GALACTOSE-3H INJECTION

1971 ◽  
Vol 51 (1) ◽  
pp. 26-51 ◽  
Author(s):  
Alfred Weinstock ◽  
C. P. Leblond
Keyword(s):  
Golgi Apparatus ◽  
Phosphotungstic Acid ◽  
Secretory Granules ◽  
Low Ph ◽  
Enamel Matrix ◽  
Rat Incisor ◽  
Golgi Region ◽  
The Matrix

The elaboration of enamel matrix glycoprotein was investigated in secretory ameloblasts of incisor teeth in 30–40-g rats. To this end, the distribution of glycoprotein was examined histochemically by the use of phosphotungstic acid at low pH, while the formation of glycoprotein was traced radioautographically in animals sacrificed 2.5–30 min after galactose-3H injection. Histochemically, the presence of glycoprotein is observed in ameloblasts as well as in the enamel matrix; in ameloblasts glycoprotein occurs within the Golgi apparatus in amounts increasing from the outer to the inner face of the stacks of saccules, and is concentrated in condensing vacuoles and secretory granules; in the enamel matrix, glycoprotein is observed within linear subunits. Radioautographs at 2.5 min after injection demonstrate the uptake of galactose-3H label by Golgi saccules, indicating that galactose-3H is incorporated into glycoprotein within this organelle. After 5–10 min, the label collects in the condensing vacuoles and secretory granules of the Golgi region. By 20–30 min, the label appears in the secretory granules of the apical (Tomes') processes, as well as in the enamel matrix (next to the distal end of the apical processes, and at the tips of matrix prongs). In conclusion, galactose contributes to the formation of glycoprotein within the Golgi apparatus. The innermost saccules then distribute the completed glycoprotein to condensing vacuoles, which later evolve into secretory granules. These granules rapidly migrate to the apical processes, where they discharge their glycoprotein content to the developing enamel.

Spermatogenesis in the Dragonfly with Particular Reference to the Cytoplasmic Organelles

1972 ◽  
Vol 30 ◽  
pp. 110-111
Author(s):  
Sant S. Sekhon
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Mature Sperm ◽  
Electron Microscopic ◽  
Cytoplasmic Organelles ◽  
Microscopic Studies ◽  
Insect Sperm ◽  
Large Round

Although there have been numerous studies concerning the morphogenetic changes accompanying the maturation of insect sperm, only a few deal with the sperm differentiation in the dragonflies. In two recent electron microscopic studies Kessel, has comprehensively treated the erlationship of microtubules to the nucleus and mid-piece structures during spermiogenesis in the dragonfly. The purpose of this study is to follow the sequential nuclear and cytoplasmic changes which accompany the differentiation of spermatogonium into a mature sperm during spermatogenesis in the dragonfly (Aeschna sp.).The dragonfly spermatogonia are characterized by large round nuclei. Loosely organized chromatin is usually unevenly distributed within the spermatogonial nuclei. The scant cytoplasm surrounding the nucleus contains mitochondria, the Golgi apparatus, elements of endoplasmic reticulum and numerous ribosomes (Fig. 1).

The structure of the gills of the axolotl, Ambystoma mexicanum

1987 ◽  
Vol 45 ◽  
pp. 824-825
Author(s):  
Mohinder S. Jarial
Keyword(s):  
Leydig Cells ◽  
Secretory Granules ◽  
Light And Electron Microscopy ◽  
Cell Types ◽  
Ambystoma Mexicanum ◽  
Basal Cells ◽  
Granular Cells ◽  
Gill Filaments ◽  
Mitotic Figures ◽  
Apical Membranes

The axolotl is a strictly aquatic salamander in which the larval external gills are retained throughout life. The external gills of the adult axolotl have been studied by light and electron microscopy for ultrastructural evidence of ionic transport. The thin epidermis of the gill filaments and gill stems is composed of 3 cell types: granular cells, the basal cells and a sparce population of intervening Leydig cells. The gill epidermis is devoid of muscles, and no mitotic figures were observed in any of its cells.The granular cells cover the gill surface as a continuous layer (Fig. 1, G) and contain secretory granules of different forms, located apically (Figs.1, 2, SG). Some granules are found intimately associated with the apical membrane while others fuse with it and release their contents onto the external surface (Fig. 3). The apical membranes of the granular cells exhibit microvilli which are covered by a PAS+ fuzzy coat, termed “glycocalyx” (Fig. 2, MV).

scholarly journals SYNTHESIS, MIGRATION, AND RELEASE OF PRECURSOR COLLAGEN BY ODONTOBLASTS AS VISUALIZED BY RADIOAUTOGRAPHY AFTER [3H]PROLINE ADMINISTRATION

1974 ◽  
Vol 60 (1) ◽  
pp. 92-127 ◽  
Author(s):  
Melvyn Weinstock ◽  
C. P. Leblond
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Phosphotungstic Acid ◽  
Secretory Granules ◽  
Low Ph ◽  
Collagen Fibrils ◽  
Dentin Collagen ◽  
Odontoblast Process ◽  
High Radioactivity

The elaboration of dentin collagen precursors by the odontoblasts in the incisor teeth of 30–40-g rats was investigated by electron microscopy, histochemistry, and radioautography after intravenous injection of tritium-labeled proline. At 2 min after injection, when the labeling of blood proline was high, radioactivity was restricted to the rough endoplasmic reticulum, indicating that it is the site of synthesis of the polypeptide precursors of collagen, the pro-alpha chains. At 10 min, when the labeling of blood proline had already declined, radioactivity was observed in spherical portions of Golgi saccules containing entangled threads, and, at 20 min, radioactivity appeared in cylindrical portions containing aggregates of parallel threads. The parallel threads measured 280–350 nm in length and stained with the low pH-phosphotungstic acid technique for carbohydrate and with the silver methenamine technique for aldehydes (as did extracellular collagen fibrils). The passage of label from spherical to cylindrical Golgi portions is associated with the reorganization of entangled into parallel threads, which is interpreted as the packing of procollagen molecules. Between 20 and 30 min, prosecretory and secretory granules respectively became labeled. These results indicate that the cylindrical portions of Golgi saccules transform into prosecretory and subsequently into secretory granules. Within these granules, the parallel threads, believed to be procollagen molecules, are transported to the odontoblast process. At 90 min and 4 h after injection, label was present in predentin, indicating that the labeled content of secretory granules had been released into predentin. This occurred by exocytosis as evidenced by the presence of secretory granules in fusion with the plasmalemma of the odontoblast process. It is proposed that pro-alpha chains give rise to procollagen molecules which assemble into parallel aggregates in the Golgi apparatus. Procollagen molecules are then transported within secretory granules to the odontoblast process and released by exocytosis. In predentin procollagen molecules would give rise to tropocollagen molecules, which would then polymerize into collagen fibrils.

scholarly journals INDUCTION OF ENDOMETRIAL PEROXIDASE SYNTHESIS AND SECRETION BY ESTROGEN AND ESTROGEN ANTAGONIST

1974 ◽  
Vol 62 (2) ◽  
pp. 449-459 ◽  
Author(s):  
Andrew Churg ◽  
Winston A. Anderson
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Combined Treatment ◽  
Initial Injection ◽  
Immature Rats ◽  
Glandular Cells ◽  
Endogenous Peroxidase ◽  
Estrogen Antagonist

Synthesis of peroxidase was induced in the uterine epithelium of immature rats by multiple doses over a 24–96-h period of either 17 ß-estradiol, the estrogen-antagonist Parke-Davis CI-628, or a combination of estradiol plus antagonist. Endogenous peroxidase activity first appeared in the cisternae of the rough endoplasmic reticulum of surface epithelial and glandular cells within 24–48 after the initial injection. Uterine peroxidase activity was also visible in the cisternae of the Golgi apparatus, in Golgi-derived secretory granules, and within the uterine and glandular lumen. Some cells of the epithelium produced little or no peroxidase, even after 96 h. Whereas the antagonist appeared to induce synthesis and secretion of peroxidase, neither the antagonist alone nor the combined treatment (estradiol plus antagonist) reproduced the estradiol-mediated growth in organ size and increased lumen diameter.

scholarly journals Golgi apparatus, GERL, and secretory granule formation within neurons of the hypothalamo-neurohypophysial system of control and hyperosmotically stressed mice.

1981 ◽  
Vol 90 (2) ◽  
pp. 474-484 ◽  
Author(s):  
R D Broadwell ◽  
C Oliver
Keyword(s):  
Golgi Apparatus ◽  
Secretory Granule ◽  
Supraoptic Nucleus ◽  
Salt Water ◽  
Secretory Granules ◽  
Hyperosmotic Stress ◽  
Granule Formation ◽  
Smooth Membrane ◽  
Secondary Lysosomes ◽  
The Relationship

The vasopressin-producing neurons of the hypothalamo-neurohypophysial system are a particularly good model with which to consider the relationship between the Golgi apparatus nd GERL and their roles in secretory granule production because these neurons increase their synthesis and secretion of vasopressin in response to hyperosmotic stress. Enzyme cytochemical techniques for acid phosphatase (AcPase) and thiamine pyrophosphatase (TPPase) activities were used to distinguish GERL from the Golgi apparatus in cell bodies of the supraoptic nucleus from normal mice, mice hyperosmotically stressed by drinking 2% salt water, and mice allowed to recover for 5-10 d from hyperosmotic stress. In nonincubated preparations of control supraoptic perikarya, immature secretory granules at the trans face of the Golgi apparatus were frequently attached to a narrow, smooth membrane cisterna identified as GERL. Secretory granules were occasionally seen attached to Golgi saccules. TPPase activity was present in one or two of the trans Golgi saccules; AcPase activity appeared in GERL and attached immature secretory granules, rarely in the trans Golgi saccules, and in secondary lysosomes. As a result of hyperosmotic stress, the Golgi apparatus hypertrophied, and secretory granules formed from all Golgi saccules and GERL. Little or no AcPase activity could be demonstrated in GERL, whereas all Golgi saccules and GERL-like cisternae were TPPase positive. During recovery, AcPase activity in GERL returned to normal; however, the elevated TPPase activity and secretory granule formation seen in GERL-like cisternae and all Golgi saccules during hyperosmotic stress persisted. These results suggest that under normal conditions GERL is the predominant site for the secretory granule formation, but during hyperosmotic stress, the Golgi saccules assume increased importance in this function. The observed cytochemical modulations in Golgi saccules and GERL suggest that GERL is structurally and functionally related to the Golgi saccules.

scholarly journals THE ELABORATION OF PROTEIN AND CARBOHYDRATE BY RAT PARATHYROID CELLS AS REVEALED BY ELECTRON MICROSCOPE RADIOAUTOGRAPHY

1971 ◽  
Vol 51 (3) ◽  
pp. 596-610 ◽  
Author(s):  
K. Nakagami ◽  
H. Warshawsky ◽  
C. P. Leblond
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Intravenous Injection ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Glycoprotein Precursor ◽  
Secretion Granules ◽  
And Migration ◽  
The One ◽  
Membrane Cell

The parathyroid glands of young rats were radioautographed after a single injection of the protein precursor tyrosine-3H in the hope of identifying the sites of synthesis and migration of newly formed protein in the gland cells. The same procedure was used after injection of the glycoprotein precursor galactose-3H. As early as 2 min after intravenous injection of tyrosine-3H, the label was mainly found in the rough endoplasmic reticulum suggesting that cisternal ribosomes are sites of protein synthesis. By 5 and 10 min, much of the label had migrated from the rough endoplasmic reticulum into the Golgi apparatus. By 20 and 30 min, some label had migrated from there into secretory granules. By 45 min and 1 hr, the label content of the cell had decreased, indicating release of labeled material outside the cell. At 2 min after intravenous injection of galactose-3H, the label was mainly present in the Golgi apparatus, where presumably galactose is taken up into glycoprotein. By 10 min, some label appeared in secretion granules and by 30 min release of the material to the outside of the cell was under way. In conclusion, it is likely that the tyrosine-labeled protein material consists mainly of the parathyroid hormone. The galactose-labeled carbohydrate material would be either associated with the hormone in the cell or be part of a distinct glycoprotein which may be the one present on the outer surface of the plasma membrane (cell coat).

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