scholarly journals THE LOCALIZATION OF ENDOGENOUS PEROXIDASE IN THE LACRIMAL GLAND OF THE RAT DURING POSTNATAL DEVELOPMENT

1972 ◽  
Vol 53 (3) ◽  
pp. 662-680 ◽  
Author(s):  
V. Herzog ◽  
F. Miller
Keyword(s):  
Endoplasmic Reticulum ◽  
Postnatal Development ◽  
Rough Endoplasmic Reticulum ◽  
Lacrimal Gland ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Secretory Cells ◽  
Lacrimal Fluid ◽  
Endogenous Peroxidase

The distribution of endogenous peroxidase activity in the lacrimal gland of the rat during postnatal development was investigated by electron microscope cytochemistry Peroxidase activity is first found 6 hr after birth in only a few acinar cells At this stage, reaction product fills only localized segments of the scant rough endoplasmic reticulum and of the perinuclear cisternae. Peroxidase activity thus develops asynchronously in a given cell as well as in the secretory cell population as a whole 2 days after birth, all cisternae of the rough endoplasmic reticulum of a peroxidase-positive cell contain reaction product, but the majority of the acinar cells is still negative During the next days, the number of peroxidase-positive cells and the amount of the rough endoplasmic reticulum increase rapidly. By 15 days postparturition, all secretory cells are peroxidase-positive. Reaction product is then found in all cisternae of the rough endoplasmic reticulum including the perinuclear cisternae, in smooth surface vesicles located mainly between the rough endoplasmic reticulum and the Golgi stacks, in condensing vacuoles, and in all secretory granules The Golgi cisternae rarely contain reaction product In total homogenates and in fractions of glandular tissue of adult rats, peroxidatic and catalatic activities are demonstrable. The microsomal fractions and the postmicrosomal supernatants were used to separate peroxidase from catalase by precipitation with ammonium sulfate, and the following parameters were determined: substrate (H2O2-) optimum (∼ 2.0 x 10-4M), pH-optimum (pH 6 5), temperature-optimum (42°C), and the absorption maximum (415 nm before and 425 nm after addition of H2O2) The same parameters were obtained from lacrimal fluid peroxidase. Both peroxidase from lacrimal gland and that from lacrimal fluid are almost completely inhibited by 10-3M aminotriazole and are possibly identical enzymes. Peroxidase is secreted into lacrimal fluid, which does not contain catalase.

scholarly journals DEVELOPMENT OF ENDOGENOUS PEROXIDASE IN FETAL RAT SUBMANDIBULAR GLAND

1973 ◽  
Vol 21 (1) ◽  
pp. 42-50 ◽  
Author(s):  
SHOHEI YAMASHINA ◽  
TIBOR BARKA
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Submandibular Gland ◽  
Rough Endoplasmic Reticulum ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Prenatal Development ◽  
Reaction Products ◽  
Cell Type ◽  
Endogenous Peroxidase

The prenatal development of endogenous peroxidase activity in the submandibular gland of rat was investigated by means of the diaminobenzidine-H2O2 histochemical method. The submandibular gland of a 16-day-old fetus was composed of cords of uniform, undifferentiated cells which contained no secretory granules and revealed no peroxidase activity. Peroxidase activity first appeared at the 17th day of gestation in the cisternae of the rough endoplasmic reticulum and nuclear envelope in a few cells. At the 18th day of gestation cells which exhibited reaction products in the rough endoplasmic reticulum and nuclear envelope also contained secretory granules with a strong peroxidase activity. During the last days of gestation the number of peroxidase positive cells, which contained numerous secretory granules, increased. The peroxidase-containing cells are the immediate precursors of the proacinar cells of early postnatal stages. During the same time period, when the peroxidase-containing cells differentiated, a second cell type also differentiated in the cellular cords. The development of this cell type was marked by the appearance of secretory granules stainable with toluidine blue. Through the prenatal development, this cell type revealed no peroxidase activity and was identified with the terminal tubule cell of the newborn. The morphologic and cytochemical findings indicate that terminal tubule cells and proacinar cells are committed cells; the former differentiate toward 2nd order intercalated duct cells and the latter transform to mature acinar cells.

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 Relationship between the golgi apparatus, gerl, and secretory granules in acinar cells of the rat exorbital lacrimal gland

1977 ◽  
Vol 74 (2) ◽  
pp. 399-413 ◽  
Author(s):  
AR Hand ◽  
C Oliver
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Golgi Apparatus ◽  
Lacrimal Gland ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Secretory Proteins ◽  
Thiamine Pyrophosphatase ◽  
Variable Distance ◽  
Secretory Enzyme

The method of secretory granuleformation in the acinar cells of the rat exorbital lacrimal gland was studied by electron microscope morphological and cytochemical techniques. Immature secretory granules at the inner face of the Golgi apparatus were frequently attached to a narrow cisternal structure similar to GERL as described in neurons by Novikoff et al. (Novikoff, P. M., A. B. Novikoff, N. Quintana, and J.-J. Hauw. 1971. J. Cell Bio. 50:859-886). In the lacrimal gland. GERL was located adjacent to the inner Golgi saccule, or separated from it by a variable distance. Portions of GERL were often closely paralleled by modified cisternae of rough endoplasmic reticulum (RER), which lacked ribosomes on the surface adjacent to GERL. Diaminobenzidine reaction product of the secretory enzyme peroxidase was localized in the cisternae of the nuclear envelope, RER, peripheral Golgi vesicles, Golgi saccules, and immature and mature secretory granules. GERL was usually free of peroxidase reaction product or contained only a small amount. Thiamine pyrophosphatase reaction product was present in two to four inner Golgi saccules; occasionally, the innermost saccule was dilated and fenestrated, and contained less reaction product than the next adjacent saccule. Acid phosphatase (AcPase) reaction product was present in GERL, immature granules, and, rarely, in the innermost saccule, but not in the rest of the Golgi saccules. Thick sections of AcPase preparations viewed at 100 kV revealed that GERL consisted of cisternal, and fenestrated or tublular portions. The immature granules were attached to GERL by multiple connections to the tublular portions. These results suggest that, in the rat exorbital lacrimal gland, the Golgi saccules participate in the transport of secretory proteins, and that GERL is involved in the formation of secretory granules.

scholarly journals Changes in cell polarity during mitosis in rat parotid acinar cells.

1991 ◽  
Vol 39 (8) ◽  
pp. 1077-1087 ◽  
Author(s):  
H Tamaki ◽  
S Yamashina
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Cell Function ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Surface Polarity ◽  
Drug Induced ◽  
Parotid Acinar Cells

We studied the ultrastructure and cytochemistry of mitotic parotid acinar cells in vivo after induction of mitosis by isoproterenol injection. With entrance of the cells into the division cycle, the Golgi apparatus lost its characteristic stacked structure and internal polarity among the cisternae, appearing as fragments distributed throughout the cytoplasm. These fragments consisted of electron-lucent vesiculotubular structures and electron-dense 70-nm vesicles; neither component showed thiamine pyrophosphatase activity, a marker for trans cisternae of the Golgi apparatus, but the 70-nm vesicles showed a positive reaction for osmium impregnation, indicating retention of the cis nature. The rough endoplasmic reticulum was dilated and fragmented. Recovery of the structure of Golgi apparatus and rearrangement of rough endoplasmic reticulum occurred in daughter cells during telophase. These changes were the same as those observed after drug-induced inhibition of protein transport. The secretory granules were not dispersed but were divided into two groups with which centrioles were closely associated. Both groups migrated with the centrioles as far as the next interphase. The distribution of 5'-nucleotidase on the luminal plasma membrane showed no change during the process of division, thus demonstrating that surface polarity was maintained during mitosis. These changes in organelle structure and distribution may be due to the conversion of cell function from a secretory to a mitotic action.

scholarly journals LOCALIZATION OF PEROXIDASE ACTIVITY IN THE DEVELOPING SUBMANDIBULAR GLAND OF NORMAL AND ISOPROTERENOL-TREATED RATS

1972 ◽  
Vol 20 (11) ◽  
pp. 855-872 ◽  
Author(s):  
SHOHEI YAMASHINA ◽  
TIBOR BARKA
Keyword(s):  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Submandibular Gland ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Chronic Administration ◽  
Secretory Material ◽  
Old Rats ◽  
Tubule Cells

The localization of peroxidase activity was studied in the developing submandibular gland of normal and isoproterenol-treated rats using a diaminobenzidine-H2O2 method. During postnatal development peroxidase activity was localized in the proacinar and acinar cells. The proacinar cells were characterized by the presence of polymorphic secretory granules that gave a strong peroxidase reaction, particularly in the glands of 1-day-old rats. In addition to the secretory granules, enzyme activity was demonstrated in the rough endoplasmic reticulum and nuclear envelope. The terminal tubule cells and duct cells were devoid of peroxidase activity. The secretory granules in the fully developed acinar cells revealed little or no enzyme activity. Isoproterenol stimulated the secretion of the peroxidase-positive granules from the proacinar cells. The stimulation was followed by a reaccumulation of peroxidase-positive secretory material. During this process enzyme activity was demonstrable in the Golgi complex. Isoproterenol had no effect on the terminal tubule cells. A less effective depletion of the secretory granules from the proacinar cells was seen after pilocarpine administration. Chronic administration of isoproterenol to 5-day-old rats led to an acceleration of the differentiation of acinar cells and to a hypertrophy of the gland, without significant change in the localization of peroxidase activity.

Analysis of the Anterior Secretory Cells of Onchidohs Muricata (Nudibranchia)

1981 ◽  
Vol 39 ◽  
pp. 614-615
Author(s):  
Roy Skidmore
Keyword(s):  
Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Golgi Body ◽  
The Body ◽  
Secretory Cells ◽  
Secretory Vesicles ◽  
High Magnification ◽  
Large Numbers ◽  
Membrane Bound ◽  
Sole Of The Foot

The long-necked secretory cells in Onchidoris muricata are distributed in the anterior sole of the foot. These cells are interspersed among ciliated columnar and conical cells as well as short-necked secretory gland cells. The long-necked cells contribute a significant amount of mucoid materials to the slime on which the nudibranch travels. The body of these cells is found in the subepidermal tissues. A long process extends across the basal lamina and in between cells of the epidermis to the surface of the foot. The secretory granules travel along the process and their contents are expelled by exocytosis at the foot surface.The contents of the cell body include the nucleus, some endoplasmic reticulum, and an extensive Golgi body with large numbers of secretory vesicles (Fig. 1). The secretory vesicles are membrane bound and contain a fibrillar matrix. At high magnification the similarity of the contents in the Golgi saccules and the secretory vesicles becomes apparent (Fig. 2).

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).

scholarly journals ULTRASTRUCTURAL VARIATIONS IN N,N'-BIS(4-AMINOPHENYL)-N,N'-DIMETHYLETHYLENEDIAMINE (BED) OXIDASE LOCALIZATION IN RAT LIVER AND PAROTID GLAND WITH VARIATION IN LENGTH OF FIXATION

1972 ◽  
Vol 20 (12) ◽  
pp. 1024-1030 ◽  
Author(s):  
W. ALLEN SHANNON ◽  
ARNOLD M. SELIGMAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Parotid Gland ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Terminal Oxidase ◽  
Outer Compartment ◽  
Fixation Reaction

The localization and reactivity of a terminal oxidase which oxidizes N,N'-bis(4-amino-phenyl)-N,N'-dimethylethylenediamine (BED) were studied in rat liver and parotid gland after varying the concentration of formaldehyde fixative and the length of fixation. Reaction product was observed in mitochondrial outer compartments, smooth elements of rough endoplasmic reticulum, some Golgi lamellae, perinuclear membranes and cytoplasmic membranous structures often associated with mitochondria. A reaction also occurred in the limiting membrane and, to some degree, in the material comprising the secretory granules of the parotid. The reaction in the mitochondrial outer compartment was extremely formaldehyde-sensitive. Controls in which diaminobenzidine (DAB) was substituted for BED showed reaction only in mitochondrial cristae and outer compartments, whereas controls without either reagent showed no reactivity.

Anatomy, Histology, and Ultrastructure of Salivary Glands of the Burrower Bug, Scaptocoris castanea (Hemiptera: Cydnidae)

2019 ◽  
Vol 25 (6) ◽  
pp. 1482-1490 ◽  
Author(s):  
Jamile Fernanda Silva Cossolin ◽  
Luis Carlos Martínez ◽  
Monica Josene Barbosa Pereira ◽  
Lucia Madalena Vivan ◽  
Hakan Bozdoğan ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Salivary Gland ◽  
Salivary Glands ◽  
Rough Endoplasmic Reticulum ◽  
Accessory Gland ◽  
Excretory Duct ◽  
Secretory Cells ◽  
Morphological Description ◽  
Basal Cells ◽  
Narrow Lumen

AbstractThe burrower bug Scaptocoris castanea Perty, 1830 (Hemiptera: Cydnidae) is an agricultural pest feeding on roots of several crops. The histology and ultrastructure of the salivary glands of S. castanea were described. The salivary system has a pair of principal salivary glands and a pair of accessory salivary glands. The principal salivary gland is bilobed with anterior and posterior lobes joined by a hilus where an excretory duct occurs. The accessory salivary gland is tubular with a narrow lumen that opens into the hilus near the excretory duct, suggesting that its secretion is stored in the lumen of the principal gland. The cytoplasm of the secretory cells is rich in the rough endoplasmic reticulum, secretory vesicles with different electron densities and mitochondria. At the base of the accessory gland epithelium, there were scattered cells that do not reach the gland lumen, with the cytoplasm rich in the rough endoplasmic reticulum, indicating a role in protein production. Data show that principal and accessory salivary glands of S. castanea produce proteinaceous saliva. This is the first morphological description of the S. castanea salivary system that is similar to other Hemiptera Pentatomomorpha, but with occurrence of basal cells in the accessory salivary gland.

scholarly journals A COMPARATIVE CYTOCHEMICAL STUDY OF MICROBODIES (PEROXISOMES) IN GREAT ALVEOLAR CELLS OF RODENTS, RABBIT AND MONKEY

1972 ◽  
Vol 20 (3) ◽  
pp. 180-191 ◽  
Author(s):  
EVELINE E. SCHNEEBERGER
Keyword(s):  
Endoplasmic Reticulum ◽  
Peroxidase Activity ◽  
Guinea Pigs ◽  
Smooth Endoplasmic Reticulum ◽  
Alveolar Cells ◽  
Cytochemical Study ◽  
Peroxidatic Activity ◽  
Endogenous Peroxidase ◽  
Light Staining

Lungs from rodents, lagomorphs and primates were briefly fixed in purified glutaraldehyde and incubated with diaminobenzidene and peroxide at pH 7.6 for the demonstration of peroxidase activity and at pH 9.0 for the demonstration of peroxidatic activity of catalase. Great alveolar cells of all animals except the rabbit contained round to elongated microbodies that stained at pH 9.0. In mice, rough and smooth endoplasmic reticulum and the perinuclear cisternae of these cells were also stained. At pH 7.6 there was no staining of great alveolar cells in any species, except in mice, where a light staining of the endoplasmic reticulum, perinuclear cisternae and microbodies persisted. In rodents, microbodies ranged in diameter from 0.13 µ in mice to 0.22 µ in guinea pigs. In monkeys they measured approximately 0.15 µ. Microbodies were not identified with certainty in rabbit great alveolar cells. In rodents the ratio of microbodies to mitochondria was roughly 1:1, whereas in primates it was roughly 1:2. Using appropriate inhibitors it was concluded that staining at pH 9.0 was due to peroxidatic activity of catalase within peroxisomes. Extraperoxisomal staining in mice was attributed to endogenous peroxidase.

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