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 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 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 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.

Ultrastructure of the Genital Duct Epithelium of the Male Port Jackson Shark, Heterodontus-Portusjacksoni

1992 ◽  
Vol 40 (3) ◽  
pp. 257 ◽  
Author(s):  
RC Jones ◽  
M Lin
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Close Association ◽  
Ciliated Cells ◽  
Dense Bodies ◽  
Ductuli Efferentes ◽  
Apical Vesicles

The genital ducts of Heterodontus portusjacksoni are lined by a ciliated epithelium. In the ductuli efferentes the epithelium is low and contains numerous intraepithelial leucocytes which often contain large dense bodies. All epithelial cells are ciliated and are characterised by apical vesicles, vacuoles and glycogen granules, some rough endoplasmic reticulum, dense bodies and lipid droplets, and a Golgi apparatus. The initial segment of the ductus epididymidis is lined by a very tall epithelium of ciliated and non-ciliated cells. The non-ciliated cells contain numerous apical vesicles, a large Golgi apparatus and numerous mitochondria and secretory granules in close association with an extensive endoplasmic reticulum. The terminal segment of the ductus epididymidis is lined by a low columnar epithelium. A proximal region, occupying part of the head of the epididymis, is similar to the epithelium in the ductuli efferentes. Distally, all the epithelial cells are ciliated. They are characterised by considerable dilated endoplasmic reticulum, a Golgi apparatus, apical vesicles, and numerous mitochondria and secretory granules. The secretory tubules of Leydig's glands are lined by a very tall epithelium with non-ciliated cells containing extensive, dilated, rough endoplasmic reticulum, a large Golgi apparatus, and numerous mitochondria and secretory granules. The significance of the structural differentiation of the duct is discussed in relation to the evolution of the mammalian epididymis.

scholarly journals Ultrastructure of mononuclear phagocytes developing in liquid bone marrow cultures. A study on peroxidatic activity

1979 ◽  
Vol 149 (1) ◽  
pp. 17-26 ◽  
Author(s):  
JWM Van Der Meer ◽  
RHJ Beelen ◽  
DM Fluitsma ◽  
R Van Furth
Keyword(s):  
Bone Marrow ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Nuclear Envelope ◽  
Rough Endoplasmic Reticulum ◽  
Precursor Cells ◽  
Mononuclear Phagocytes ◽  
Peroxidatic Activity

Monoblasts, promonocytes, and macrophages in in vitro cultures of murine bone marrow were studied ultrastructurally, with special attention to peroxidatic activity. Monoblasts show peroxidatic activity in the rough endoplasmic reticulum and nuclear envelope as well as in the granules. The presence of peroxidatic activity in the Golgi apparatus could not be determined. Promonocytes have peroxidase-positive rough endoplasmic reticulum, Golgi apparatus, nuclear envelope, and granules, as previously reported. During culture, cells are formed with peroxidatic activity similar to that of monocytes or exudate macrophages (positive granules; negative Golgi apparatus, RER, and nuclear envelope); we call these cells early macrophages. In addition, transitional macrophages with both positive granules and positive RER, nuclear envelope, negative Golgi apparatus (as in exudate- resident macrophages in vivo), and mature macrophages with peroxidatic activity only in the RER and nuclear envelope (as in resident macrophages in vivo) were found. A considerable number of cells without detectable peroxidatic activity were also encountered. Our finding that macrophages with the peroxidatic pattern of monocytes (early macrophages), exudate-resident macrophages (transitional macrophages), and resident macrophages (mature macrophages), develop in vitro from proliferating precursor cells deriving from the bone marrow, demonstrates once again that resident macrophages in tissues originate from precursor cells in the bone marrow. Therefore, this conclusion can no longer be challenged on the basis of a cytochemical difference between monocytes and exudate macrophages on the one hand and resident macrophages on the other.

scholarly journals IN VIVO INCORPORATION OF 3H-GALACTOSE BY THYROID FOLLICULAR CELLS OF THE RAT, AS SHOWN BY ELECTRON MICROSCOPIC RADIOAUTOGRAPHY

1972 ◽  
Vol 20 (3) ◽  
pp. 220-224 ◽  
Author(s):  
A. HADDAD
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Side Chains ◽  
Follicular Cells ◽  
Electron Microscopic ◽  
Thyroid Follicular Cells ◽  
Apical Vesicles ◽  
Electron Microscopic Radioautography

Radioactive galactose was injected intravenously into rats and localized in thyroid follicular cells by electron microscopic radioautography at intervals ranging from 2.5 to 30 min after injection. The galactose label was mostly present in the Golgi apparatus at 2.5 min, with some of it in the adjacent rough endoplasmic reticulum. By 30 min, the label was found in apical vesicles and colloid. It was concluded that galactose is added to the carbohydrate side chains of incomplete thyroglobulin molecules during their travel through the cisternae of the endoplasmic reticulum into the Golgi apparatus; the uptake begins as this organelle is approached, but predominates within it. The thyroglobulin molecule which has thus been labeled is transported by the apical vesicles to the colloid.

Subdomains of the rough endoplasmic reticulum in colon goblet cells of the rat: lectin-cytochemical characterization.

1992 ◽  
Vol 40 (7) ◽  
pp. 919-930 ◽  
Author(s):  
A Ellinger ◽  
M Pavelka
Keyword(s):  
Endoplasmic Reticulum ◽  
Sialic Acid ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Ricinus Communis ◽  
Secretory Granules ◽  
Lectin Binding ◽  
Helix Pomatia ◽  
Goblet Cells ◽  
Rat Colon

Using lectin binding, we characterized subdomains of the rough endoplasmic reticulum (rER) in goblet cells of the rat colon. In this cell type, special rER regions can be differentiated on the basis of their content of low electron density and dilated cisternal spaces in conventional transmission electron microscopic preparations. The fine fibrillar content of these cisternal regions demonstrated high-affinity binding with lectins from wheat germ, Helix pomatia, Griffonia simplicifolia I-A4 and -B4, and Ricinus communis I, although not with the sialic acid-specific Limax flavus lectin and the fucose-binding Ulex europaeus I lectin. Sugar-inhibitory experiments indicated that glycoconjugates packed within these regions bound the lectins with higher affinity than molecules present in the Golgi apparatus and secretory granules. Furthermore, the lectin binding patterns of the rER subdomains differed from those of the Golgi apparatus and mucin granules: the terminal sugar residues sialic acid and fucose were demonstrable in the Golgi apparatus and mucin granules and were absent from the rER, while galactose-recognizing lectins bound intensely at these rER regions, weakly to Golgi elements, and were almost absent from mucin granules.

Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60 and hsp70 in distinct compartments along the secretory pathway of the acinar cells

1994 ◽  
Vol 107 (3) ◽  
pp. 539-549 ◽  
Author(s):  
C.S. Velez-Granell ◽  
A.E. Arias ◽  
J.A. Torres-Ruiz ◽  
M. Bendayan
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Secretory Pathway ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Pancreatic Tissue ◽  
Secretory Proteins ◽  
Trans Golgi Network ◽  
Hsp70 Protein ◽  
Golgi Network

Three chaperones, the chaperonins cpn10 and cpn60, and the hsp70 protein, were revealed by immunochemistry and cytochemistry in pancreatic rat acinar cells. Western immunoblotting analysis of rat pancreas homogenates has shown that antibodies against cpn10, cpn60 and hsp70 protein recognize single protein bands of 25 kDa, 60 kDa and 70 kDa, respectively. Single bands for the cpn10 and cpn60 were also detected in pancreatic juice. Immunofluorescence studies on rat pancreatic tissue revealed a strong positive signal in the apical region of the acinar cells for cpn10 and cpn60, while an immunoreaction was detected at the juxtanuclear Golgi region with the anti-hsp70 antibody. Immunocytochemical gold labeling confirmed the presence of these three chaperones in distinct cell compartments of pancreatic acinar cells. Chaperonin 10 and cpn60 were located in the endoplasmic reticulum, Golgi apparatus, condensing vacuoles and secretory granules. Interestingly, the labeling for both cpn10 and cpn60 followed the increasing concentration gradient of secretory proteins along the RER-Golgi-granule secretory pathway. On the contrary, the labeling for hsp70 was mainly concentrated in the endoplasmic reticulum and the Golgi apparatus. In the latter, the hsp70 was found to be primary located in the trans-most cisternae and to colocalize with acid phosphatase in the trans-Golgi network. The three chaperones were also present in mitochondria. In view of the role played by the chaperones in the proper folding, sorting and aggregation of proteins, we postulate that hsp70 assists the adequate sorting and packaging of proteins from the ER to the trans-Golgi network while cpn10 and cpn60 play key roles in the proper packaging and aggregation of secretory proteins as well as, most probably, in the prevention of early enzyme activation in secretory granules.

scholarly journals The Golgi apparatus and GERL during postnatal differentiation of rat parotid acinar cells: an electron microscopic cytochemical study.

1984 ◽  
Vol 32 (5) ◽  
pp. 477-485 ◽  
Author(s):  
A I Doine ◽  
C Oliver ◽  
A R Hand
Keyword(s):  
Young Adult ◽  
Golgi Apparatus ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Sprague Dawley ◽  
Electron Microscopic ◽  
Cytochemical Study ◽  
Parotid Acinar Cells ◽  
Postnatal Differentiation ◽  
Rat Parotid

Morphological and cytochemical changes in the Golgi apparatus and GERL of differentiating parotid acinar cells were examined in Sprague-Dawley rats from 5 days to young adult. At day 5, the Golgi apparatus consisted of 3-6 narrow saccules, with short segments of GERL lying adjacent to the trans Golgi saccule. As the glands matured, the Golgi apparatus increased in size and the saccules became broadened and fenestrated reaching a maximum from days 15-20. The saccules subsequently narrowed slightly and by day 25 resembled those seen in young adults. Numerous cisternae of GERL could be seen at the trans face during this period. While the glands were maturing, marked changes occurred in the distribution of thiamine pyrophosphatase (TPPase) activity in the Golgi saccules. In the immature cells, TPPase activity was restricted to 1 or 2 trans Golgi saccules. However, by day 10 TPPase could also be localized in immature secretory granules and in GERL-like cisternae. Unreactive segments of GERL were also present. This pattern of localization persisted until day 20, after which the TPPase activity in the GERL-like cisternae diminished gradually until by day 40 TPPase again was localized in 1-2 trans Golgi saccules and an occasional immature secretory granule. Acid phosphatase (AcPase) activity was localized primarily in lysosomes in the very young animals and increased in GERL with age up to day 15. From days 15 to 20 there was a decrease in the amount of activity seen in GERL, but from day 20 on, the AcPase activity increased until it reached that seen in young adult animals. These results indicate that the presence of TPPase activity in GERL-like cisternae and immature secretory granules may be dependent upon the developmental as well as the physiologic state of the acinar cells and lend further support to the suggestion that GERL is derived from the trans Golgi saccules.

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.

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