scholarly journals Enzyme modulation of the Golgi apparatus and GERL: a cytochemical study of parotid acinar cells.

1983 ◽  
Vol 31 (8) ◽  
pp. 1041-1048 ◽  
Author(s):  
C Oliver ◽  
A R Hand
Keyword(s):  
Enzyme Activity ◽  
Secretory Granule ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Enzyme Localization ◽  
Cytochemical Study ◽  
Postnatal Maturation ◽  
Parotid Acinar Cells ◽  
Enzyme Modulation ◽  
Thiamine Pyrophosphatase

The distribution of thiamine pyrophosphatase (TPPase) and acid phosphatase (AcPase) has been examined in resting parotid acinar cells as well as during decreased and increased secretory granule production. In resting acinar cells, TPPase activity was restricted to the trans Golgi saccules and AcPase activity was localized in GERL and immature secretory granules. Although secretory granule production is diminished during ethionine intoxication, no significant alteration in the distribution of either TPPase or AcPase was noted. However, marked changes in enzyme localization, especially of TPPase, occurred during accelerated secretory granule production. The alterations were essentially the same for all of the conditions studied (recovery from ethionine treatment, recovery from a protein depletion diet, secretory stimulation with isoproterenol, and postnatal maturation of the parotid gland). During maximal secretory granule production, TPPase activity was localized not only in the trans Golgi saccules, but also in GERL-like cisternae and immature secretory granules. The immature secretory granules were often in continuity with the GERL-like cisternae. At the same time that the TPPase activity was increased, the AcPase activity was frequently diminished. These modulations in enzyme activity provide evidence that GERL is derived from the trans Golgi saccule.

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 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 Monoclonal antibody to a common antigen of secretory granule membranes: intracellular localization and recycling of the antigen after secretion.

1992 ◽  
Vol 40 (6) ◽  
pp. 793-806 ◽  
Author(s):  
S Yamashita ◽  
K Yasuda
Keyword(s):  
Monoclonal Antibody ◽  
Secretory Granule ◽  
Secretory Granules ◽  
Intracellular Localization ◽  
Acinar Cells ◽  
Membrane Glycoproteins ◽  
Molecular Weights ◽  
Parotid Acinar Cells ◽  
Granule Membrane ◽  
Immunohistochemical Studies

Monoclonal antibody (MAb) 170-5 was generated to the secretory granule membrane of rat parotid acinar cells. The MAb recognized integral membrane glycoproteins (SG 170 antigen) localized on the luminal side of the secretory granules with N-linked carbohydrates, molecular weights 92, 84, 76, 69, and 65 KD. Immunohistochemical studies indicated that the SG 170 antigen was found in the secretory granules of both exocrine and endocrine cells and in the lysosomes of various cells in the rat. Immunoelectron microscopy with immunogold revealed that the antigen was present on the membrane of the secretory granules, lysosomes, the Golgi vesicles, and condensing vacuoles in pancreatic and parotid acinar cells and in AR42J rat pancreatic tumor cells; the Golgi stacks exhibited no immunoreaction. The common localization of the antigen in the secretory granule membranes indicated that this antigen may play an essential role in regulated secretion. Employing HRP-labeled MAb 170-5, we followed the retrieval of the antigen after exocytosis in AR42J cells. The MAb was internalized specifically with antigen-mediated endocytosis. It was transported to endosomes, subsequently to the trans-Golgi network, and then packaged into secretory granules. However, the Golgi stacks revealed no uptake of the labeled antibody.

A primary culture of parotid acinar cells retaining capacity for agonists-induced amylase secretion and generation of new secretory granules

2005 ◽  
Vol 320 (3) ◽  
pp. 455-464 ◽  
Author(s):  
Junko Fujita-Yoshigaki ◽  
Asako Tagashira ◽  
Tomoyoshi Yoshigaki ◽  
Shunsuke Furuyama ◽  
Hiroshi Sugiya
Keyword(s):  
Primary Culture ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Amylase Secretion ◽  
Parotid Acinar Cells

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 Uptake and fate of luminally administered horseradish peroxidase in resting and isoproterenol-stimulated rat parotid acinar cells.

1978 ◽  
Vol 76 (1) ◽  
pp. 207-229 ◽  
Author(s):  
C Oliver ◽  
A R Hand
Keyword(s):  
Horseradish Peroxidase ◽  
Secretory Granule ◽  
Extracellular Fluid ◽  
Acinar Cells ◽  
Granule Formation ◽  
Parotid Acinar Cells ◽  
Junctional Complexes ◽  
Rat Parotid ◽  
Endocytic Vesicles ◽  
Gain Access

The formation and fate of apical endocytic vesicles in resting and isoproterenol-stimulated rat parotid acinar cells were studied using luminally administered horseradish peroxidase (HRP) to mark the vesicles. The tracer was taken up from the lumen by endocytosis in small, smooth-surfaces "c"- or ring-shaped vesicles. About 1 h after HRP administration the vesicles could be found adjacent to the Golgi apparatus. At later times HRP reaction product was localized in multivesicular bodies and lysosomes; in isoproterenol-stimulated cells it was also present in autophagic vacuoles. HRP reaction product was never localized in any structure associated with secretory granule formation. These results suggest that the apical endocytic vesicles play a role in membrane recovery, but that they are degraded and not reutilized directly in secretory granule formation. Additionally, it was found that when isoproterenol was injected before HRP administration, the apical junctional complexes became permeable to the tracer, allowing it to gain access to the lateral and basal intercellular spaces. This permeability may provide an additional route whereby substances in the extracellular fluid could reach the saliva.

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.

Secretory proteins without a transport signal are retained in secretory granules during maturation in rat parotid acinar cells

2015 ◽  
Vol 60 (4) ◽  
pp. 642-649 ◽  
Author(s):  
Osamu Katsumata-Kato ◽  
Megumi Yokoyama ◽  
Miwako Matsuki-Fukushima ◽  
Takanori Narita ◽  
Hiroshi Sugiya ◽  
...  
Keyword(s):  
Secretory Granules ◽  
Acinar Cells ◽  
Secretory Proteins ◽  
Parotid Acinar Cells ◽  
Rat Parotid

Isoprenaline-induced and constitutive members of a proline-rich protein sub-group from mouse parotid glands studied with monoclonal antibody NAL1

1989 ◽  
Vol 3 (1) ◽  
pp. 7-14 ◽  
Author(s):  
N. Divecha ◽  
H. Mansouri ◽  
D. Peat ◽  
G. Cope ◽  
L. Partridge ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Secretory Granules ◽  
Acinar Cells ◽  
Enzyme Linked Immunosorbent Assay ◽  
Parotid Glands ◽  
Parotid Acinar Cells ◽  
The Family ◽  
Before And After ◽  
Proline Rich Protein

ABSTRACT Members of the proline-rich protein (PRP) family of mouse parotid glands were analysed before and after stimulation with the β-agonist isoprenaline by using a monoclonal antibody raised against the induced PRP A30 (GP-27). Antibody NAL1 reacted strongly with isoprenaline-induced B-type PRP precursors and their salivary counterparts, but not against the A-type PRPs A10 (Gp-66) and A20 (GP-45) or human salivary proteins, and it is likely that NAL1 recognizes a proline-rich repeat variant unique to this group of rodent PRPs. PRP-related antigens were observed in the parotid glands (N10 and N20) and saliva of normal mice. The antigens were located immunocytochemically in secretory granules of parotid acinar cells of both normal and isoprenaline-stimulated mice. The total amount of PRP antigens increased 16-fold from 2·5 to 40% of parotid protein after 10 days of isoprenaline treatment, as estimated by enzyme-linked immunosorbent assay. Immunoblotting showed that new PRP species appeared during the period of increase. After treatment with isoprenaline, B-type PRPs appeared first, followed by A30 and another member of the family. These results show that the mouse PRP family is larger than previously thought and can be divided immunologically into sub-groups. That a subset of PRPs are produced in the normal mouse indicates that there is differential β-adrenergic regulation within the family, and also has implications for the role of PRPs in the normal maintenance of healthy dentition and other processes.

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