Effects of intra- and extracellular H+ and Na+ concentrations on Na+-H+ antiport activity in the lacrimal gland acinar cells

1990 ◽  
Vol 417 (4) ◽  
pp. 382-390 ◽  
Author(s):  
Yoshitaka Saito ◽  
Terutaka Ozawa ◽  
Akinori Nishiyama
Keyword(s):  
Lacrimal Gland ◽  
Acinar Cells

scholarly journals Identification and Functional Distribution of Intracellular Ca2+ Channels in Mouse Lacrimal Gland Acinar Cells

2007 ◽  
Vol 1 (1) ◽  
pp. 8-16 ◽  
Author(s):  
P. Koulen ◽  
W. E. Medina-Ortiz ◽  
E. V. Gregg ◽  
A. M. Brun-Zinkernagel
Keyword(s):  
Lacrimal Gland ◽  
Acinar Cells ◽  
Functional Distribution ◽  
Ca2 Channels

scholarly journals Hormonal Regulation of the Dry Eye.

2020 ◽  
pp. 1-3
Keyword(s):  
Estrogen Receptors ◽  
Dry Eye ◽  
Lacrimal Gland ◽  
Hormonal Regulation ◽  
Acinar Cells ◽  
Young Males ◽  
Physiological Conditions ◽  
Clear Vision ◽  
Menopausal Women ◽  
Males And Females

Abstract For protection of environmental insults and clear vision the outer most surface (the cornea) of the human eye has to be kept moist with the secretion of the lacrimal gland. During old age (in both the genders) and certain physiological conditions (in females) the pathophysiological conditions of lacrimal gland alter which results in Dry/Wet eye. Most of the menopausal women and young males and females face dry eye disorder due to environmental insults and therefore, we hypothesize that the acinar cells of lacrimal gland should have estrogen receptors. In support of this earlier we have localized estrogen receptors on eye lens epithelial cells that also regulated by sex steroid hormones.

Adenosine Receptor Signalling in the Rabbit Lacrimal Gland Acinar Cells is Ca2+ Dependent

2005 ◽  
Vol 3 ◽  
pp. S60
Author(s):  
Maria C. Edman ◽  
Sofia V. Andersson ◽  
Dick Delbro ◽  
J. Peter Gierow
Keyword(s):  
Lacrimal Gland ◽  
Adenosine Receptor ◽  
Acinar Cells ◽  
Receptor Signalling

Fluid phase endocytosis by isolated rabbit lacrimal gland acinar cells

1995 ◽  
Vol 60 (5) ◽  
pp. 511-525 ◽  
Author(s):  
J. Peter Gierow ◽  
Robert W. Lambert ◽  
Austin K. Mircheff
Keyword(s):  
Lacrimal Gland ◽  
Acinar Cells ◽  
Fluid Phase ◽  
Fluid Phase Endocytosis

M3 muscarinic acetylcholine receptor coupling to PLC in rat exorbital lacrimal acinar cells

1993 ◽  
Vol 264 (6) ◽  
pp. C1550-C1560 ◽  
Author(s):  
P. Mauduit ◽  
H. Jammes ◽  
B. Rossignol
Keyword(s):  
Acetylcholine Receptor ◽  
Lacrimal Gland ◽  
Inositol Phosphate ◽  
Muscarinic Acetylcholine Receptor ◽  
Acinar Cells ◽  
Muscarinic Agonist ◽  
Homogeneous Population ◽  
Muscarinic Antagonist ◽  
Muscarinic Acetylcholine ◽  
High Affinity

This study was designed to characterize the muscarinic acetylcholine receptor (mAChR) subtype present in rat exorbital lacrimal gland as well as its biochemical coupling. The nonselective muscarinic antagonist [N-methyl-3H]scopolamine ([3H]NMS) binds with high affinity to a homogeneous population of binding sites in both membranes [dissociation constant (Kd) = 82.3 +/- 3.2 pM] and acinar cell (Kd = 170.3 +/- 20 pM) preparations. Muscarinic antagonist inhibition of [3H]NMS binding is homogeneous with the following order of potency: atropine > or = 4-diphenylacetoxy-N-methylpiperidine (4-DAMP) > pirenzepine > 11-([2-(diethylamino)-ethyl]-1-piperidinyl)-acetyl- 5,11-dihydro-6H-pirido[2,3-b]1,4,benzo diazepine-6-one (AFDX 116). Both the affinity of the selective antagonists 4-DAMP, pirenzepine, and AFDX 116 and Northern blot analysis of lacrimal gland mRNAs show a single mAChR population of the M3 subtype. Muscarinic agonist inhibition of [3H]NMS binding displays both high (approximately 20%)- and low-affinity sites (approximately 80%). Both the receptor occupancy and the stimulation by agonists or the inhibition by antagonists of the accumulation of [3H]inositol phosphate were examined under identical conditions with respect to tissue preparations (acinar cells) and buffer (Krebs-Ringer). Results demonstrate 1) the efficient coupling of the M3 mAChR subtype with the phosphatidylinositol (4,5))bisphosphate-specific phospholipase C activity and 2) that the efficacy of a muscarinic agonist is dependent on its structure. Lastly, comparison of the agonists affinity and potency to trigger the [3H]inositol phosphate accumulation suggests that the occupation of the high-affinity agonist binding state of the M3 mAChR was involved in the cellular response.

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.

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