Identification of G-proteins in rat parotid gland plasma membranes and granule membranes: presence of distinct components in granule membranes

1992 ◽  
Vol 115 (2) ◽  
Author(s):  
Nawab Ali ◽  
DevendraK. Agrawal ◽  
Peter Cheung
Keyword(s):  
Parotid Gland ◽  
G Proteins ◽  
Plasma Membranes ◽  
Rat Parotid Gland ◽  
Rat Parotid

Ca2+-independent phospholipase A2 activity in apical plasma membranes from the rat parotid gland

2001 ◽  
Vol 46 (9) ◽  
pp. 789-799 ◽  
Author(s):  
Masako Mizuno-Kamiya ◽  
Hiroshi Inokuchi ◽  
Yasunaga Kameyama ◽  
Koji Yashiro ◽  
Atsushi Fujita
Keyword(s):  
Parotid Gland ◽  
Phospholipase A2 ◽  
Plasma Membranes ◽  
Rat Parotid Gland ◽  
Rat Parotid ◽  
Phospholipase A2 Activity

Kinetic analysis of rat parotid gland muscarinic receptors in vivo: comparison with brain and heart

1993 ◽  
Vol 264 (3) ◽  
pp. G541-G552
Author(s):  
Y. Hiramatsu ◽  
R. Kawai ◽  
R. C. Reba ◽  
T. R. Simon ◽  
B. J. Baum ◽  
...  
Keyword(s):  
Parotid Gland ◽  
Plasma Membranes ◽  
Specific Binding ◽  
Muscarinic Acetylcholine Receptor ◽  
Binding Potential ◽  
Specific Binding Sites ◽  
Rat Parotid Gland ◽  
Rat Parotid

(RR)- and (SS)-quinuclidinyl iodobenzilate enantiomers [(RR)- and (SS)-IQNB, active and inert, respectively] have been synthesized for quantitative evaluation of muscarinic acetylcholine receptor (mAChR) binding. Pharmacokinetic approaches have not been used previously to assess in vivo IQNB binding in nonexcitable tissues. We have applied this method to examine mAChRs in rat parotid gland in comparison to those in brain and heart. Short-term infusion studies in vivo showed that the "instantaneous" reversible binding of (RR)- and (SS)-IQNB was high in the parotid (greater nonspecific binding potential), intermediate in the heart, and lowest in cortex and cerebellum. Long-term bolus injection experiments showed that the parotid gland mAChRs possessed a binding potential for receptor specific sites (380), which was intermediate between that of parietal cortex (930) and cerebellum (10) and greater than that of heart (165). In vitro binding to plasma membranes was generally consistent with the in vivo findings. In aggregate, these studies show that mAChRs can be evaluated in vivo in a nonexcitable tissue with the use of stereospecific ligands and a pharmacokinetic approach. The data suggest that IQNB, a mAChR antagonist, can identify characteristics of specific binding sites, which may reflect tissue differences.

Localization of a low Mr GTP-binding protein, rap1 protein, in plasma membranes and secretory granule membranes of rat parotid gland

Life Sciences ◽  
1994 ◽  
Vol 55 (3) ◽  
pp. 213-219 ◽  
Author(s):  
Yasunaga Kameyama ◽  
Koh-ichi Nagata ◽  
Masako Mizuno-Kamiya ◽  
Yutaka Yokota ◽  
Atsushi Fujita ◽  
...  
Keyword(s):  
Parotid Gland ◽  
Secretory Granule ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Rat Parotid Gland ◽  
Rat Parotid

scholarly journals Study of G-proteins and phospholipase C in rat parotid gland membranes

1995 ◽  
Vol 67 ◽  
pp. 77
Author(s):  
Kohei Sawaki ◽  
Indu S. Ambudkar ◽  
Bruce J Baum ◽  
Mitsuru Kawaguchi
Keyword(s):  
Parotid Gland ◽  
Phospholipase C ◽  
G Proteins ◽  
Rat Parotid Gland ◽  
Rat Parotid

scholarly journals Quantitative immunoelectron microscopic localization of (Na+,K+)ATPase in rat parotid gland.

1987 ◽  
Vol 35 (8) ◽  
pp. 871-879 ◽  
Author(s):  
T Iwano ◽  
M Akayama ◽  
A Yamamoto ◽  
K Omori ◽  
T Kumazawa ◽  
...  
Keyword(s):  
Parotid Gland ◽  
Plasma Membranes ◽  
Basolateral Membrane ◽  
Protein A ◽  
Acinar Cells ◽  
Gold Particles ◽  
Duct Cells ◽  
Rat Parotid Gland ◽  
Basal Plasma ◽  
Rat Parotid

Distribution of (Na+,K+)ATPase on the cell membranes of acinar and duct cells of rat parotid gland was investigated quantitatively by immunoelectron microscopy using the post-embedding protein A-gold technique. In acinar cells, ATPase was localized predominantly on the basolateral plasma membranes. A small but significant amount of (Na+,K+)ATPase was, however, detected on the luminal plasma membranes, especially on the microvillar region of the acinar cells; the surface density on the luminal membrane was approximately one third of that on the basolateral membranes. In duct cells, many gold particles were found on the basolateral membrane, especially along the basal infoldings of the plasma membranes, whereas no significant gold particles were found on the luminal plasma membranes, suggesting unilateral distribution of ATPase in duct cells. We suggest that in acinar cells sodium ion is not only transported paracellularly but is also actively transported intracellularly into the luminal space by the (Na+,K+)ATPase located on the luminal plasma membranes, and that water is passively transported to the luminal space to form a plasma-like isotonic primary saliva, while in the duct cells the same ion is selectively re-absorbed intracellularly by (Na+,K+)ATPase found in abundance along the many infoldings of the basal plasma membranes, thus producing the hypotonic saliva.

scholarly journals Plasma membrane of the rat parotid gland: preparation and partial characterization of a fraction containing the secretory surface.

1982 ◽  
Vol 95 (1) ◽  
pp. 8-19 ◽  
Author(s):  
P Arvan ◽  
J D Castle
Keyword(s):  
Plasma Membrane ◽  
Parotid Gland ◽  
Membrane Fraction ◽  
Adenosine Triphosphatase ◽  
Plasma Membranes ◽  
Junctional Complex ◽  
Salivary Gland Cell ◽  
Plasma Membrane Fraction ◽  
Rat Parotid Gland ◽  
Rat Parotid

A plasma membrane fraction from the rat parotid gland has been prepared by a procedure which selectively enriches for large membrane sheets. This fraction appears to have preserved several ultrastructural features of the acinar cell surface observed in situ. Regions of membrane resembling the acinar luminal border appear as compartments containing microvillar invaginations, bounded by elements of the junctional complex, and from which basolateral membranes extend beyond the junctional complex either to contact other apical compartments or to terminate as free ends. Several additional morphological features of the apical compartments suggest that they are primarily derived from the surface of acinar cells, rather than from the minority of other salivary gland cell types. Enzymatic activities characteristically associated with other cellular organelles are found at only low levels in the plasma membrane fraction. The fraction is highly enriched in two enzyme activities--K+ -dependent p-nitrophenyl phosphatase (K+ -NPPase, shown to be Na+/K+ adenosine triphosphatase; 20-fold) and gamma-glutamyl transpeptidase (GGTPase; 26-fold)--both known to mark plasma membranes in other tissues. These activities exhibit different patterns of recovery during fractionation, suggesting their distinct distributions among parotid cellular membranes. Secretion granule membranes also exhibit GGTPase, but no detectable K+ -NPPase. Since Na+/K+ adenosine triphosphatase and GGTPase, respectively, mark the basolateral and apical cellular surfaces in other epithelia, we hypothesize that these two enzymes mark distinct domains in the parotid plasmalemma, and that GGTPase, as the putative apical marker, may signify a compositional overlap between the two types of membranes which fuse during exocytosis.

scholarly journals Functional Regulation of Protein Synthesis in the Rat Parotid Gland

1971 ◽  
Vol 246 (12) ◽  
pp. 3879-3884 ◽  
Author(s):  
Leo M. Sreebny ◽  
Dorthea A. Johnson ◽  
Murray R. Robinovitch
Keyword(s):  
Protein Synthesis ◽  
Parotid Gland ◽  
Rat Parotid Gland ◽  
Functional Regulation ◽  
Rat Parotid
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