| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Department of Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles 90089-9121; and 2 Department of Molecular and Cell Biology, 3 Lawrence Berkeley Laboratory, and 4 Electron Microscope Lab, University of California, Berkeley, California 94720
Clathrin from
H-K-ATPase-rich membranes derived from the tubulovesicular compartment
of rabbit and hog gastric acid secretory (parietal) cells was
characterized biochemically, and the subcellular localization of
membrane-associated clathrin in parietal cells was characterized
by immunofluorescence, electron microscopy, and immunoelectron
microscopy. Clathrin from H-K- ATPase-rich membranes was determined
to be comprised of conventional clathrin heavy chain and a predominance
of clathrin light chain A. Clathrin and adaptors could be induced to
polymerize quantitatively in vitro, forming 120-nm-diameter basketlike
structures. In digitonin-permeabilized resting parietal cells, the
intracellular distribution of immunofluorescently labeled clathrin was
suggestive of labeling of the tubulovesicular compartment. Clathrin was
also unexpectedly localized to canalicular (apical) membranes, as were
-adaptin and dynamin, suggesting that this membrane domain of
resting parietal cells is endocytotically active. At the
ultrastructural level, clathrin was immunolocalized to canalicular
and tubulovesicular membranes. H-K-ATPase was immunolocalized to
the same membrane domains as clathrin but did not appear to be enriched
at the specific subdomains that were enriched in clathrin. Finally, in
immunofluorescently labeled primary cultures of parietal cells, in
contrast to the H-K-ATPase, intracellular clathrin was found not to
translocate to the apical membrane on secretagogue stimulation. Taken
together, these biochemical and morphological data provide a framework
for characterizing the role of clathrin in the regulation of membrane
trafficking from tubulovesicles and at the canalicular membrane in
parietal cells.
hydrogen-potassium-adenosinetriphosphatase; apical membrane recycling; tubulovesicles; dynamin; gastric microsomes
This article has been cited by other articles:
|
|
 |
|
  C. S. Chew, X. Chen, R. J. Bollag, C. Isales, K. H. Ding, and H. Zhang Targeted disruption of the Lasp-1 gene is linked to increases in histamine-stimulated gastric HCl secretion Am J Physiol Gastrointest Liver Physiol, July 1, 2008; 295(1): G37 - G44. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. A. Lapierre, K. M. Avant, C. M. Caldwell, A.-J. L. Ham, S. Hill, J. A. Williams, A. J. Smolka, and J. R. Goldenring Characterization of immunoisolated human gastric parietal cells tubulovesicles: identification of regulators of apical recycling Am J Physiol Gastrointest Liver Physiol, May 1, 2007; 292(5): G1249 - G1262. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Zanner, M. Gratzl, and C. Prinz Expression of the endocytic proteins dynamin and amphiphysin in rat gastric enterochromaffin-like cells J. Cell Sci., May 1, 2004; 117(11): 2369 - 2376. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. G. Duman, N. J. Pathak, M. S. Ladinsky, K. L. McDonald, and J. G. Forte Three-dimensional reconstruction of cytoplasmic membrane networks in parietal cells J. Cell Sci., March 15, 2002; 115(6): 1251 - 1258. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. M. Sherry, D. H. Malinowska, R. E. Morris, G. M. Ciraolo, and J. Cuppoletti Localization of ClC-2 Cl{-} channels in rabbit gastric mucosa Am J Physiol Cell Physiol, June 1, 2001; 280(6): C1599 - C1606. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |
