Basement Membrane Modulation of Stimulated Secretion by Lacrimal Acinar Cells

1994 ◽  
pp. 37-44
Author(s):  
Gordon W. Laurie ◽  
J. Douglas Glass ◽  
Rebecca A. Ogle
Keyword(s):  
Basement Membrane ◽  
Acinar Cells ◽  
Lacrimal Acinar Cells

"BM180": a novel basement membrane protein with a role in stimulus-secretion coupling by lacrimal acinar cells

1996 ◽  
Vol 270 (6) ◽  
pp. C1743-C1750 ◽  
Author(s):  
G. W. Laurie ◽  
J. D. Glass ◽  
R. A. Ogle ◽  
C. M. Stone ◽  
J. R. Sluss ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Membrane Protein ◽  
Acinar Cells ◽  
Basement Membranes ◽  
Enzyme Linked Immunosorbent Assay ◽  
Regulated Secretion ◽  
Basement Membrane Protein ◽  
Stimulus Secretion Coupling ◽  
Lacrimal Acinar Cells ◽  
Laminin 1

Regulated secretion requires the developmental coupling of neuronal or hormonal stimuli to an exocytotic response, a multistep pathway whose appearance may be linked with cellular adhesion to the newly formed exocrine cell basement membrane. We screened for adhesion-associated coupling activity using lacrimal acinar cells and have identified “BM180”, a novel basement membrane protein enriched in guanidine HCl extracts of lacrimal and parotid exocrine secretory glands. BM180 resides primarily in a previously inexamined lower molecular-mass basement membrane peak (peak 2) that contains cell adhesion activity inhibitable with the anti-BM180 monoclonal antibody 3E12. Removal of peak 2 by gel filtration or preincubation of basement membrane with 3E12 decreased regulated peroxidase secretion by one-half without affecting constitutive secretion or the amount of cellular peroxidase available for release. Adding back peak 2 restored regulated secretion in a dose-dependent and 3E12-inhibitable manner and suggested a synergistic relationship between BM180 and laminin 1. BM180 has a mobility of 180 and 60 kDa in the absence or presence of dithiothreitol, respectively, and shows no immunological identity by competitive enzyme-linked immunosorbent assay with laminin 1, collagen IV, entactin, fibronectin, BM-40, perlecan, or vitronectin. We propose that BM180 is an important resident of certain glandular basement membranes where it interacts with the cell surface, thereby possibly signaling the appearance of a transducing element in the stimulus-secretion coupling pathway.

Role of laminin-1, collagen IV, and an autocrine factor(s) in regulated secretion by lacrimal acinar cells

1998 ◽  
Vol 275 (1) ◽  
pp. C278-C284 ◽  
Author(s):  
Lanlin Chen ◽  
J. Douglas Glass ◽  
Staci C. Walton ◽  
Gordon W. Laurie
Keyword(s):  
Basement Membrane ◽  
Acinar Cells ◽  
Collagen Iv ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Regulated Secretion ◽  
Stimulus Secretion Coupling ◽  
Lacrimal Acinar Cells ◽  
Laminin 1

Adhesion to novel basement membrane component BM180 in the presence of laminin-1 promotes stimulus-secretion coupling in lacrimal acinar cells [G. W. Laurie, J. D. Glass, R. A. Ogle, C. M. Stone, J. R. Sluss, and L. Chen. Am. J. Physiol. 270 ( Cell Physiol. 39): C1743–C1750, 1996]. The identity of the active laminin-1 site and the possibility that other promoters of coupling are present in the acinar cell microenvironment were probed by use of different substrates, media, neutralizing antibodies and cell numbers. Regulated peroxidase secretion was unaffected by basement membrane coat concentration and was detectable at reduced levels in serum-free medium. Anti-laminin-1 antibodies, particularly against sites in the β1 and γ1 chains, but not α1 chains, partially suppressed regulated secretion, as did an anti-collagen IV antibody. Without effect were RGD peptide and antibodies against entactin, the β1-integrin subunit, and several growth factors. Increasing cell number in serum-free medium revealed an unknown, serum-maskable, secretion-enhancing activity with a remarkable specificity for regulated secretion. Stimulus-secretion coupling, therefore, appears to be modulated by several extracellular factors whose relative contributions remain to be determined.

Effects of MeCh, thapsigargin, and La3+ on plasmalemmal and intracellular Ca2+ transport in lacrimal acinar cells

1990 ◽  
Vol 258 (6) ◽  
pp. C1006-C1015 ◽  
Author(s):  
C. Y. Kwan ◽  
H. Takemura ◽  
J. F. Obie ◽  
O. Thastrup ◽  
J. W. Putney
Keyword(s):  
Plasma Membrane ◽  
Muscarinic Receptor ◽  
Extracellular Space ◽  
Receptor Agonist ◽  
Inositol Phosphates ◽  
Acinar Cells ◽  
Direct Channel ◽  
Physiological Conditions ◽  
Parotid Cells ◽  
Lacrimal Acinar Cells

The Ca2(+)-mobilizing actions of the muscarinic receptor agonist, methacholine (MeCh), and the microsomal Ca2+ pump inhibitor, thapsigargin, were investigated in lacrimal acinar cells. As previously shown for parotid cells (J. Biol. Chem. 264: 12266-12271, 1989), thapsigargin activates both internal Ca2+ release and Ca2+ entry from the extracellular space without increasing cellular inositol phosphates. The inorganic Ca2+ antagonist La3+ inhibited MeCh- or thapsigargin-activated Ca2+ entry. However, when added before MeCh or thapsigargin, La3+ inhibited the extrusion of Ca2+ at the plasma membrane. This phenomenon was exploited in protocols designed to investigate the pathways for filling agonist-sensitive Ca2+ stores in lacrimal cells. The results show that, in contrast to previous suggestions that external Ca2+ is required to replenish agonist-regulated Ca2+ stores, the inhibition of Ca2+ extrusion permits recycling of Ca2+ released by MeCh back into an MeCh- and thapsigargin-sensitive pool. Thus, although extracellular Ca2+ is the major source for refilling the intracellular Ca2+ stores under physiological conditions, the pathway by which this Ca2+ enters the pool need not be a direct one. These results are consistent with the recently revised capacitative model for the refilling of intracellular Ca2+ stores through Ca2+ influx subsequent to Ca2+ depletion, according to which refilling of intracellular Ca2+ stores occurs via a cytoplasmic route rather than a direct channel between intracellular Ca2+ stores and the extracellular space.

Discovering the mechanism of capacitative calcium entry

2006 ◽  
Vol 291 (6) ◽  
pp. C1104-C1106 ◽  
Author(s):  
Juan A. Rosado
Keyword(s):  
Acinar Cells ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Historical Significance ◽  
Intracellular Ca ◽  
Lacrimal Acinar Cells ◽  
Classic Paper

This essay examines the historical significance of an APS classic paper that is freely available online: Kwan CY, Takemura H, Obie JF, Thastrup O, and Putney JW Jr. Effects of MeCh, thapsigargin, and La3+ on plasmalemmal and intracellular Ca2+ transport in lacrimal acinar cells. Am J Physiol Cell Physiol 258: C1006–C1015, 1990. ( http://ajpcell.physiology.org/cgi/reprint/258/6/C1006 )

IL-2 Immunoreactive Proteins in Lacrimal Acinar Cells

2002 ◽  
pp. 795-799 ◽  
Author(s):  
Yan Zhang ◽  
Jiansong Xie ◽  
Limin Qian ◽  
Joel E. Schechter ◽  
Austin K. Mircheff
Keyword(s):  
Acinar Cells ◽  
Lacrimal Acinar Cells

Potential Role of Disrupted Lacrimal Acinar Cells in Dry Eye during Pregnancy

2002 ◽  
pp. 153-157 ◽  
Author(s):  
Joel E. Schechter ◽  
Michael Pidgeon ◽  
Donald Chang ◽  
Yi-Ching Fong ◽  
Melvin D. Trousdale ◽  
...  
Keyword(s):  
Dry Eye ◽  
Potential Role ◽  
Acinar Cells ◽  
Lacrimal Acinar Cells
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