Abstract
Extensive molecular trafficking exists between the basal-lateral plasma membrane (blm) and endomembrane compartments of lacrimal gland acinar cells. Proteins normally must be segregated consistently between the lacrimal acinar cell’s apical secretory pathway, lysosomal pathway, and basal-lateral membrane recycling pathway. A recent analytical subcellular fractionation study (Yang et al., 1999b) showed that significant changes in the distributions of a variety of endomembrane proteins occur when lacrimal acinar cells are stimulated with 10 µM carbachol for 20 min. In that study, the amount of β-hexosaminidase, typically a lysosomal enzyme, but also a secretory enzyme in lacrimal acinar cells, increased in isolated low-density trans-Golgi network (ld-tgns) believed to represent domains of the trans-Golgi network that mediate traffic to the basal-lateral membrane. This increase was accompanied by net redistributions of protein into the ld-tgns and blm of proteins from other endomembrane compartments. These included galactosyltransferase from the Golgi complex, Rab6 from domains of the high-density trans-Golgi network (hd-tgns) that are believed to mediate traffic both to secretory vesicles and pre-lysosomes (preLys), and immature forms of cathepsin B from the hd-tgns and preLys. We have proposed that such alterations of protein segregation and targeting in the endomembrane traffic might overwhelm peripheral tolerance mechanisms and provoke local autoimmune responses (Mircheff et al., 1996, Mircheff et al., this volume).
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References
D.A. Brown and J.K. Rose, Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical surface, Cell 68: 533 (1992).
J.P. Gierow, T. Yang, A. Bekmezian, N. Liu, J. Norian, S.A. Kim, S. Rafisolyman, H. Zeng, C.T. Okamoto, R.L. Wood, and A.K. Mircheff, Na-K-ATPase in lacrimal gland acinar cell endosomal system: correcting a case of mistaken identity. Am. J. Physiol. 271: C1685 (1996).
H.R. Hope, and L.J. Pike, Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains, Mol. Biol. Cell 7: 843 (1996).
A.K. Mircheff, N. Nowroozi, T. Yang, L. Qian, A. Segawa, and J.H. Zernik, Acidic β-galactosidase in lacrimal acinar cells. Invest. Ophthalmol. Vis Sci. 40: S63 (2000).
N. Nowroozi, S. Kim, A. Gupta, S. Warita, and J.H. Zernik, High levels of GM1-ganglioside β-galactosidase in the salivary glands and GM1-like ganglioside storage in parotids of deficient mice, Caraniofac. Genet. Dev. Biol. 19: 41 (1999).
G.A. Scheele, S. Fukuoka, and S.D. Freedman, Role of the GP2/THP family of GPI-anchored proteins in membrane trafficking during regulated exocrine secretion. Pancreas 9: 139 (1994).
K. Simons and G. van Meer, Lipid sorting in epithelial cells. Biochemistry 27: 6197 (1988).
T. Yang, H. Zeng, J. Zhang, C.T. Okamoto, D.W. Warren, R.L. Wood, M. Bachmann, and A.K. Mircheff, Major histocompatibility complex class II molecules, cathepsins B and D, and La/SSB proteins in lacrimal gland acinar cell endomembranes. Am. J. Physiol. 277: C994 (1999a).
T. Yang, H. Zeng, J. Zhang, C.T. Okamoto, D.W. Warren, R.L. Wood, M. Bachmann, and A.K. Mircheff, Stimulation with carbachol alters endomembrane distribution and plasma membrane expression of intracellular proteins in lacrimal gland acinar cells. Exp. Eye. Res. 69: 651 (1999b).
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Qian, L., Xie, J., Mircheff, A.K. (2002). Glycolipid-Rich Membrane Microdomains in Lacrimal Acinar Cell Endomembrane Compartments. In: Sullivan, D.A., Stern, M.E., Tsubota, K., Dartt, D.A., Sullivan, R.M., Bromberg, B.B. (eds) Lacrimal Gland, Tear Film, and Dry Eye Syndromes 3. Advances in Experimental Medicine and Biology, vol 506. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0717-8_27
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DOI: https://doi.org/10.1007/978-1-4615-0717-8_27
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