Expression of MAL, an Integral Protein Component of the Machinery for Raft-mediated Apical Transport, in Human Epithelia
Open Access
- 1 May 2003
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 51 (5) , 665-673
- https://doi.org/10.1177/002215540305100512
Abstract
The MAL protein is the only integral membrane protein identified as being an essential component of the machinery necessary for apical transport in the canine MDCK cell line, a paradigm of polarized epithelial cells. To characterize the range of human epithelia that use MAL-mediated pathways of transport, we performed an immunohistochemical survey of normal tissues using a monoclonal antibody (MAb) specific for the MAL protein. For comparison, different types of carcinoma were also analyzed. MAL, with a characteristic strong supranuclear granular distribution, was detected in specific types of normal epithelial cells throughout the respiratory system, the gastrointestinal and genitourinary tracts, and in exocrine and endocrine glands. Absorptive cells (e.g., enterocytes), and many different types of specialized secretory cells, either organized in discrete clusters (e.g., endocrine cells in the pancreas), gathered together in an endocrine gland (e.g., thyroid), interspersed with other cells in glands (e.g., parietal cells), or dispersed singly among other cells (e.g., type 2 pneumocytes) were positive for MAL. We also analyzed a series of epithelial renal and thyroid tumors and found alterations dependent on the particular histological type of tumor. These results open potential applications of the anti-MAL antibody for the characterization of neoplastic tissue.Keywords
This publication has 28 references indexed in Scilit:
- Lipid rafts mediate biosynthetic transport to the T lymphocyte uropod subdomain and are necessary for uropod integrity and functionBlood, 2002
- MAL Mediates Apical Transport of Secretory Proteins in Polarized Epithelial Madin-Darby Canine Kidney CellsJournal of Biological Chemistry, 2001
- BENE, a Novel Raft-associated Protein of the MAL Proteolipid Family, Interacts with Caveolin-1 in Human Endothelial-like ECV304 CellsJournal of Biological Chemistry, 2001
- MAL, a novel integral membrane protein of human T lymphocytes, associates with glycosylphosphatidylinositol-anchored proteins and Src-like tyrosine kinasesEuropean Journal of Immunology, 1998
- Recombinant Expression of the MAL Proteolipid, a Component of Glycolipid-enriched Membrane Microdomains, Induces the Formation of Vesicular Structures in Insect CellsPublished by Elsevier ,1997
- Structural and Biochemical Similarities Reveal a Family of Proteins Related to the MAL Proteolipid, a Component of Detergent-Insoluble Membrane MicrodomainsBiochemical and Biophysical Research Communications, 1997
- VIP17/MAL, a proteolipid in apical transport vesiclesFEBS Letters, 1995
- Expression of vascular adhesion molecules on human endothelia in autoimmune thyroid disordersClinical and Experimental Immunology, 1995
- Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytesJournal of Neuroscience Research, 1995
- Cell polarity and epithelial oncogenesisTrends in Cell Biology, 1991