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Vol. 8, Issue 11, 2241-2251, November 1997
and
*Department of Medical Biochemistry and Genetics, and
Detergent-insoluble complexes prepared from pig small intestine are
highly enriched in several transmembrane brush border enzymes including
aminopeptidase N and sucrase-isomaltase, indicating that they reside in a glycolipid-rich environment in vivo. In the
present work galectin-4, an animal lectin lacking a N-terminal signal
peptide for membrane translocation, was discovered in these complexes
as well, and in gradient centrifugation brush border enzymes and
galectin-4 formed distinct soluble high molecular weight clusters.
Immunoperoxidase cytochemistry and immunogold electron microscopy
showed that galectin-4 is indeed an intestinal brush border protein; we
also localized galectin-4 throughout the cell, mainly associated with
membraneous structures, including small vesicles, and to the rootlets
of microvillar actin filaments. This was confirmed by subcellular
fractionation, showing about half the amount of galectin-4 to be in the
microvillar fraction, the rest being associated with insoluble
intracellular structures. A direct association between the lectin and
aminopeptidase N was evidenced by a colocalization
along microvilli in double immunogold labeling and by the ability of an
antibody to galectin-4 to coimmunoprecipitate aminopeptidase N and sucrase-isomaltase. Furthermore,
galectin-4 was released from microvillar, right-side-out vesicles as
well as from mucosal explants by a brief wash with 100 mM lactose, confirming its extracellular localization. Galectin-4 is therefore secreted by a nonclassical pathway, and the brush border enzymes represent a novel class of natural ligands for a member of the galectin
family. Newly synthesized galectin-4 is rapidly "trapped" by
association with intracellular structures prior to its apical secretion, but once externalized, association with brush border enzymes
prevents it from being released from the enterocyte into the intestinal
lumen.
Structural Cell Biology Unit, Department of Medical
Anatomy, The Panum Institute, University of Copenhagen, Denmark
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