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(Received for publication, April 23, 1997, and in revised form, July 16, 1997)
From the Departments of By using receptor-associated protein (RAP) as an
affinity target, an intrinsic factor-vitamin B12
(IF-B12)-binding renal epithelial protein of ~460 kDa was
copurified together with the transcobalamin-B12-binding 600-kDa receptor, megalin. IF-B12 affinity chromatography
of renal cortex membrane from rabbit and man yielded the same
~460-kDa protein. Binding studies including surface plasmon resonance
analyses of the protein demonstrated a calcium-dependent
and high affinity binding of IF-B12 to a site distinct from
the RAP binding site. The high affinity binding of IF-B12
was dependent on complex formation with vitamin B12. Light
and electron microscope autoradiography of rat renal cortex
cryosections incubated directly with
IF-57Co-B12 and rat proximal tubules
microinjected in vivo with the radioligand demonstrated
binding of the ligand to endocytic invaginations of proximal tubule
membranes followed by endocytosis and targeting of vitamin
B12 to lysosomes. Polyclonal antibodies recognizing the
~460-kDa receptor inhibited the uptake. Immunohistochemistry of
kidney and intestine showed colocalization of the IF-B12
receptor and megalin in both tissues. In conclusion, we have identified the epithelial IF-B12-binding receptor as a ~460-kDa
RAP-binding protein facilitating endocytosis.
Volume 272, Number 42,
Issue of October 17, 1997
pp. 26497-26504
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Characterization of an Epithelial ~460-kDa Protein That
Facilitates Endocytosis of Intrinsic Factor-Vitamin B12
and Binds Receptor-associated Protein
,
,
,
and
Cell Biology and
Medical Biochemistry,
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