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J. Biol. Chem., Vol. 277, Issue 13, 11255-11264, March 29, 2002
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From the Department of Biochemistry, Medical College of Wisconsin,
Milwaukee, Wisconsin 53226
Two distinct mannose 6-phosphate (Man-6-P)
receptors (MPRs), the cation-dependent MPR (CD-MPR) and the
insulin-like growth factor II/MPR (IGF-II/MPR), recognize a diverse
population of Man-6-P-containing ligands. The IGF-II/MPR is a type I
transmembrane glycoprotein with a large extracytoplasmic region
composed of 15 repeating domains that display sequence identity
to each other and to the single extracytoplasmic domain of the CD-MPR.
A structure-based sequence alignment of the two distinct
Man-6-P-binding sites of the IGF-II/MPR with the CD-MPR implicates
several residues of IGF-II/MPR domains 3 and 9 as essential for Man-6-P
binding. To test this hypothesis single amino acid substitutions were
made in constructs encoding either the N- or the C-terminal
Man-6-P-binding sites of the bovine IGF-II/MPR. The mutant IGF-II/MPRs
secreted from COS-1 cells were analyzed by pentamannosyl
phosphate-agarose affinity chromatography, identifying four residues
(Gln-392, Ser-431, Glu-460, and Tyr-465) in domain 3 and four residues
(Gln-1292, His-1329, Glu-1354, and Tyr-1360) in domain 9 as essential
for Man-6-P recognition. Binding affinity studies using the lysosomal enzyme,
Identification of Residues Essential for Carbohydrate
Recognition by the Insulin-like Growth Factor II/Mannose
6-Phosphate Receptor*
,
-glucuronidase, confirmed these results. Together these analyses provide strong evidence that the two Man-6-P-binding sites of
the IGF-II/MPR are structurally similar to each other and to the CD-MPR
and utilize a similar carbohydrate recognition mechanism.
*
This work was supported in part by Grant DK42667 from the
National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
This work was performed during the tenure of a fellowship from the
American Heart Association, Northland Affiliate, Inc.
§
Recipient of an Established Investigatorship from the American
Heart Association. To whom correspondence should be addressed. Tel.:
414-456-4698; Fax: 414-456-6510; E-mail: ndahms@mcw.edu.
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