|
|
Blood, Vol. 109, Issue 12, 5223-5229, June 15, 2007
The macrophage CD163 surface glycoprotein is an erythroblast adhesion receptor
Blood Fabriek et al.
109: 5223
Supplemental materials for: Fabriek et al, Vol 109, Issue 12, 5223-5229
Files in this Data Supplement:
- Figure S1. The predicted rat CD163 amino acid sequence (XP_232342) and its alignment to mouse (AAK16065)24 and human (CAA80542)23 CD163 (PDF, 15.2 KB) -
Links: AAK16065 and CAA80542
Alignments were performed with the clustalW algorithm version 1.82 and adjusted manually. Amino acid identities for the full-length proteins were rat-mouse 89%, rat-human 74%, and human-mouse 73%. The positions of the peptides identified by amino acid sequencing (Fig. 1D) are indicated in red; the first of these (ie, VTQAPEGRKKELRLAG) also indicates the N-terminus of the mature polypeptide. The peptides that were synthesized and analyzed for erythroblast binding are highlighted in blue. Dotted lines indicate respective leader and transmembrane regions; the scavenger domain boundaries are also indicated.
- Figure S2 (PDF, 99.7 KB) -
Microphotographs of the red pulp areas from the spleen of a juvenile 7 day old rat (A), or an adult animal 6 days after Plasmodium brucei infection (B) double-stained with mAb ED2 for rat CD163 (black) and mAb OX2617 for rat transferrin receptor-positive erythroblasts (red). Note that essentially all erythroblastic islands have macrophages with high levels of CD163.
|
|
