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J Biol Chem, Vol. 273, Issue 8, 4530-4538, February 20, 1998
From the The primary structure of human macrophage
receptor with collagenous structure (MARCO) was determined from
cDNA clones and shown to be highly similar to that of mouse
(Elomaa, O., Kangas, M., Sahlberg, C., Tuukkanen, J., Sormunen, R.,
Liakka, A., Thesleff, I., Kraal, G., and Tryggvason, K. (1995)
Cell 80, 603-609). Features such as potential carbohydrate
attachment sites in the extracellular spacer domain III and the
interruption of Gly-Xaa-Yaa repeats in the collagenous domain IV were
conserved between the two species. However, the human MARCO polypeptide
chain lacked the intracellular cysteine present in mouse, as well as
two extracellular cysteines that form interchain disulfide bonds in the
murine protein. In situ hybridization showed MARCO to be
strongly expressed in macrophages of several tissues of human
individuals with sepsis. No expression was observed in other cell
types. The bacteria-binding region of MARCO was determined in binding
studies with full-length and truncated variants of MARCO, and localized
to a region proximal to the cysteine-rich part of the COOH-terminal
domain V. The intrachain disulfide bond pattern of domain V was
established showing that these bonds are between cysteine pairs C1-C5,
C2-C6, and C3-C4.
Structure of the Human Macrophage MARCO Receptor and
Characterization of Its Bacteria-binding Region
,,,,,
Division of Matrix Biology, Department of
Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden and the § Institute of Biotechnology,
University of Helsinki, FIN-00014 Helsinki, Finland
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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