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J. Biol. Chem., Vol. 269, Issue 31, 19751-19756, 08, 1994

Structural analysis of proteoglycan macrophage colony-stimulating factor

F Kimura, S Suzu, Y Nakamura, N Wakimoto, Y Kanatani, N Yanai, N Nagata and K Motoyoshi
Third Department of Internal Medicine, National Defense Medical College, Saitama, Japan.

Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony- stimulating factor (M-CSF). We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells. PG- M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200- kDa subunit. The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF). The results obtained with the carboxyl- terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing. The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro- Arg is essential to process PG-M-CSF to 85-kDa M-CSF. Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412. We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
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