Insulin-like growth factor binding protein-6 (IGFBP-6) is found in ser
um, cerebrospinal fluid and conditioned media from human fibroblasts.
It has a marked preferential binding affinity for IGF-II over IGF-I. T
he present study demonstrates that IGFBP-6 purified from human cerebro
spinal fluid is O-glycosylated but not N-glycosylated. Enzymatic degly
cosylation does not alter the high affinity of IGFBP-6 for IGF-II (Ka
4.4+/-2.2 x 10(11) M-1) or its preference for IGF-II over IGF-I. The e
ffect of glycosylation of IGFBP-6 on its secretion, in vivo stability
or localization remains to be determined.