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人胰岛素样生长因子结合蛋白-6是O-糖基化的。

Human insulin-like growth factor binding protein-6 is O-glycosylated.

作者信息

Bach L A, Thotakura N R, Rechler M M

机构信息

Growth and Development Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

出版信息

Growth Regul. 1993 Mar;3(1):59-62.

PMID:7683533
Abstract

Insulin-like growth factor binding protein-6 (IGFBP-6) is found in serum, cerebrospinal fluid and conditioned media from human fibroblasts. It has a marked preferential binding affinity for IGF-II over IGF-I. The present study demonstrates that IGFBP-6 purified from human cerebrospinal fluid is O-glycosylated but not N-glycosylated. Enzymatic deglycosylation 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 effect of glycosylation of IGFBP-6 on its secretion, in vivo stability or localization remains to be determined.

摘要

胰岛素样生长因子结合蛋白-6(IGFBP-6)存在于血清、脑脊液以及人成纤维细胞的条件培养基中。它对IGF-II的结合亲和力明显高于IGF-I。本研究表明,从人脑脊液中纯化的IGFBP-6是O-糖基化的而非N-糖基化的。酶促去糖基化不会改变IGFBP-6对IGF-II的高亲和力(Ka 4.4 +/- 2.2 x 10(11) M-1),也不会改变其对IGF-II相对于IGF-I的偏好性。IGFBP-6糖基化对其分泌、体内稳定性或定位的影响仍有待确定。

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