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• W1978126211 abstract "The insulin‐like growth factor binding proteins (IGFBPs) are responsible for regulation of the effects and the bioavailability of the insulin‐like growth factors (IGFs). We screened for circulating fragments of human IGFBP‐5 in human hemofiltrate. Identification of IGFBP‐5 peptides in the fractions of our peptide bank generated from hemofiltrate was performed by their immunoreactivity and their capacity to bind IGF‐I. Different fragments of IGFBP‐5 with molecular sizes from 12 to 25 kDa were identified. C‐terminal peptides of IGFBP‐5 with molecular masses of 13.3 and 13.5 kDa were purified by consecutive chromatographic steps and sequenced. Sequence analysis of the peptides revealed the (double) sequences (K)FVGGAENXAHPRII and MVPRAVYLPNXDRKG. In addition, a smaller fragment with M r 2722 of the central IGFBP‐5 region was purified and showed the sequence HTRISELKAEAVKKDRRKKLTQS (residues 121–143) indicating plasma proteolysis of IGFBP‐5 C‐terminal to amino acids Lys‐120, Ser‐143, Lys‐144, and Arg‐188. According to mass spectrometric and sequence analysis, Thr‐152 was shown to be O ‐glycosylated. Fractions containing C‐terminal IGFBP‐5 fragments revealed significant IGF‐I binding properties. Our results indicate that plasma proteolysis of IGFBP‐5 preferentially occurs C‐terminally to basic residues and generates different C‐terminal fragments, possibly acting in an IGF‐dependent manner and bearing intrinsic biological functions." @default.
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• W1978126211 date "1998-12-18" @default.
• W1978126211 modified "2023-10-18" @default.
• W1978126211 title "Isolation and characterization of circulating 13‐kDa C‐terminal fragments of human insulin‐like growth factor binding protein‐5" @default.
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• W1978126211 doi "https://doi.org/10.1016/s0014-5793(98)01497-5" @default.
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