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 Mr 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ständker L,Wobst P,Mark S,Forssmann WGdoi
10.1016/s0014-5793(98)01497-5subject
Has Abstractpub_date
1998-12-18 00:00:00pages
281-6issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01497-5journal_volume
441pub_type
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