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Study · Not a test of the peptide alone · 2020

1 result

Biochemical determinants of the IGFBP-3-hyaluronan interaction.

Dorandish S, Devos J, Clegg B, Price D, Muterspaugh R, Guthrie J, Heyl DL, Evans HG

FEBS open bio22 Jul 2020Cited by 16 (Europe PMC)

PMID32592613 (opens in a new tab)PMCIDPMC7396449 (opens in a new tab)DOI10.1002/2211-5463.12919 (opens in a new tab)PepBankPUB-32592613
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Summary

IGFBP-3, the most abundant IGFBP and the main carrier of insulin-like growth factor I (IGF-I) in the circulation, can bind IGF-1 with high affinity, which attenuates IGF/IGF-IR interactions, thereby resulting in antiproliferative effects. The C-terminal domain of insulin-like growth factor-binding protein-3 (IGFBP-3) is known to contain an 18-basic amino acid motif capable of interacting with either humanin (HN) or hyaluronan (HA). We previously showed that the 18-amino acid IGFBP-3 peptide is capable of binding either HA or HN with comparable affinities to the full-length IGFBP-3 protein and that IGFBP-3 can compete with the HA receptor, CD44, for binding HA. Blocking the interaction between HA and CD44 reduced viability of A549 human lung cancer cells. In this study, we set out to better characterize IGFBP-3-HA interactions. We show that both stereochemistry and amino acid identity are important determinants of the interaction between the IGFBP-3 peptide and HA and for the peptide's ability to exert its cytotoxic effects. Binding of IGFBP-3 to either HA or HN was unaffected by glycosylation or reduction of IGFBP-3, suggesting that the basic 18-amino acid residue sequence of IGFBP-3 remains accessible for interaction with either HN or HA upon glycosylation or reduction of the full-length protein. Removing N-linked oligosaccharides from CD44 increased its ability to compete with IGFBP-3 for binding HA, while reduction of CD44 rendered the protein relatively ineffective at blocking IGFBP-3-HA interactions. We conclude that both deglycosylation and disulfide bond formation are important for CD44 to compete with IGFBP-3 for binding HA.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study1

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone1

In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Humanin.

  1. 01LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    Binding of IGFBP-3 to humanin or hyaluronan was unaffected by glycosylation or reduction of IGFBP-3.

    In plain wordsIn lab tests, IGFBP-3 still bound humanin after changes to its sugar groups or disulfide bonds.

    Peptide
    Humanin
    Outcome
    No significant changeIGFBP-3 binding to humanin after glycosylation or reduction
    Study

    n: not reported in source

    in vitro binding assays
    Outcome group
    Receptor activity and mechanism · Whole body

    Source sentences

    Summary
    Binding of IGFBP-3 to either HA or HN was unaffected by glycosylation or reduction of IGFBP-3,

    In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 21:44 UTC

    Study results updated

  2. Version 1

    13 Oct 2026, 16:31 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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