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Structural & cell research

IGF-1 LR3

LR3 structure and binding-protein comparisons explain how its apparent potency changes with the cell environment. Native IGF-I findings remain separate pathway context.

Research summary

Isolation and validation of human prepubertal skeletal muscle cells: maturation and metabolic effects of IGF-I, IGFBP-3 and TNFalpha.

The Journal of physiology 2005

Grohmann M, Foulstone E, Welsh G, Holly J, Shield J, Crowne E, Stewart C

Primary human skeletal-muscle cell culture

Native IGF-I promoted proliferation and differentiation in child-derived skeletal-muscle cell cultures and partly opposed inhibition associated with TNF-α. Responses differed from adult-derived cultures, illustrating how the cellular setting changes growth-factor biology. The material was native IGF-I, so this is pathway context rather than a result for IGF-1 LR3.

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Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency.

Journal of molecular endocrinology 1992

Francis GL, Ross M, Ballard FJ, Milner SJ, Senn C, McNeil KA, Wallace JC, King R, Wells JR

Cellular and animal mechanistic research

Long-[Arg3]-IGF-I produced stronger responses than native IGF-I in cell systems that released IGF-binding proteins, but was less potent in a fibroblast system without detectable binding proteins. Receptor and binding-protein comparisons linked this contrast to altered IGFBP interactions. The medium therefore helps determine the analogue’s apparent biological potency.

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Solution structure and backbone dynamics of long-[Arg(3)]insulin-like growth factor-I.

The Journal of biological chemistry 2000

Laajoki LG, Francis GL, Wallace JC, Carver JA, Keniry MA

Molecular and analytical characterisation

Solution-structure measurements showed that Long-[Arg3]-IGF-I retained the overall IGF-I domain with changes near the N-terminus and a flexible extension. The structural differences help explain altered binding-protein interactions. They describe the characterised analogue rather than confirming the folding or sequence of a separate commercial batch.

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Models studied

  • LR3 structure and IGF-binding-protein interactions
  • LR3 and native IGF-I cell comparisons
  • Native IGF-I pathway context

Key findings

  • Binding proteins change apparent potency

    The binding-protein environment changed LR3’s apparent potency, including a weaker response in one system without detectable IGFBPs.

  • Structure of the extended analogue

    A retained IGF-I fold and flexible N-terminal extension provide structural context for altered interactions.

  • Native IGF-I as pathway context

    Native IGF-I cell findings supply pathway context and remain explicitly separate from LR3 results.

References

  1. Isolation and validation of human prepubertal skeletal muscle cells: maturation and metabolic effects of IGF-I, IGFBP-3 and TNFalpha.

    The Journal of physiology 2005

    Grohmann M, Foulstone E, Welsh G, Holly J, Shield J, Crowne E, Stewart C

    PMID 16081485

    View on PubMed

  2. Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency.

    Journal of molecular endocrinology 1992

    Francis GL, Ross M, Ballard FJ, Milner SJ, Senn C, McNeil KA, Wallace JC, King R, Wells JR

    PMID 1378742

    View on PubMed

  3. Solution structure and backbone dynamics of long-[Arg(3)]insulin-like growth factor-I.

    The Journal of biological chemistry 2000

    Laajoki LG, Francis GL, Wallace JC, Carver JA, Keniry MA

    PMID 10744677

    View on PubMed

For laboratory research use only. Content is provided for research reference and is not intended as medical or veterinary guidance.