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Study · In vitro (cells) · 2010

3 results

Proteinase B disruption is required for high level production of human mechano-growth factor in Saccharomyces cerevisiae.

Morozkina EV, Marchenko AN, Keruchenko JS, Keruchenko ID, Khotchenkov VP, Popov VO, Benevolensky SV

Journal of molecular microbiology and biotechnology8 Jun 2010Cited by 3 (Europe PMC)

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study3

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Activity measurement

    In human postnatal myoblasts, recombinant MGF showed biological activity in a proliferation assay.

    In plain wordsIn lab tests with human muscle precursor cells, MGF made in yeast showed biological activity in a growth assay.

    Outcome
    Direction not reportedBiological activity in myoblast proliferation assay
    Study

    humann: not reported in source

    Human postnatal myoblasts
    Outcome group
    Muscle injury and repair · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The biological activity of recombinant MGF was verified in a proliferation assay employing human postnatal myoblasts.

Studies that did not test the peptide alone2

In this study, MGF / PEG-MGF 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 MGF / PEG-MGF.

  1. 02LabNot a test of MGF / PEG-MGF aloneIn vitro (cells)Mechanism

    In Saccharomyces cerevisiae expressing human MGF, proteinase B was the enzyme responsible for MGF processing.

    In plain wordsIn yeast that make human MGF, the enzyme proteinase B was the one that broke MGF down.

    Outcome
    Not applicableEnzyme that degrades MGF in yeast
    Study

    Saccharomyces cerevisiaen: not reported in source

    Recombinant yeast expressing human MGF
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    The proteinase B was identified as the enzyme responsible for MGF processing.
    1 context sentence
    Summary · context
    Human MGF was expressed in Saccharomyces cerevisiae, but the yield of the recombinant protein was low due to its rapid degradation.

    In this study, MGF / PEG-MGF 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 MGF / PEG-MGF.

  2. 03LabNot a test of MGF / PEG-MGF aloneIn vitro (cells)Other

    In Saccharomyces cerevisiae, deleting the proteinase B gene (Deltaprb1) gave a fivefold increase in recombinant human MGF yield, to 50 mg/l.

    In plain wordsIn yeast, removing the proteinase B gene gave a fivefold higher yield of human MGF, reaching 50 mg/l.

    Outcome
    IncreaseRecombinant MGF yield
    Study

    Saccharomyces cerevisiaen: not reported in source

    Recombinant yeast strain with Deltaprb1 deletion
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Measurements

    MGF yield
    50 mg/l
    Deltaprb1 yeast strain

    Source sentences

    Summary
    A yeast strain with Deltaprb1 deletion was created resulting in a fivefold increase of MGF yield that reached 50 mg/l.
    1 context sentence
    Summary · context
    Human MGF was expressed in Saccharomyces cerevisiae, but the yield of the recombinant protein was low due to its rapid degradation.

    In this study, MGF / PEG-MGF 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 MGF / PEG-MGF.

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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