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Study · Not a test of the peptide alone · 2022

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N-Linked Glycosylation in Chinese Hamster Ovary Cells Is Critical for Insulin-like Growth Factor 1 Signaling.

Salvi R, Kumar C, Brahmbhatt K, Subedi R, Idicula-Thomas S, Madan T, Biswas B

International journal of molecular sciences29 Nov 2022Cited by 5 (Europe PMC)

PMID36499281 (opens in a new tab)PMCIDPMC9735751 (opens in a new tab)DOI10.3390/ijms232314952 (opens in a new tab)PepBankPUB-36499281
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Summary

Cell surface proteins carrying N-glycans play important roles in inter- and intracellular processes including cell adhesion, development, and cellular recognition. Dysregulation of the glycosylation machinery has been implicated in various diseases, and investigation of global differential cell surface proteome effects due to the loss of N-glycosylation will provide comprehensive insights into their pathogenesis. Cell surface proteins isolated from Parent Pro-5 CHO cells (W5 cells), two CHO mutants with loss of N-glycosylation function derived from Pro-5 CHO (Lec1 and Lec4 cells), were subjected to proteome analysis via high-resolution LCMS. We identified 44 and 43 differentially expressed membrane proteins in Lec1 and Lec4 cells, respectively, as compared to W5 cells. The defective N-glycosylation mutants showed increased abundance of integrin subunits in Lec1 and Lec4 cells at the cell surface. We also found significantly reduced levels of IGF-1R (Insulin like growth factor-1 receptor); a receptor tyrosine kinase; and the GTPase activating protein IQGAP1 (IQ motif-containing GTPase activating protein), a highly conserved cytoplasmic scaffold protein) in Lec1 and Lec4 cells. In silico docking studies showed that the IQ domain of IQGAP1 interacts with the kinase domain of IGF-1R. The integrin signaling and insulin growth factor receptor signaling were also enriched according to GSEA analysis and pathway analysis of differentially expressed proteins. Significant reductions of phosphorylation of ERK1 and ERK2 in Lec1 and Lec4 cells were observed upon IGF-1R ligand (IGF-1 LR3) stimulation. IGF-1 LR3, known as Long arginine3-IGF-1, is a synthetic protein and lengthened analog of insulin-like growth factor 1. The work suggests a novel mechanism for the activation of IGF-1 dependent ERK signaling in CHO cells, wherein IQGAP1 plausibly functions as an IGF-1R-associated scaffold protein. Appropriate glycosylation by the enzymes MGAT1 and MGAT5 is thus essential for processing of cell surface receptor IGF-1R, a potential binding partner in IQGAP1 and ERK signaling, the integral components of the IGF pathway.
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, IGF-1 LR3 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 IGF-1 LR3.

  1. 01LabNot a test of IGF-1 LR3 aloneIn vitro (cells)Mechanism

    In CHO cells lacking N-glycosylation function (Lec1 and Lec4), phosphorylation of ERK1 and ERK2 after stimulation with the IGF-1R ligand IGF‑1 LR3 was significantly reduced.

    In plain wordsIn lab cells without normal sugar-chain processing, IGF‑1 LR3 triggered less ERK signaling. The test used IGF‑1 LR3 as a tool.

    Peptide
    IGF-1 LR3
    Outcome
    DecreaseERK1/ERK2 phosphorylation after IGF-1R ligand stimulation
    Study

    Chinese hamstern: not reported in source

    Lec1 and Lec4 CHO N-glycosylation mutants
    Comparator
    Parent W5 CHO cells
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Significant reductions of phosphorylation of ERK1 and ERK2 in Lec1 and Lec4 cells were observed upon IGF-1R ligand (IGF-1 LR3) stimulation.
    1 context sentence
    Summary · context
    Cell surface proteins isolated from Parent Pro-5 CHO cells (W5 cells), two CHO mutants with loss of N-glycosylation function derived from Pro-5 CHO (Lec1 and Lec4 cells), were subjected to proteome analysis via high-resolution LCMS.

    In this study, IGF-1 LR3 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 IGF-1 LR3.

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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