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Related Concept Videos

Glucagon-like Receptor Agonists01:24

Glucagon-like Receptor Agonists

Incretins include glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which stimulate insulin secretion post-meals. In type 2 diabetes, GIP's efficacy is reduced, making GLP-1 a viable drug target. GIP originates from preproGIP.
GLP-1, when administered in high doses intravenously, triggers insulin secretion, inhibits glucagon release, slows gastric emptying, reduces food intake, and restores normal insulin secretion. However, its rapid inactivation by the...
Production of Pharmaceuticals01:30

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Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a significant...
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Short-term regulation of food intake primarily involves neural signals from the gastrointestinal (GI) tract, blood nutrient levels, and GI tract hormones. Communication between the gut and brain via vagal nerve fibers plays a significant role in evaluating the contents of the gut. Clinical studies have shown that protein ingestion produces a more prolonged response in these nerve fibers compared to an equivalent amount of glucose. Additionally, the activation of stretch receptors caused by GI...

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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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E-peptides control bioavailability of IGF-1.

Marianne Smedegaard Hede1, Ekaterina Salimova, Agnieszka Piszczek

  • 1European Molecular Biology Laboratory (EMBL)-Mouse Biology Unit, Monterotondo, Rome, Italy.

Plos One
|December 20, 2012
PubMed
Summary

The E-peptides of Insulin-like growth factor 1 (IGF-1) bind to the extracellular matrix, controlling IGF-1 bioavailability. This mechanism prevents systemic circulation, enabling targeted delivery of IGF-1 and other therapeutic proteins.

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Immunoprecipitation with an Anti-Epitope Tag Affinity Gel to Study Protein-Protein Interactions

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Regenerative Medicine

Background:

  • Insulin-like growth factor 1 (IGF-1) is a key cytoprotective agent with therapeutic potential.
  • Transgenic IGF-1 over-expression aids tissue repair but doesn't significantly increase serum IGF-1 levels.
  • Alternative splicing of IGF-1 propeptides generates C-terminal extension (E) peptides with high positive charge.

Purpose of the Study:

  • To investigate the role of IGF-1 E-peptides in controlling IGF-1 bioavailability.
  • To determine if E-peptides mediate IGF-1 binding to the extracellular matrix (ECM).
  • To assess the potential of E-peptides for targeted protein delivery.

Main Methods:

  • Utilized decellularized mouse tissue for in vitro binding assays.
  • Examined the binding affinity of murine IGF-1 to the ECM.
  • Tested binding of E-peptide-fused relaxin to decellularized ECM to assess E-peptide specificity.

Main Results:

  • Murine IGF-1 demonstrated in vitro binding to decellularized ECM, mediated by E-peptides.
  • Binding affinity varied, indicating specific interactions with ECM components.
  • E-peptides fused to relaxin exhibited similar avid binding to decellularized ECM, independent of IGF-1.

Conclusions:

  • IGF-1 E-peptides control IGF-1 bioavailability by facilitating ECM binding.
  • This mechanism limits systemic circulation of IGF-1.
  • E-peptides offer a strategy for tethering IGF-1 and other therapeutic proteins to specific sites.