MGF VS PEG-MGF

Mechano Growth Factor has a huge socio-economic impact on diseases in the aging population. Its functions still require a lot of research. This small peptide shows adequate tissue penetration and can be manufactured at a little cost and modified to Pegylated-Mechano Growth Factor, increasing its stability. They are good candidates for developing into excellent methods for diagnosis and therapy. Expectedly, such compounds attract the attention of pharmaceutical industries. You can contact us at Loti Labs to buy peptides that are available for research purposes only.

A BRIEF INTRODUCTION OF MGF

Mechano Growth Factor (MGF) is a synthetically manufactured peptide that is an alternative splicing variant of Insulin-like Growth Factor-1 (IGF-1). It is first described in skeletal muscle and serves as a local tissue repair factor that responds to changes in physiological conditions or environmental stimuli inducing muscle cell proliferation. It activates satellite cells in the muscle, increasing the number of desmin-positive myogenic precursor cells resulting in hypertrophy or regeneration. It functions as a neuroprotectant in brain ischemia.

MGF is classified as IGF-1Eb in rats with a 52 base pair insert, but as IGF-1Ec in humans with a 49 base pair insert within the E domain of exon 5. It has a relatively short half-life of only a few minutes, and this is the reason why PEG-MGF was developed to help offset this particular disadvantage.

WHAT IS PEG-MGF

PEG-MGF (Pegylated Mechano Growth Factor) is a variant of IGF-1. PEGylation modifies MGF by fusing polyethylene glycol (PEG) to it, increasing its half-life from a few minutes to days, subsequently allowing it to be carried through the bloodstream for a long period before it is broken down and cleared by the kidneys. This process is essential for repairing muscle in animals after exercise or injury by promoting nitrogen retention and increasing protein synthesis.

MECHANISM OF ACTION

Several studies in animals have shown PEG-MGF in the muscle’s regenerative process. It upregulates protein synthesis and activates satellite cells. PEG-MGF is a potent inducer of muscle hypertrophy in experiments after the cDNA of PEG-MGF was inserted into a plasmid vector and introduced by intramuscular injection. Its addition to muscle myoblasts increased proliferation and retarded differentiation even in the presence of anti-IGF-1 receptor antibodies, possibly through activating matrix fibrinolytic and metalloproteinase systems. Also, intensive exercise stimulates the release of growth hormone in the muscles to release MGF since there is a decrease in the level of this hormone when animals age.

Also, a recent study of PEG-MGF demonstrated that Protein Kinase C activity is needed for this peptide activation (translocation to the nucleus) of NF-E2-related factor-2 (Nrf2), which in turn increases heme oxygenase-1 expression, a critical event in mediating neuroprotection of neurons from oxidative stress-induced apoptosis in the brain.

THE EFFECTS OF PEG-MGF

Beyond muscle, PEG-MGF has been proposed to have other effects in the body of animal test subjects.

• In the heart, there is a temporary regulation of PEG-MGF expression in response to ischemia associated myocardial infarction. Its expression is induced within an hour and remains elevated for up to 8 weeks. Intracoronary delivery of this peptide elicits myocardial protection and improves hemodynamic function to a large extent than mature IGF-1 following myocardial infarction in sheep. Cellular protection conferred by PEG-MGF was due to an inhibition of apoptosis in the infarct border zone.

• PEG-MGF is shown to increase the proliferation and migration of mesenchymal bone marrow-derived stem cells, which is a source of autologous stem cells for transplantation into the heart.

• Also, PEG-MGF appears to stimulate pro-angiogenic activities in human vascular endothelial cells. Therefore, it could bestow potentially useful therapeutic actions at the level of vascular regeneration and collateralization, to restore blood flow in the heart following myocardial infarction.

• MGF is overexpressed in the regenerating regions following global adult brain ischemia. Its transcripts expressed during brain development, show highly specific temporal distributions. Moreover, neonatal hypoxia and hypoxia-ischemia insults produce increased and prolonged-expression of the MGF isoform only.

• Furthermore, IGF-1 plays a role in the interface between neurons of injured or damaged muscle. In amyotrophic lateral sclerosis, ALS (a disease with loss of motor neurons and progressive muscle weakness) muscle overexpression of IGF-1 slowed the disease progression. With treatment using PEG-MGF resulted in improvements. More motor neurons survived in PEG-MGF treated mice.

LOOKING FOR WHERE TO BUY PEPTIDES

You can purchase MGF from Loti Labs. Buy peptides which are USA-made for the integrity of your research. It is tested through HPLC and Mass spectrometry to ensure quality. MGF is commonly sold in 2mg vials. It is available in lyophilized powder form. Buy your peptides from us today!

References:

Shang J, Fan X, Liu H. The role of mechano-growth factor E peptide in the regulation of osteosarcoma. Oncology Letters. 2015 Aug;10(2):697-704. DOI: 10.3892/ol.2015.3339.

Zabłocka B, Goldspink PH, Goldspink G, Górecki DC. Mechano-Growth Factor: an important cog or a loose screw in the repair machinery?. Front Endocrinol (Lausanne). 2012;3:131. Published 2012 Nov 1. doi:10.3389/fendo.2012.00131

Kravchenko, I.V., Furalyov, V.A. & Popov, V.O. Stimulation of mechano-growth factor expression by myofibrillar proteins in murine myoblasts and myotubes. Mol Cell Biochem 363, 347–355 (2012) doi:10.1007/s11010-011-1187-5

Matheny RW Jr, Nindl BC, Adamo ML. Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology. 2010;151(3):865–875. doi:10.1210/en.2009-1217

Goldspink research on Mechano Growth Factor: it’s potential for optimizing physical training as well as misuse in doping British Journal of Sports Medicine 2005;39:787-788.