Igf-1 Protein

Posted on December 10, 2013 by Maxim Peptide

IGF-1 stands for insulin-like growth factor 1,
which is often sold under the name
somatomedin C. This is a protein that is
encoded b the IGF1 gene in humans,
though it is seen in other forms in a !ariet
of tpes of animals. This peptide is
commonl referred to as the sulfation factor
which creates non-suppresible insulin-like
acti!it.
IGF-1 has taken on this name because it is
has a molecular structure that is !er
similar to insulin and acts in a !er similar
wa to this chemical. "atural !ersions of
IGF-1 contain #$ amino acids that are
aligned in a single chain.
IGF-1 is largel produced in the li!er with endocrine hormones and can target tissues using autocrine and paracrine
mechanisms. This is stimulated b growth hormone, though can be limited b a lack of growth hormone receptors,
under nutrition or failure of the signaling pathwas downstream of the signaling pathwa. IGF-1 is almost alwas
bound with the binding proteins of IGF%P-& which is one of the most abundant proteins in this snthesis.
In rats IGF-1 was found to be associated with dietar casein and ha!ing a negati!e association of protein-free diets.
Plants ha!e been found to contain biologicall acti!e recombinant IGF-1, which was noted in transgenic rice grains.
Role in Muscle Repair
"ew studies ha!e indicated that IGF-1 is !ital to repairing and regenerating muscle tissue in animals.
'keletal muscle is a highl dnamic tissue that is designed to respond to e(ternal and endogenous stimuli
which includes mechanical loading, growth factors and alterations. 'oleus muscle in particular is found to
e(press muscular atroph then the muscles are not used or e(tensi!el damaged.
IGF-1 has been implicated as a regulator in muscle modulation and repair, including controlling muscle si)e in
animals. This was e(amined for a !iral mediated o!ere(pression of this peptide on soleus muscle following the
immobili)ation of the hind limb upon reloading in mice.
*uring this process recombinant c*"+ !iruses containing IGF-1 were in,ected into the posterior hind limbs of
the test sub,ects and the contralateral limb was simultaneousl pro!ided with an application of saline.
+t -$ weeks the hind limbs of the mice were immobili)ed for two weeks as a means of inducing atroph in the
ankle plantar fle(or and soleus muscles. The mice were then allowed to reambulate and the reco!er of these
tissues was monitored for up to -1 das.
Initial findings re!ealed that o!ere(pression of IGF-1 were attenuated with the reloading induced damage of the
soleus muscles. This was used b the mouse.s bod to accelerate regeneration to force reco!er of the
muscles. /0I scans of the nice also showed that markers of muscle damage were lower in those that were
in,ected with IGF-1 in the soleus muscles at the --1 da market after reambulation.
The reduction of the pre!alence of damage to the muscles after an application of IGF-1 was confirmed !ia
histolog. This showed a lower fraction of abnormal muscle tissue in the areas that were e(posed to IGF-1 - das
after reambulation occurred.
The e!idence that IGF-1 assists with muscle regeneration showed timel increases in the central nuclei including a
paired bo( transcription factor, ele!ated /o* m0"+ and embryonic myosin. This helps to demonstrate that IGF-
1 ma ha!e potential in protecting skeletal muscle from damage b increasing regeneration and repair of the
tissues.
Mechanism of Action
The actions of IGF-1 are primaril mediated b the receptors it binds to, allowing it to interact with a wide !ariet of
tissues and cell tpes in animal bodies.
%inding to different acti!ators of +2T signaling pathwas can stimulate cell proliferation or growth. It is also
found to be a mediator of growth hormone effects from the anterior pituitar gland, which in turn mo!es from the
bloodstream to the li!er to trigger the production of IGF-1. It has also been seen to inhibit programmed cell
death.
+nimal tissues throughout the bod in a !ariet of different species ha!e been found to interact with IGF-1
including cartilage, skeletal muscle, kidnes, li!er, skin, ner!es, lungs, hematopoietic cells and others. This
peptide can be used to create effects similar to insulin, control the de!elopment and growth of cells and
snthesi)e *"+. This is particularl seen in ner!e cells.
*eficiencies of IGF-1 or the presence of growth hormone ha!e been shown to cause animals to displa a
diminished stature, though suppling animals with recombinant growth hormone or IGF-1 in clinical trials has
been found to help increase their si)e. 0esearchers hope to continue to research this potential to de!elop a
treatment for plan for conditions such as 3aron sndrome. 0esearch has also been found to impro!e these
conditions in cattle and IGF-1 has been found to help impro!e reproduction in these animals.
IGF-10 and growth factor receptors can be triggered using multiple pathwas. PI&2 has been found to be an
influential downstream partner in mammals, acting as a target for rapamcin. The full interaction of these receptors
is still being in!estigated.
Receptors and Binding
IGF-1 has been found to bind with two surface receptors, though research is still ongoing to determine other
connecti!e points.
IGF-1 ma bind to insulin receptors as well as IGF10. The latter appears to ha!e phsiologic effects that ha!e
an increased affinit for IGF-1 rather than those that are bound to the insulin receptors.
%oth of these receptors are a trosine kinase that causes phosphate molecules to be added to certain trosines.
IGF-1 will also acti!ate insulin receptors at around .1 times the potenc of insulin. Part of this signaling
response ma be caused b IGF10 insulin receptor heterodimers that bind with insulin 1$$ fold less effecti!el.
This has not been shown to correlate with the true potenc of IGF-1 in !i!o. This is also not effecti!e in inducing
phosphorlation of insulin receptors.
IGF-1 production is seen throughout an animal.s life but production is highest during an animal.s pubertal
growth spurt with le!els graduall reducing as the animal reaches old age.
4ther IGF%P molecules take on an inhibitor role when interacting with these peptides. IGF%P-- and 1 can bind
with IGF-1 with a higher affinit than the bindings at the receptors. This is used b an animal.s bod to increase
serum le!els of these chemicals to decrease the acti!it of IGF-1 when there is no longer a need for this
peptide.
IGF-1 has been found to be closel related to IGF-- which can bind with the same receptors, though IGF-- can also
bind with IGF-- receptors. IGF-0 receptors do not ha!e the signal transduction capacities that allow it to snc
with IGF-1 to make this protein more a!ailable, so it will often bind with IGF-10.
3ike the name implies, IGF-1 is related to insulin due to its structural properties. It is capable of acting with insulin
receptors though it is not nearl as effecti!e in this capacit as traditional insulin. 'plice !ariants of IGF-1 are
identical at the mature region but ha!e different 5 domains as /GF.
IGF-1 is found to be naturall pre!alent as animals are de!eloping the proper tissues and structure the animal.s
uni6ue phsiolog re6uires. This peptide is also found to be used b adult animals for anabolic mechanisms.
'nthetic !ersions of IGF-1 ha!e been found to ha!e a mecasermin that has potential in managing growth failure,
though research is still ongoing to determine the best was of utili)ing this propert.
Resource Box:
http788en.wikipedia.org8wiki8Insulin-like9growth9factor91