Laminine & the Stem Cell Architect, FGF

Updated July 28, 2016
laminine fgf fibroblast growth factor

What is FGF or FibroBlast Growth Factor?

FibroBlast Growth Factor or FGF is not a stem cell therapy but has a “stem cell like” behavior. FGF signals the cell or stem cells to repair or restore damaged or aging cells to its original state. Sources of concentrated FGF can vary from injectable vials or in the case of Laminine, from an avian egg during its embryonic stage. FGFs are key players in the processes of proliferation and differentiation of wide variety of cell tissues.

Why is it important?

It was discovered in recent decades that FGF plays an important role in cell signalling and repair. In the evolution of stem cell therapy, FGF has become an important preparation before stem cells can actually be transferred to the body. Without FGF, the stem cells in the body will not know what to do or where to go.

In the 1930s, a compound that is essential in supporting embryonic development, later called Fibroblast Growth Factor (FGF), was responsible for the development and formation of important body parts of an embryo. The same principle applies in human fetus. (Source: The embryo project)

While FGF is readily available in the human placenta, its availability to the human body diminishes over time and essentially vanishes as we age. Our body is incapable of producing its own FGF, so it must derive it from the food supply. (Source: LPGN)


Introduction to the Clinical Study

C J Powers, S W McLeskey and A Wellstein
School of Nursing, Department of Pharmacology, Department of Oncology, Lombardi Cancer Center,
Georgetown University, Washington, DC 20007, USA

Fibroblast growth factors (FGFs) are small polypeptide growth factors, all of whom share in common certain structural characteristics, and most of whom bind heparin avidly. Many FGFs contain signal peptides for secretion and are secreted into the extracellular environment, where they can bind to the heparan-like glycosaminoglycans (HLGAGs) of the extracellular matrix (ECM). From this reservoir, FGFs may act directly on target cells, or they can be released through digestion of the ECM or the activity of a carrier protein, a secreted FGF binding protein.

FGFs bind specific receptor tyrosine kinases in the context of HLGAGs and this binding induces receptor dimerization and activation, ultimately resulting in the activation of various signal transduction cascades. Some FGFs are potent angiogenic factors and most play important roles in embryonic development and wound healing. FGF signaling also appears to play a role in tumor growth and angiogenesis, and autocrine FGF signaling may be particularly important in the progression of steroid hormone-dependent cancers to a hormone-independent state

Etymology

FibroBlast (FB) are basic building block of fibrous tissue that includes the brain, nervous system, eye, blood vessels, heart, stomach, skin, liver, kidney, muscle & bone. The main function of FibroBlast is to maintain the structural integrity of connective tissues. Growth Factors (GF) are the most common cells of connective tissues in the body. The suffix “Blast” is used in cellular biology to denote a stem cell or a cell in an “Activated state of metabolism”.

Key Points of FGF

  • FGF is responsible for signaling cell restoration, repair, & rejuvenation.
  • FGFs are key players in the proliferation and differentiation of cells and tissues.
  • FGF is responsible for signaling cell restoration, repair, & rejuvenation.

laminine fgf fibroblast growth factor

Definition

Fibroblast growth factors or FGFs are a family of growth factors involved in angiogenesis, wound healing and embryonic development. The FGFs are heparin binding proteins and interactions with cell surface associated heparin sulfate proteoglycans have been shown to be essential for FGF signal transduction.

FGFs are key players in the processes of proliferation and differentiation of wide variety of cell tissues.

A detailed day‐by‐day study was performed in 1988 (A4, A11). Discovered only in the seventies, and also a peptide, this FGF is critical in the development of embryos, including humans. However, it is not found to be circulating in the human adult bodies.

Nerve growth factor (NGF) is a small secreted protein with is important for the growth, maintenance and survival of certain target neurons (nerve cells). It also functions as a signaling molecule. [1] [2] It is perhaps the prototypical growth factor, in that it is one of the first to be described. While “nerve growth factor” refers to a single factor, [3] ‘nerve growth factors” refers to a family of factors also known as neurotorphins. [4] Other members of the neurotropic family that are well-recognized include Brain-Derived Neurotropic Factor (BDNF), Neurotropin-3 (NT-3) and Neurotropin 4/5 (NT-4/5).

EGF results in cellular proliferation, differentiation and survival.[5] EGF is a low molecular weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including Submandibular gland and Parotid gland. Salivary EGF which seems also regulated by dietary inorganic iodine also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing oral and gastro esophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acid, pepsin, and trypsin and to physical, chemical and bacterial agents. [6]

CTGF (connective tissue growth factor) is a cysteine rich, matrix associated, heparin binding protein. In vitro, CTGF mirrors some of the effects of TGH beta on skin fibroblasts such as simulation of extracellular heparin matrix binding proteins. CTGF has important roles in many biological processes, including cell adhesion, migration, proliferation, angiogenesis, skeletal development, and tissue wound repair, and is critically involved in fibrotic disease and several forms of cancers.

How is FGF helpful to humans?

The precise blend of oligopeptides may be seen as building blocks, without a bridge, or a director. The role of such a director is fulfilled by a growth factor known as the Fibroblast Growth Factor, (repair factor) or FGF. FGF is prolific in PESE, as well as in the human placenta. On the 11th day of the incubation cycle of a chicken egg, the embryonic tissue shows a steep increase in the FGF, with the appropriate peptides to form the solid organs and bones (A1).

FGF is responsible for building the linings in the blood vessels, creating the infrastructure for the nutrients to flow to critical areas of the brain and organs. Research credits FGF with the potential to directly affect many neuro disorders because of clear results of the ability of FGF to affect the growth of neurites (A2). Neurites are signal senders (Axons) and signal receivers (dendrites) attached to the brain neurons.

Research (A7) has also shown clearly that new cell cultures show a dramatic increase in peptide and amino acid uptake in the presence of FGF. This result gives credence to the hypothesis that embryonic growth is influenced by a very precise mechanism, which combines unique combinations of amino acids, peptides and FGF.

Since FGF is not circulating in adults, multiple research projects on the effects of FGF serum to cure neurological disorders have been carried out. Fundamental to the research is the fact discovered by Altman, J. in 1962 (A26) that neural STEM cells are formed by the body in response to abnormalities, and are resident in certain zones of the brain. The brain is therefore ready to repair the damage, and these cells have shown to differentiate into a wide range of neurons (A27). Neurons derived from such neural stem cells are capable of migrating to various regions of the Central Nervous System. Over a decade of work, both in vivo and ex vivo has revealed that exposure to such neural stem cells to FGF permits direct differentiation into the required neural cells (A14, A25).

Mechanism of Action – The role of FGF in human development

Source: PDR 2016

The bioactive peptides in Laminine stimulate the dormant stem cells to utilize the phyto amino acids and marine protein to repair damaged aged cells.

Drying the photo-embryonic fluid before the peptides are “used up” to build organs and bones, allows us to provide this building, repairing, maintenance mechanism of perfectly balanced amino acids, peptides and growth factors to humans.

Nature has devised an extremely versatile mechanism to provide nutrition with miraculous precision to the embryo of living creatures. The precise blend of oligopeptides may be seen as building blocks, without a bridge, or a director. The role of such a director is fulfilled by a growth factor known as the Fibroblast Growth Factor, or FGF, also a bioactive peptide. FGF is prolific in proto-embryonic liquid as well as the human placenta. On the 11th day of the incubation cycle of a chicken egg, the chicken tissue shows a steep increase in these bioactive peptides, with the appropriate peptides to form the solid organs and bones (3). A detailed day-by-day study was performed in 1988 (5; 7). Discovered only in the seventies, FGF and bioactive peptides are critical in the development of embryos, including humans.

Bioactive peptides are responsible for building the linings in the blood vessels, creating the infrastructure for the nutrients to flow to critical areas of the brain and organs. Research credits bioactive peptides with the potential to directly affect many neuro disorders because of clear results of the ability of bioactive peptides to affect the growth of neurites (4). Neurites are signal senders (Axons) and signal receivers (dendrites) attached to the brain neurons.

Research (6) has also shown clearly that new cell cultures show a dramatic increase in peptide and amino acid uptake in the presence of FGF. This result gives credence to the hypothesis that embryonic growth is influenced by a very precise mechanism, which combines unique combinations of amino acids, peptides and FGF.


The Role of Protein & FibroBlast (dnalc.org)

Fibroblast is the most common type of cell found in connective tissue. Fibroblasts secrete collagen proteins that are used to maintain a structural framework for many tissues. They play a critical role in wound healing. Fibroblasts are the most common cells of connective tissue in animals.

WATCH VIDEO: Cell Signalling of Proteins & FibroBlast by DNAC

Proteins & FibroBlast

DNA Learning Center (DNALC) is the world’s first science center devoted entirely to genetics education. Please note timelines at 2:45 & 11:48



(02:45 Minutes) Fibroblasts, like all your cells, have a fluid, outer membrane that regulates the flow of molecules in and out. The gray structures sticking out of the cell membrane are receptors for incoming signals. When the growth factor from the platelet (shown in purple and blue) encounters a matching receptor, it binds to it. A second receptor protein joins in, making the growth factor fit like a key in a lock. The binding of the growth factor causes the receptor to change shape. This change in the protein conducts the signal through the membrane and into the cell’s interior – the cytoplasm. You’ll see this better from inside the cell.

(11:48 Minutes) The released growth factors will communicate with other cells to continue the healing process. These growth factors will attract more fibroblasts to the wound site and remodel the clot for better healing. Other proteins produced by this signalling pathway will tell the fibroblast cell to grow and divide, making many new cells to heal the wound. With the cooperation of many different cells, damage to the injured knee can be quickly repaired. Every day, your cells communicate and cooperate to keep you healthy. They act and interact; they grow, divide and die; all through the amazing language of cell signals.

Fibroblasts and fibrocytes are two states of the same cells, the former being the activated state, the latter the less active state, concerned with maintenance and tissue metabolism. Currently, there is a tendency to call both forms fibroblasts. The suffix “blast” is used in cellular biology to denote a stem cell or a cell in an activated state of metabolism.

Laminine also contains Amino Acids needed by FGF
→ They are the building blocks of proteins.
→ Amino Acids makes about 75% of our body.
→ Essential to nearly all chemical or bodily function.
→ Laminine has a full chain of 22 Amino Acids.

In recent years, the popularity of FibroBlast Growth Factor (FGF) into the mainstream has brought together this time Pharmaceutical companies who wants to incorporate the ingredient into their drugs or medicine.

fgf laminine research

Image from PNAS.org

Gordon Institute & Research

From 2010 to present, several medical conventions on FGF were conducted and participated by large Pharmaceutical corporation such as Aveo, Genentech, Merck Serono, Sanofi Aventis, Amgen, and National Insitutes of Health (NIH).

laminine gordon drugs pharmaceutical doctor


A simple Google search for FGF will result to a lot of research and studies.

Journal Frontier: FGF2 activates TRPC
http://journal.frontiersin.org/Journal/10.3389/fphys.2014.00038/full
FGF2 fibroblast growth factor 2 in Homo sapien: This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth.
http://www.ncbi.nlm.nih.gov/gene/2247
PNAS: FGF-2 regulation of neurogenesis in adult hippocampus after brain injury
http://www.pnas.org/content/98/10/5874.abstract
NCBI: Fibroblast growth factor-2-induced cardio protection against myocardial infarction
http://www.ncbi.nlm.nih.gov/pubmed/22304432
SBRC: The role of FGF-2 in Acute and Chronic Cardiac Response to Injury

Dr. Elissavet Kardami – Muscle Cell Biochemistry

Wikipedia: Fibroblast growth factor-2 (FGF-2) is a protein of the FGF family.[1] The Fibroblast growth factor (FGF) family, which includes 23 proteins, is involved in diverse functions in the embryo and the adult [1]. FGF-2 plays a role in a multitude of developmental and biological processes, including limb development, tissue repair, mesoderm induction, lung development and maintenance of neuron survival [1]. The wide range of roles this protein plays in development and differentiation has brought increasing attention to the clinical potential uses.
http://en.wikipedia.org/wiki/User:FGF2/sandbox


REFERENCES
(1) Roberts, Pamela R, et al. Nutrition Vol. 14, No. 3, 1998
(2) Kuljis, Rodrigo O. Jour. of Neuropathology & Exp. Neur., 1994.
(3) Jiangyong Min, et al. Jour. of Neuroscience Res., 86:2984‐2991 (2008)
(4) Z.Y. Zhou, et al. Neuroscience, Vol. 90, No. 4, 1493‐1499, 1999
(5) Arvanitakis, Constantine. Am. Jour. of Physiology, Vol. 231, No. 1, July 1976.
(6) Kristoffer, ester S., ETC Research & Development, Oslo, Norway.
(A1) Joseph‐Silverstein, Jacquelyn, et al (June 1989) Basic Fibroblast Growth Factor in the Chick Embryo: Immunolocalization to Striated Muscle Cells and Their Precursors. The Journal of Cell Biology, 108: 2459‐2466.
(A2) Hatten, M. E., et al (1988) In Vitro Neurite Extension by Granule Neurons is Dependent upon Astroglial‐Derived Fibroblast Growth Factor. Developmental Biology, 125:280‐289.
(A4) Seed, Jennifer, et al (1988) Fibroblast Growth Factor Levels in the Whole Embryo and Limb Bud during Chick Development. Developmental Biology, 128:50‐57.
(A11) Seed, Jennifer, et al (1988) Fibroblast Growth Factor Levels in the Whole Embryo and Limb Bud during Chick Development. Developmental Biology, 128:50‐57.
(A14) La Spada, Albert R (December 2005) Huntington’s disease and Neurogenesis: FGF‐2 to the Rescue? Vol. 102.
(A24) Hagg, Theo (2005) Molecular Regulation of Adult CNS Neurogenesis: an Integrated View.
(A25) Bjugstad, K. B., et al (2001) IGF‐1 and bFGF Reduce Glutaric Acid and 3‐ Hydroxyglutaric Acid Toxicity in Striatal Cultures.
(A26) Altman, J. (1962) Science 132:1127‐1128.
(A27) Arlotta, P., et al (2003) Exp. Gerontol, 38:173‐182.


→ Beginnings of FGF, Fertilized Avian Egg and how it works to benefit you.

29 Comments

  1. Larry Maheu-Reply
    June 30, 2015 at 4:46 am

    Someone emailed me and said Laminine no longer produced its FGF from Avian egg whites. Apparently, a U.S. company produced a substitute and Laminine decided to use it.. This is supposed to have happened in 2012. Your website was dated 2014.
    Cab you shed some light about this for me?
    Larry Maheu June 30, 2015

    • July 1, 2015 at 12:22 am

      Since early 2012, LifePharm Global Network has sourced its Fertilized Avian Egg Extract from organic, cage-free, hormone-free chicken farms in the United States, which is then developed with the process of Hygienic Evaporative Cooling. Hygienic Evaporative Cooling keeps the peptide chains that are so important in Laminine intact when converting the Fertilized Avian Egg Extract from a liquid to a powdered form. This technology is exclusive to LifePharm Global Network and was not readily available anywhere else in the world besides the United States. Previously, LPGN sourced its Fertilized Avian Egg Extract from Norway, but the change occurred in order to ensure the quality, traceability and supply of our materials. The laws governing avian products are especially stringent in the U.S.A., and LifePharm Global Network prides itself on operating under FDA and cGMP guidelines. You can find the answer to this, and other common questions here: https://altheadistributor.com/downloads_materials/ENG-Laminine-FAQ.pdf

  2. Jane-Reply
    August 10, 2016 at 2:29 am

    Hi there, I am a bodybuilder and FGF is listed as a banned substance for natural competitions. I have approached Lifepharm for clarification on the FGF content in Laminine and how long it stays in the body as clearly I cant risk having FGF in my urine if tested. However they have declined to assist me. Can you provide any guidance on this subject? How far out should I stop taking Laminine? Or indeed is it detectable? Thanks in advance. Jane

    • August 10, 2016 at 9:09 am

      World Anti-Doping Agency prohibits any form of drug or chemical substance that will cause an athlete to have the edge, simply because he/she has access to these expensive aids for muscles gain in general. This can also refer to FGFs in vial, injectable form. This potent form of FGF is traceable and comes as a form of treatment to activate stem cells in the body. Laminine’s FGF form part of the egg peptides/protein/amino acids, it is food in form, much like how vitamins work. The FGF in Laminine is not synthesized and is naturally produced in a partially incubated egg. Thus Laminine should NOT be classified as one and the same with injectable FGF that anti-doping agency prohibits. To begin with, the potency is much different. On a personal note as to traceability, I believe it is difficult to quantify because you take Laminine as food, incorporated with your diet. Laminine can also be classified as as dietary supplements which is encouraged by USDAA, and not listed in the USAAD prohibited list.

  3. Dr D-Reply
    February 28, 2017 at 4:23 am

    To say that the human body does not produce FGF is incorrect – the body produces 22 types of FGF. Which raises another issue: when you state that laminine contains FGF, which FGF are you referencing? As mentioned previously, humans produce 22 different FGF peptides that are produced by different tissues, signal through different receptors and exert different effects on different cell types.

    • March 1, 2017 at 3:41 am

      Referring to the 22 members of the FGF family that have been identified, although these are structurally related to signaling molecules (amino acids found in the body), the best source will still be through diet/food because the body (adults) can no longer make a significant amount of these, as compared to fetus or infants, where FGF/angiogenesis is required.

      Laminine’s FGF2 (family of growth factors) has been found in other animals such as cows, and in the case of Laminine, extracted from partially incubated hen egg, that has the highest quality of FGF known to science to date. Although the basic fibroblast growth factor (FGF-2) in the hypothalamic-pituitary system can be found, the expression of FGF-2 mRNA in the pituitary is low; the protein is widely distributed in both its neural and anterior lobes. Thus when the egg extract (Laminine) was discovered (also known as YTE), the supply through a diet of these proteins (rich in FGF2), has to come through a supplement. We know this based on clinical studies that show the ingestion of supplement rich with FGF(2), has greatly affected cells to heal more rapidly, than a person just eating healthy food.

      We do take note of rephrasing the article if it insinuated that the body cannot produce FGFs altogether. Thank you.

Leave A Comment

Copy Protected by Chetan's WP-Copyprotect.