Bioactive Silicon (OSA) Improves Aged Skin and Reduces Wrinkling

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Whole Foods Magazine

April 2005

Bioactive Silicon (OSA) Improves Aged Skin and Reduces Wrinkling:

An interview with Drs. Dirk Vanden Berghe and Andre Barel.

By

Richard A. Passwater, Ph.D. and Richard Passwater, Jr.

Bioactive silicon is of great importance to our health in several ways. A new study verifies that

silicons systemic absorption of bioactive silicon as choline-stabilized orthosilicic acid (ch-OSA)produce rapid results actually observable and measurable by reduced skin wrinkling as well as internalhealth benefits. These measurable indicators include improved nail appearance and healthierosteoporosis-resistant bones. A new clinical study shows that in just 20 weeks, shallow wrinkles

improved by up to 30% and skin elasticity improved by 55%, as well as a significant reduction ofbrittleness in nails and hair. Also, we have new information as to how silicon works to bring aboutthese benefits.

I have invited silicon experts, Professor Dirk Vanden Berghe of the University of Antwerp (Belgium)and Professor Andre Barel of the Free University of Brussels (Belgium) to discuss their research withus. In this two-part discussion, we will look at how skin health indicates the health of internal organs

and blood vessels and how silicon is critical to skin health. In Part 1, well review the role of silicon ingiving skin its healthy, youthful look, and in Part 2 well discuss the clinical results of this newstudythat show that silicon supplementation as choline-stabilized orthosilicic acid (ch-OSA) reduceswrinkling and improves skin and nails

In December, we had a conversation with Dr. Vanden Berghe about the essentiality of silicon to

humans. He informed us about how silicon is a main support element for life and how silicon isimportant to the strength of our blood vessels, organs, skin, hair and bones. We discussed how thebiologically active form of silicon, choline-stabilized orthosilicic acid (ch-OSA), provides chemical linkswithin and between polysaccharide chains of glycoaminoglycans (GAG) including glucosamine,hyaluronic acid, chondroitin sulfate and other GAG.

These silicon links formed by ch-OSA are important not only to structural strength, but also to skinhealth. Skin health is dependent of skin nourishment which is effectively achieved by dietary ch-OSA.Skin beauty on the surface (epidermis) is determined by the underlying tissue (dermis andhypodermis). Many people are silicon-deficient which results in rough, dry and wrinkled skin. It is agood practice to regularly use moisturizing lotions, aged and dry skin is help comparatively littlecompared to what can be achieved by internal nourishment. As people age, their skin usuallydecreases in silicon content due to diet. This appears to be a major contributing factor to dry skin andwrinkling.

What we perceive as beautiful skinis skin that is smooth and resiliently tight (elastic). This is afunction of collagen (the main skin protein) and water content. Collagen production is not merely amatter of eating the right proteins and amino acids, but also the nutrients that facilitate collagenproduction such as silicon and vitamin C. The collagen should be properly supported with silicon-based links and aldehyde links, and not improperly cross-linked by random free-radical damage. So,

skin collagen and water content are silicon-dependent. The questions we examine here are willsilicon supplementation slow wrinkling and decrease existing wrinkles.

Dr. Vanden Berghe is a professor on the Faculty of Pharmaceutical, Biomedical and VeterinarySciences at the University of Antwerp in Belgium. He is also the holder of various international patents

on antimicrobial compounds and food supplements and has authored more than 250 internationalpublications with peer review. Professor Vanden Berghe is also an internationally recognized experton the biological activities of flavonoids and other natural compounds.


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Prof. AndrO. Barel is Head of the Laboratory of General and Biological Chemistry and professor ofChemistry, Biochemistry, Oral Biochemistry, and Cosmetic Sciences, at the Faculty of PhysicalEducation and Physiotherapy, Free University of Brussels (VUB), Belgium. He is the author ofnumerous book chapters, publications, and abstracts in dermato-cosmetic sciences and is a memberof the executive committee of theInternational Society for Bioengineering and the Skinand

theSocitFrancophone d'Ingrie Cutane. He is also a consultant for internationaldermatological and cosmetic companies.

Passwater and Passwater: What is the importance of realizing that a deficiency in silicon can beindicated by skin health?

VANDEN BERGHE: First of all it should be mentioned that skin health itself is very important. Many

health problems are reflected in the skin. The skin is the largest organ in the body. An adults skin is15 to 20 percent of total body weight. Skin performs several vital functions. Foremost, it serves as aprotective barrier between internal organs and external environment. Healthy skin impedes thepenetration of microorganisms which can cause infections and protects against irritants.

A good support of skin by the underlying connective tissue is essential for skin function. Connectivetissue is composed of cells which produce the fibrous protein matrixes of collagen and elastin, as wellas the hydrated (water retaining) network of amino-sugars called glycosaminoglycans (GAG). Silicon

is an essential element of this connective tissue as it determines the quality of the cells connected withits structure

[1].Furthermore, silicon is required for the structural integrity of connective tissue which

was demonstrated in the 1970s by Drs. Carlisle1and Schwarz

[2]where silicon is believed to act as a

cross-linking agent which stabilizes the glycosaminoglycan network.

To answer your question, because of the importance of silicon to the formation of connective tissue,fibroblasts and collagen

[3];signs of silicon deficiency can be observed as skin, hair and nails

deterioration such as aged skin, increased hair fall-out and brittle, dry nails.

Passwater and Passwater: Dont laugh, but technically, just what are wrinkles? Yes, we all knowwhat they look like and we know one when we see one. But, Dr. Barel, what is different about wrinkledskin compared to healthy non-wrinkled skin?

BAREL: Wrinkles are modifications of the skin surface occurring with age. The severity of thesechanges in an individual depends on genetic tendency, skin photo- type and exposure toenvironmental factors. Wrinkles arise because of a modification in dermis structure (less collagenversus young skin) and because of a decrease in the amount of water held by the epidermis.

Passwater and Passwater: Scientists studying skin refer to wrinkles and microwrinkles. Just what is a

microwrinkle?What is the difference between skin roughness,microrelief,fine linesandmicrowrinkles.

BAREL: The relief of the skin surface reflects the three-dimensional organization of the epidermis,dermis and the subcutaneous tissue. The skin microrelief is not visible with the eye but comprises a

number of lines (primaryandsecondarylines) which can be classified according to their

depth (generally in microns) and respective orientation.

These micro lines or micro wrinkles can become the location for the macro lines or wrinkles (depth of

12 mm), also known as the macrorelief. There is no precise classification of the different types ofwrinkles, and different names (lines, furrows) are used as a synonym for wrinkles in conjugation with

the adjectives fine, small, thinto better qualify them.

Skin roughness, in a physical sense, means a surface with lines of certain width and depth that can bequantified by roughness parameters. Thus, aging skin with fewer and deepened lines will be definedrougher, although it is not necessarily rough to touch.

Passwater and Passwater: Most people think of wrinkles as being caused by aging. However, time

alone has no effect on skin. Time is merely the fourth dimension. All people of the same age do nothave identically wrinkled skin. The exposure of skin to sunlight increases free radical damage and thecross-linking of skin proteins. The damage resulting from these reactions between ultraviolet energy
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from the sun and skin proteins accumulate over time. Its a product of the rate of reactions (intensity)and length of time of exposure. Antioxidant deficiency also increases the rate of wrinkling.

What does silicon have to due with reducing wrinkling?

VANDEN BERGHE: It is important both to have a good skin structure and to prevent damage to thatstructure. While sun can damage skin, so can the lack of underlying structure in the first place. Whenthe support structure (e.g. connective tissue) of the skin begins to collapse, this causes wrinkles andlines. Biological silicon in the form of choline-stabilized orthosilicic acid (ch-OSA) is very important toskin structure. Skin is dependent on silicon for producing its skin proteins and maintaining its watercontent, but I will come to that in detail later. Poor quality skin, deficient in collagen and lacking water,has poor underlying structure which results in wrinkles.

Passwater and Passwater: We have long known from animal studies that silicon is important tocollagen production. This has been from basic gross observational studies. Have we learned moredetails about the biochemistry involved?

VANDEN BERGHE: Our understanding of silicon biochemistry is growing. Animal studies haveshown that silicon deficiencies cause collagen deficiencies including bone deformities

[4],[5].Cell culture

studies[6]

are helping us understand some of the roles of silicon-dependent enzymes[7]

,observational

trials showing favorable correlations between silicon consumption and connective tissue health andintervention trials supplementing animals

[8],[9],[10],[11]with silicon are also yielding favorable results

associated with connective tissue health. Furthermore, recent research shows that silicon influencesTNF-a and hence collagen gene promoter activity

[12].

As an example, Figure 1 illustrates the results from one of our previous animal studies showing wherea five percent increase in dietary silicon as stabilized ch-OSA biologically amplifies collagen productionby 12 percent

11in the dermis.

Passwater and Passwater: Well that explains why a little extra ch-OSA has such a big effect on skin.The fact that silicon affects the enzymes that produce collagen, rather than becomes a part of collagenstructure, explains this biological amplification. For years we have looked for silicon-containingcompounds within collagen. We were looking for instances where silicon atoms replaced certain

carbon atoms in collagen. We reasoned that since silicon carbon bonds were stronger than carbon-carbon bonds, then silicon atoms substituting for carbon atoms in the amino acids that make up

collagen would make the collagen stronger, and thus, the skin better. Well come back to this pointlater.

We have learned of the relationship between silicon and enzyme activity only in the past few years.Enzymes are not consumed in reactions but serve as reusable catalysts that cause the reactions tooccur. So enzymes repeat their task over and over. In the case of collagen, the needed quantity of twoenzymes required for collagen production are small in comparison to all of the collagen that theymake. But, if the actions of these two enzymes are impaired by silicon deficiency, the difference incollagen production can be great. Conversely, a small amount of additional dietary ch-OSA tostimulate or facilitate the efficiency of these two enzymes can significantly improve collagen

production.

Before we look at this new information closer, lets start at the beginning with the role of collagen inskin health. Please elaborate on why collagen production is important to the health, look and feel ofskin. Where is collagen produced? Epidermis, dermis or Hypodermis?

BAREL: Figure 2 is a cross sectional view of the skin showing the epidermis, dermis and hypodermis.A skin cell, formed in the basal layer (a single layer of basal cells) migrates upwards for about twoweeks until it reaches the upper layer of the skin, known as the epidermis. The cell spends anothertwo weeks in the epidermis, gradually flattening out and continuing to move upwards. Then the skin

cell dies and is shed off the surface. Two to three billion skin cells are shed every day in fact, theymake up a substantial percentage of household dust.
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Collagen is produced in the dermis by fibroblasts and influences the maturation of the dermis.Collagen makes up 25 to 35% of the total protein of mammals. It has greattensile strength,and is themain component ofligamentsandtendons.Collagen forms long molecular cables that strengthentendons and the vast, resilient sheets of connective tissue that support the skin and internal organs.

Collagen molecules assemble themselves into ordered polymers called collagen fibrils. Figures 3 and4 show how collagen molecules are intertwined to form fibers that form a matrix. All contain a longstretch of triple helix connected to different types of ends. The simplest is merely a long triple helix,

with blunt ends.

As mentioned before silicon is important for optimal collagen synthesis and crucial for activating thehydroxylation enzymes for cross linking collagen, which improves the strength of collagen. Collagen is

actually a family of proteins that act as aglueto hold the body together. There are at least 19different types of collagen proteins known and each type has a different molecular composition andshape. These collagen family members are simply designated as type I, type II. etc. The main types ofcollagen found in skin and connective tissue are types I, II, III, V and XI, with type I being the principalcollagen found in skin and bone and by far the most common in the body. These have rope-like

structures and are calledfibrillar collagens.These fibrillar collagens associate side-by-side, likefibers in a rope, to form tough fibrils. These fibrils crisscross the space between nearly every one ofour cells.

About one-sixth of the body consists of spaces between cells. This space is called the interstitium andthe gel-like fluid that fills this space is called interstitial fluid. Collagen fibers extend long distances inthe interstitium. These collagen fibers provide most of the tensional strength of the tissues.

As Figures 3 and 4 show, collagen is composed of three chains, wound together in a tight triple helix.The collagen chain is over 1400 amino acids long essentially consisting of repeated sequences of

three amino acidsproline, hydroxyproline and glycine. Other amino acids, including hydroxylysine,are also found in different types of collagen, thereby giving the various types of collagen their specificshapes.

Because both proline and hydroxyproline are rigid, cyclic amino acids, they limit rotation of the proteinbackbone and thus contribute to the stability of the triple helix. Hydroxyproline has an essential role in

stabilizing the triple helix of collagen by hydrogen bonding between the hydroxyl groups and water.Hydroxyproline is created by modifying normal proline amino acids after the collagen chain is built.The reaction requires vitamin C to assist in the addition of oxygen, and as we have learned recently, italso is dependent on silicon.

Passwater and Passwater: Now lets go back and look at some of the new information. Tell us moreabout how silicon is involved in the production of collagen. Our understanding of silicons role in skinhealth has been hampered because many of us have always been looking for specific structuralcompounds that intrinsically contain silicon atoms. This is particularly true of blood vessels. Fordecades we have had evidence that silicon nourishment leads to healthier and stronger blood vessels.Yet, when we looked for silicon structural compounds, all that could be found were OSA and itschains. (Please see Figure 5)

We didnt understand that these OSA chains were strong linking agents having hydrogen bonds thatstrongly crosslink collagen fibers. Seeing OSA and its chains in the tissue was akin to seeing nitricoxide in the blood and not understanding that it was an important biochemical messenger that plays arole in many biochemical functions. Now we understand that nitric oxide is important in blood vesselrelaxation, as well as in memory and attention. Once considered irrelevant because of its molecularsize and not a structural component, nitric oxide is now known as an extremely important molecule.Perhaps, as our understanding of OSA increases, so will the value we place on silicon.

Please elaborate more about how silicon improves skin without forming a silicon-containing-aminoacid such as silaproline or silahydroxyproline, or complex silicon-containing structural molecules thatbecome interwoven with collagen.
http://en.wikipedia.org/wiki/Tensile_strengthhttp://en.wikipedia.org/wiki/Tensile_strengthhttp://en.wikipedia.org/wiki/Tensile_strengthhttp://en.wikipedia.org/wiki/Ligamenthttp://en.wikipedia.org/wiki/Ligamenthttp://en.wikipedia.org/wiki/Ligamenthttp://en.wikipedia.org/wiki/Tendonhttp://en.wikipedia.org/wiki/Tendonhttp://en.wikipedia.org/wiki/Tendonhttp://en.wikipedia.org/wiki/Tendonhttp://en.wikipedia.org/wiki/Ligamenthttp://en.wikipedia.org/wiki/Tensile_strength


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VANDEN BERGHE: There are a lot of studies that confirm the stimulating effect of silicon on collagensynthesis. Even more, there seems to be a connection between silicon and those cells in the extracellular matrix responsible for collagen synthesis where silicon is essential for the quality of these cellsergo for the quality of their product of synthesis, the connective tissue.

Now how is silicon involved? This is our proposed dual action of silicon[13]

:1) silicon as choline-stabilized orthosilicic acid is absorbed in the gut from diet. ch-OSA is a neutral molecule inphysiological conditions, it does not easily cross cell membranes by simple diffusion and flows through

the body in the presence of water. ch-OSA can only become activatedin the proteoglycan sacs ofthe connective tissue. Connective tissue is composed of cells (fibroblasts, chondrocytes, osteoblasts,

osteocytes, tenocytes,) which produce the fibrous protein matrixes of collagen and elastin, as wellas the hydrated (water retaining) network of amino-sugars called glycosaminoglycans (GAG). These

GAGs are negatively charged due to the presence of sulfate and acidic groups. Furthermore theyform covalent bonds with a protein core what leads to the formation of a proteoglycan sac. These

negatively charged GAGs attract water, cations (such as K+, Ca

2+and H

+) and positively charged

polyamines. ch-OSA, only present in the water, is also attracted by the GAGs and diffuses into theproteoglycan sac. Due to the flux of cations the negative charges of the GAGs are partiallyneutralized resulting in polarization or activationof ch-OSA.Activatedch-OSA attaches topositive charged ions and to the positive charged aminosugars (arginine, lysine, histidine) and to thehydroxylated amino acids (serine, threonine, tyrosine). This leads to associations of ch-OSA, resulting

in cross linkage of the GAGs to a strong network with a water retaining capacity essential for a goodworking connective tissue. 2) Furthermore this activatedch-OSA can be easily picked up by thecells in the connective tissue, where it stimulates the collagen synthesis.

A: The dual action of ch-OSA:

(1) Silicon is necessary for the formation of the water-retaining network of GAGs . This isrealized by conversion of neutral toactivatedch-OSA in the strong negativelyenvironment of the GAGs in the proteoglycan sac.

(2) Activatedch-OSA enters the cell and stimulates the synthesis of collagen and othercomponents of the connective tissue.

B: The proteoglycan sac in detail:

The micro environment of the proteoglycan in the connective tissue can be viewed as a sac composed

of GAGs attached to a core protein. These GAGs are negatively charged due to the presence ofsulfate and acidic groups.

Passwater and Passwater: As we mentioned earlier, hydroxyproline is an amino acid that is animportant component of collagen. The body can make proline which must be converted intohydroxyproline in the collagen structure to make proper collagen. Proline is not a dietary essentialamino acid, as it can be produced in the body from the dietary essential amino acid glutamate. Nowhydroxyproline is a story within itself. We always find hydroxyproline interesting. It is unusual to saythe least.

Hydroxyproline is found in the major protein collagen and only very rarely found in other proteins, butwhat is more interesting is that hydroxyproline is formed from proline only afterthe proline has beenincorporated into proteins.

What we especially find peculiar is that hydroxyproline is not coded for by DNA; it is produced byhydroxylation of the amino acid proline, yet it is essential for proper functioning of collagen. This would

mean that our genes arent programmed for producing hydroxyproline, yet skin requires it anddietary hydroxyproline is of no value in supplying hydroxyproline because it appears thathydroxyproline cannot be directly incorporated into collagen. Instead, proline must first be incorporatedinto pro-collagen and then converted into hydroxyproline on the growing polypeptide chain. No wonderthere are so many collagen-related diseases. About half of the proline is converted into

hydroxyproline. Dietary hydroxyproline is converted into glyoxalate, pyruvate and ketoglutarate, ratherthan incorporated into proteins (Figure 7). So eating a lot of chicken skin for its hydroxyproline content

or taking hydroxyproline supplements or cream wont help much in terms of hydroxyproline forcollagen synthesis.
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There are two forms of hydroxyproline in collagen, 3-hydroxyproline and 4-hydroxyproline. These areformed with the aid of the enzymes, prolyl 3-hydroxyproline and prolyl 4-hydroxyproline. Proline ismostly converted to 4-hydroxyproline with some converted to 3-hydroxyproline. Vitamin C is anessential cofactor for both prolyl hydroxyproline enzymes, as are iron, oxygen and alpha-ketoglutarate.Unlike an enzyme, vitamin C actually contributes portions of its structure to the process, but it gainsthat portion back through a recycling process with other compounds. Vitamin C is not just a reducingcompound, but actually a redox couple (ascorbic acid / dehydroascorbic acid), which can undergo

cycling. It is believed that in this reaction, the role of vitamin C is to maintain the enzymes iron co-

factor in a reduced state at the active site. The reaction may proceed via the intermediate formation ofa peroxyglutarate reacting with proline.

And, now you are telling us that silicon is involved with these enzymes as well. This is important,because without the conversion of certain proline residues in the pro-collagen fibrils intohydroxyproline, the fibrils can not be bundled into the collagen stable triple helix, nor can they formnormal fibers. If pro-collagen is not properly hydroxylated, the fibrils are degraded within the cell.

Two other enzymes are involved with the conversion of the amino acid lysine in some types ofcollagens into hydroxylysine to form the proper structure within those types of collagen. The enzymesgalactosyl-hydroxyllysyl glucosyltransferase and lysyl oxidase have also been shown to involve siliconby Dr. Poole and colleagues in 1985.

The assembly of collagen fibers begins in a part of the cell called the rough endoplasmic reticulum,continues in the Golgi complex and is completed outside the cell. Several modifications to the pro-collagen chains must be made before the triple helix can be formed in the rough endoplasmicreticulum.

It is well known that a lack of vitamin C in the diet can cause the skin lesions, fragile tendons andporous blood vessels of scurvy. This is because vitamin C is needed for collagen production, yetvitamin C is not part of collagen. Vitamin C is required for hydroxyproline production as a key cofactorin the enzymatic conversion of some of the proline incorporated into collagen precursor molecules intohydroxyproline step in collagen formation. Now, we know that silicon is involved as well. Although theenzyme contains copper, it is not activated by copper but by silicon through a mechanism that is notyet understood. This was first report by Dr. Edith Carlisle in 1986 and confirmed by Dr. Forrest H.

Nielsen in 1996.

VANDEN BERGHE: Yes, according to cell culture studies, the activity of prolyl hydroxylase, theenzyme required for the hydroxylation of proline to form hydroxyproline, is dependent on silicon; thuscollagen synthesis is silicon-dependent.

In 2002, Drs. C. D. Seaborn and F. H. Nielsen10

published their study in which they implanted polyvinylsponges beneath the backs of laboratory rats to monitor collagen formation. They found that in silicondeficient rats less hydroxyproline was deposited on the sponges compared to rats on a normal diet.This shows that silicon deprivation decreases collagen formation which is associated with woundhealing.

Earlier you mentioned that proline was not dietary essential as it can be produced in the body fromglutamate. It can also be produced via the ornithine pathway. Recent evidence implies that there is awidespread potential for proline synthesis from ornithine. Well, the activity of ornithineaminotransferase, an important enzyme of the ornithine pathway leading to the formation of prolineand thus collagen formation, was lower in silicon-deficient rats compared to silicon-adequate rats

10.

In our calves study11

we measured the hydroxyproline concentration in the dermis of animalssupplemented with ch-OSA and a control group given a placebo. The hydroxyproline concentrationwas statistically higher in the ch-OSA group. In skin both collagen type III and type I is found.

Passwater and Passwater: OK, professors, your biochemical review of the role of silicon in skin leads

us to the point,what are the results of your clinical study?Lets take a look at the study in theJune issue.

2005 Whole Foods Magazine and Richard A. Passwater, Ph.D.This article is copyrighted and maynot be re-produced in any form (including electronic) without the written permission of the copyrightowners.


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[1]Carlisle (1974) Silicon as an essential element. Federation Proceedings, 33: 1758-1766.

[2]Schwarz (1973) A bound form of silicon in glycosaminoglycans and polyuronides. Proc Natl Acad

Sci USA, 70(5): 1608-1612.

[3]

Carlisle (1986) Silicon as an essential trace element in animal nutrition, Silicon Biochemistry, Wiley,Chichester: 123-139.

[4]Carlisle (1976) In vivo requirement for silicon in articular cartilage and connective tissue formation in

the chick, J. Nutr., 106:478-484.

[5]Carlisle (1980) A silicon requirement for normal skull formation in chicks, J. Nutr., 110:352-359.

[6]Valerio et al. (2004) The effect of ionic products from bioactive glass dissolution on osteoblast

proliferation and collagen production, Biomaterials, 25: 2941-2948.

[7]Reffitt et al. (2003) Orthosilicic acid stimulates collagen type 1 synthesis and osteoblastic

differentiation in human osteoblast-like cells in vitro, Bone, 32: 127-135.

[8]Seaborn and Nielsen (2002) Silicon deprivation and arginine and cystine supplementation affect

bone collagen and bone and plasma trace mineral concentrations in rats, J. Trace Elem. In Exp. Med.,15(3): 113-122.

[9]Nielsen and Poellot (2004) Dietary silicon affects bone turnover differently in ovariectomized and

sham-operated growing rats, J. Trace Elem. In Exp. Med., 17(3): 137-149.

[10]Seaborn and Nielsen (2002) Silicon deprivation decreases collagen formation in wounds and bone,

and ornithine transaminase enzyme activity in liver, Biol. Trace Elem. Res., 89: 251-261.

[11]Calomme et al. (1997) Supplementation of calves with stabilized orthosilicic acid, Biol. Trace Elem

Res, 56: 153-165.

[12]Hull et al. (2004) Low dietary silicon increases TNF-alpha and collagen gene promoter activity in

mice, Experimental Biology, Abstract 364.5.

[13]Vanden Berghe (2005) Proposed action of silicon, internal discussion.
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