Are Your Fibroblasts Creating Adequate Collagen?

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A fibroblast is the most common type of cell found in connective tissue. Fibroblasts creates and secretes collagen proteins that are used to maintain a structural framework for many tissues.

The aging process interferes with the number of fibroblasts as well as the process and functionality of existing fibroblasts in the skin. [1] Between birth and the age of 80, fibroblasts can decrease by at least 50%.

Cross-linking and glycation can also destroy the fibroblasts in the skin. [2]

Enhancing the function of fibroblasts is very important and there are a number of identified substances that can be consumed to accomplish this goal.

Table:  Nutraceuticals and Herbs that Enhance the

Function of Fibroblasts        

Fibroblasts

 

 

Category

Nutraceuticals and Herbs

References

Amino Acids

 

 

 

Arginine

 A

 

Glutamine

 B

Herbs

 

 

 

Gotu Kola

 C

 

Green Tea

 D

 

Ginko Biloba

 E

 

Indian Gooseberry (Amla)

 F

Hormones

 

 

 

Melatonin

 G

Minerals

 

 

 

Magnesium

 H

Peptides

 

 

 

Carnosine

 I

Vitamins

 

 

 

Vitamin B3

 J

 

Vitamin B5

 K

 

Vitamin C

 L

Collagen is Created by Fibroblasts

Collagen is the main structural protein in the extracellular space in the various connective tissues.

CollagenTripleHelix

Collagen Triple Helix

Collagen is mostly found in:

  • Blood vessels
  • Bones
  • Cartilage
  • Corneas
  • Dentin in teeth
  • Endomysium
  • Gut
  • Intervertebral discs
  • Ligaments
  • Muscle tissue
  • Skin
  • Tendons

Collagen is an important building block in the body. It comprises:

  • 25% – 35% of the protein of the body
  • 75% of the protein of the skin
  • 2% of muscle tissue
  • 6% of tendinous muscles
  • 30% of bone
  • 40% of blood vessels
  • 90% of ligaments
  • 80% of tendons
  • 70% of cartilage

There are 28 types of collagen that have been identified.  The five most common types are:

  • Type I: skin, tendon, vascular ligature, organs, bone (main component of the organic part of bone)
  • Type II: cartilage (main collagenous component of cartilage)
  • Type III: reticulate (main component of reticular fibers), commonly found alongside type I.
  • Type IV: forms basal lamina, the epithelium-secreted layer of the basement membrane.
  • Type V: cell surfaces, hair and placenta

Collagen contains 18 amino-acids, including 8 out of 9 essential amino-acids. It is characterized by the predominance of glycine, proline and hydroxyproline, which represent about 50% of the total amino-acid content.

  • Glycine
  • Proline
  • Alanine
  • Hydroxyproline
  • Glutamic acid
  • Arginine
  • Aspartic acid
  • Serine
  • Lysine
  • Leucine
  • Valine
  • Threonine
  • Phenylalanine
  • Isoleucine
  • Hydroxylysine
  • Methionine
  • Histidine
  • Tyrosine
  • Cysteine

The most common collagen polypeptide chain in the amino acid sequence of collagen are glycine-proline-X and glycine-X-hydroxyproline. Lysine, in its pure form or modified to hydroxylysine, is also found in collagen. Glycine is found at almost every third residue. Proline makes up about 17% of collagen.

Collagen contains two uncommon derivative amino acids not directly inserted during translation. These amino acids Hydroxyproline derived from proline and Hydroxylysine derived from lysine

Both hydroxyproline and hydroxylysine are formed via the enzyme-catalyzed oxidations of the proline and lysine amino acid side chains, which occur after the collagen polypeptide has been synthesized. These enzymatic reactions require as cofactors:

  • Ascorbic acid (Vitamin C)
  • Silicon

The Importance of Silicon as a Cofactor in Collagen Synthesis

Orthosilicic Acid (also known as Monomeric Silica) (Si(OH)4) is a soluble form of Silicon that has been shown to be highly bioavailable. Orthosilica Acid consists of 3% elemental Silicon (as Orthosilicic acid) in a solution of 70 percent choline, HCl and water. It is known as Choline-stabilized orthosilicic acid.

Choline-stabilized orthosilicic acid has been shown to be a superior form of bioavailable silicon for collagen synthesis. In a study conducted in 1997 by M.R. Calomme, they

“demonstrated that orthosilicic acid was more effective than food for increasing silicon levels in the bloodstream in in collagen sythesis. Experimental and control calves were fed a standard milk formula containing normal levels of silicon for 23 weeks. One group of calves was given an additional 280 – 380 mg of orthosilicic acid per gram of body weight twice per day. The dosage was increased as the calves grew. At the end of the study the silicon levels in the blood of calves receiving orthosilicic acid was 70% higher than that of controls. Skin collagen content was significantly greater in calves receiving orthosilicic acid.” [3] [4]

Hydrolyzed Collagen

Ingesting hydrolyzed collagen, which is the common form of collagen products, has been substantiated in allowing the fibroblasts in producing collagen. [5] The hydrolyzed collagen contains all of the amino acids that comprise collagen so when ingesting it will provide the fibroblasts with the necessary amino acids to create collagen.

It is important to note that the cofactors that fibroblasts use to create collagen must also be consumed with the hydrolyzed collagen, namely Vitamin C and Choline-stabilized orthosilicic acid in order for complete synthesis of collagen.


References:

[1] Marked aging-related decline in efficiency of oxidative phosphorylation in human skin fibroblasts

[2]Effect of advanced glycation end-products on cell proliferation and cell death

[3] Calomme, M. R., et al. Supplementation of calves with stabilized orthosilicic acid. Effect on Silicon, Ca, Mg, and P concentrations in serum and the collagen concentration in skin and cartilage. Biol Trace Elem Res. 56:153-165, 1997.

[4] Biological and therapeutic effects of ortho-silicic acid and some ortho-silicic acid-releasing compounds: New perspectives for therapy

[5] Matsuda, N.; Koyama, Y., Hosaka, Y., Ueda, H., Watanabe, T., Araya, T., Irie, S. and Takehana K. (2006). “Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis”. Journal of nutrition vitaminology 52 (3): 211–215. doi:10.3177/jnsv.52.211

Postlethwaite, A.E.; Seyer, J.M.; Kang, A.H. (1978). “Chemotactic attraction of human fibroblasts to type I, II, and III collagens and collagen-derived peptides”. Proc Natl Acad Sci USA 75 (2): 871–875. doi:10.1073/pnas.75.2.871. PMC 411359. PMID 204938.

Shigemura, Y.; K Iwai; F Morimatsu; T Iwamoto; T Mori; C Oda; T Taira; EY Park; Y Nakamura; K Sato (2009). “Effect of prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin”. Journal of Agricultural and Food Chemistry 57 (2): 444–449. doi:10.1021/jf802785h. PMID 19128041


Resources:

BioSilTM

Vital ProteinsTM – Collagen Peptides


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