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Elastin and Keratin
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Elastin is secreted by the fibrocytes of the connective tissues into the intercellular network. In the dermal connective tissue, the elastin fibers are thin and sinuous. Elastin contained in the dermis represents 5% of its dry weight. In the arteries around the heart it represents 35 or 40%. Elastin is a large fibrous protein which is formed by spiral filaments than can be compared to springs. The spiral filaments consist of peptidic chains that can stretch out. The peptidic chains are connected to each other by very specific amino-acids: desmosin and isodesmosin, which builds between them, giving the molecule a reticular aspect. After stretching out, the molecules resume their original shape due to this cross linking which is essential to molecular elasticity.

Elastin serves an important function in arteries as a medium for pressure wave propagation to help blood flow and is particularly abundant in large elastic blood vessels such as the aorta. Elastin is also very important in the lungs, elastic ligaments, the skin, and the bladder, elastic cartilage. It is present in all vertebrates above the jawless fish.

With aging, the elastic fibers progressively degenerate and separate into fragments. The skin progressively loses its elasticity and lines and wrinkles start appearing. This damage to our elastic tissue cannot be avoided and is part of our natural (physiological) aging process. This process begins relatively early but accelerates considerably after age of 40.

Elastin owes its properties to its thin structure which resembles that of rubber. Professor Ladislas ROBERT defines it as the rubber of the organism. Elastin is the protein responsible for our skin’s essential elasticity and tonicity. Its decrease means aging and it can be said that ‘we are as old as our elastic fibers’. As we age, we stop producing elastin for our skin. The skin starts sagging, allowing lines, folds and wrinkles to appear and grow. This is the reason why Elastin is of the utmost importance in dermo-cosmetology as it can compensate for the loss of elastic matter in the strata of the dermis.

Keratin is an extremely strong protein which is a major component in skin, hair, nails, hooves, horns, and teeth. The amino acids which combine to form keratin have several unique properties, and depending on the levels of the various amino acids, keratin can be inflexible and hard, like hooves, or soft, as is the case with skin. Most of the keratin that people interact with is actually dead; hair, skin, and nails are all formed from dead cells which the body sheds as new cells push up from underneath. If the dead cells are kept in good condition, they will serve as an insulating layer to protect the delicate new keratin below them.
Keratin is difficult to dissolve, because it contains cysteine disulfide, which means that it is able to form disulfide bridges. These disulfide bridges create a helix shape that is extremely strong, as sulfur atoms bond to each other from across the helix, creating a fibrous matrix which is not readily soluble. Depending on how much cysteine disulfide keratin contains, the bond can be extremely strong to make hard cells like those found in hooves, or it can be softer to make flexible keratin like hair and skin. Because of the high levels of sulfur in keratin, when it is burned it emits a distinct sulfurous odor which some people find distasteful.

Keratin is formed by keratinocytes, living cells which make up a large part of skin, hair, nails, and other keratin containing parts of the body. The cells slowly push their way upwards, eventually dying and forming a protective layer of cells. Thousands of these cells are shed every day, and the process can be accelerated by various medical conditions, such as psoriasis. Damage to the external layer of keratin can cause skin, hair, and nails to look unhealthy or flaky.
Hair and nails on humans especially tend to become dry and brittle, because the dead keratin is being pushed to great lengths. By eating foods like gelatin and keeping hair and nails moist, they can be grown out while still remaining healthy. In general, the thicker the layer of keratin, the healthier the hair or nail is, because the dead cells outside protect the living cells at the core. Keeping the external layer of keratin moisturized will also keep it healthy and prevent cracking and splitting, whether the keratin is forming the hooves of a horse of the skin of a human.

What is Elastin / Keratin?
Elastin is a protein in connective tissue that is elastic and allows many tissues in the body to resume their shape after stretching or contracting. Elastin helps skin to return to its original position when it is poked or pinched. Elastin is also an important load-bearing tissue in the bodies of mammals and used in places where mechanical energy is required to be stored. In humans, elastin is encoded by the ELN gene.

Keratin refers to a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human skin. It is also the key structural component of hair and nails.

How is it Made?
The biosynthesis of Elastin begins with the embryonic period and continues till we reach adulthood. Our body stops producing Elastin around that time in our lives. Our natural Elastin is no longer renewed.

Where is it Found?
The elastin in anti-aging products is typically taken from birds and cows with the theory that it can improve human skin elasticity by application.

Benefits / Uses
Collagen and elastin are needed to repair and maintain the walls of the circulatory system. Veins, arteries and capillaries are all dependant on vitamin C to maintain their strength and integrity. If you don't get enough, then your body starts using cholesterol to make repairs. Cholesterol creates a more rigid, fragile repair than collagen and elastin do. Collagen and elastin make flexible soft repairs. Maintaining a regular intake of vitamin C helps your body to keep its arterial walls healthy.

Ingestible collagen does work better because of a more effective method of delivery. What goes into your stomach passes quickly into the bloodstream where it can then be carried to the areas that are most in need of the repair and maintenance that these tissues can provide. One has to understand that the material that goes into these collagen supplements is same one that not only maintains the structural integrity of your skin but they are also the material that the cardiovascular system and organ walls are made from.

This is the reason that when the production centers of the body begin to produce increasingly lower amounts of this structural tissue, it is the skin that suffers the most. The only types of collagen supplements that will accomplish this are the ones that have functional keratin in them. This is unique blend of keratin proteins which have been proven to stimulate a dramatic increase in the body’s output of both collagen and elastin. Functional keratin is capable of giving all of the collagen and elastin that is needed for skin to become fuller, firmer and wrinkle-free.

Possible Side-Effects / Precautions / Possible Interactions
There are no side-effects of elastin, keratin noted till now.

Research Studies / References

arw Curran ME, Atkinson DL, Ewart AK, Morris CA, Leppert MF, Keating MT (April 1993). "The elastin gene is disrupted by a translocation associated with supravalvular aortic stenosis". Cell 73 (1): 159–68. PMID 8096434.


arw Kielty CM, Sherratt MJ, Shuttleworth CA (July 2002). "Elastic fibres". J. Cell. Sci. 115 (Pt 14): 2817–28. PMID 12082143.

arw Sage EH, Gray WR (1977). "Evolution of elastin structure". Adv. Exp. Med. Biol. 79: 291–312. PMID 868643

arw Uittom J, Rosenblom. Elastic fibers. In: Freedberg IM, Eisen AZ, Wolff K, et al., eds. Fitzpatrick's Dermatology in Internal Medicine. 5th ed. New York: McGraw-Hill; 1999: Chap 20.

arw Bernstein EF and Uitto J. The effect of photodamage on dermal extracellular matrix. Clin Dermatol 1996; 14:143-151.

arw Mecham RP and Davis EC. "Elastic fiber structure and assembly" In: Extracellular Matrix Assembly and Structure. Yurchenco PD, Birk DE, and Mecham RP, eds. Academic Press:San Diego, 1994, pp. 281-310

arw Hickman, Cleveland Pendleton; Roberts, Larry S.; Larson, Allan L. (2003). Integrated principles of zoology. Dubuque, IA: McGraw-Hill. p. 538. ISBN 0-07-243940-8.

arw Kreplak L, Doucet J, Dumas P, Briki F (2004). "New aspects of the alpha-helix to beta-sheet transition in stretched hard alpha-keratin fibers". Biophys J 87 (1): 640–7. doi:10.1529/biophysj.103.036749. PMID 15240497.


arw Voet, Donald; Voet, Judith; Pratt, Charlotte, "PROTEINS: THREE-DIMENSIONAL STRUCTURE", Fundamentals of Biochemistry, p. 158,, retrieved 2010-10-01, "Fibrous proteins are characterized by a single type of secondary structure: a keratin is a left-handed coil of two a helices"

arw "Secondary Protein".'chm/vchembook/566secprotein.html. Retrieved 2010-09-23.

arw Schweizer J, Bowden PE, Coulombe PA, Langbein L, Lane EB, Magin TM, Maltais L, Omary MB, Parry DA, Rogers MA, Wright MW. New consensus nomenclature for mammalian keratins. J Cell Biol. 2006 Jul 17;174(2):169-74.

arw Schweizer J, Bowden PE, Coulombe PA, et al. (July 2006). "New consensus nomenclature for mammalian keratins". J. Cell Biol. 174 (2): 169–74. doi:10.1083/jcb.200603161. PMID 16831889. PMC 2064177.

arw Australia. "Spiders - Silk structure". Retrieved 2010-09-23.

arw Shiratsuchi H, Saito T, Sakamoto A, Itakura E, Tamiya S, Oshiro Y, Oda Y, Toh S, Komiyama S, Tsuneyoshi M. Mutation analysis of human cytokeratin 8 gene in malignant rhabdoid tumor: a possible association with intracytoplasmic inclusion body formation. Mod Pathol 2002;15:146-53.

arw Itakura E, Tamiya S, Morita K, Shiratsuchi H, Kinoshita Y, Oshiro Y, et al. Subcellular distribution of cytokeratin and vimentin in malignant rhabdoid tumor cells: three-dimensional imaging with confocal laser scanning microscopy and double immunofluorescence. Mod Pathol 2001; 14: 854–861.

arw Omary MB, Ku NO, Strnad P, Hanada S (July 2009). "Toward unraveling the complexity of simple epithelial keratins in human disease". J. Clin. Invest. 119 (7): 1794–805. doi:10.1172/JCI37762. PMID 19587454. PMC 2701867.