What is keratin and what has it ever done for us? Fundamental to life, keratin abundant tissue has provided clothing, shelter, adornments, tools and utensils over millennia. Keratin is the key component of our skin, hair and nails. Its protein building blocks have amino acid chains, coiled, cross-linked and classified as either hard or soft. It separates us from our environment by forming thin, flexible skin, strong hair and rigid nails. Even embryonic teeth have a keratin layer!
Internal linkages provide keratin with its stability, enzyme resistance and insolubility (although it can absorb water). Skin, hair and nails are multi-layered, maturing from a nail matrix, hair bulb or epidermal basal layer. Keratinocytes leave their germinal base, change shape, and begin producing and accumulating keratin. They then harden and become flexible, flat, and water resistant corneocytes. This cornification differs between each structure, but general processes and purposes are shared. Finally, keratin producing cells die. Keratinised tissue is avascular.
The primary characteristic of keratin tissue is its appearance of overlapping scales. However, other characteristics include:
- Stratum corneum cells (SC) – these are packed, brick-wall like, within a lipid matrix. Enzymes degrade corneocyte linkages enabling shedding – also known as desquamation.
- Cuticle (hair) cells – these cement in protein, face away from the scalp and are protected by sebum. Below this is the cortex which has strong, elongated, tightly packed keratinised cells.
- Nails with long narrow fibres embedded in protein are highly flexible. Nails get their strength from three linked keratin layers, where oils and moisture cement and lubricate the nail plate. Functionality results from the nails shape, which mirrors that of the underlying bone.
- Hair and nails retaining tight inter-corneocyte connections don’t desquamate. However, hair sheds through life cycle programming and nail corneocytes are buffed off with friction and activity.
Multiple genes regulate keratin production, primarily in accordance with tissue type and cell maturity. Over time however, mutations can reduce the mechanical resilience of the cells and break the cell-to-cell linkages.
Disruption and Potential Damage
Disruption to our keratin scales can change the initially smooth, soft and lustered appearance, to a dull appearance with rough, disordered scales, making the tissue susceptible to damage. Other impacts include:
- Disrupted cellular links:
- Dermatophyte infection – microbial enzymes break cellular links. Dermatophytes consume keratin for nutrition, extending to fresh areas as the source diminishes.
- External physical and chemical forces, such as hair styling, can also break cellular links.
- Reduced surface lipids – age and exposure causes dryness, diminishing the protective layers of all keratin structures.
- Physical damage:
- Trauma, scars and nail-bed deformity can reduce adherence of nail plate.
- Nail matrix damage (a cyst for example) can result in poor nail formation.
- Reduced waterproofing
- Nail care
- Cuticle – emerges from proximal nail fold towards fingertip, sealing the new (soft) keratin until it hardens (providing waterproofing).
- Hyponychium – at the free edge of the nail plate, the hyponychium provides a mechanical and immunologic barrier. It can be disrupted from vigorous nail hygiene.
- Skin care
- Harsh hygiene measures can diminish SC lipids causing dull, flaking, inflamed or symptomatic skin.
- Nail care
- Cell replacement: defective keratinisation causes nail pitting, thickening skin, hair loss.
- Physical disruption to growth patterns (hormonal, medication – disruption to rapidly multiplying cells eg chemotherapy):
- nail ridge patterns.
- hair growth cycles disrupted; hair thinning (male or female pattern), and hair loss.
So what has keratin ever done for us? Lots! It enables life, maintains appearance, reflects our systems health, facilitates fine motor function and sensation and keeps our tissues strong and resilient!
[show_more more=”Show References” less=”Hide References” align=”center” color=”#808080″]
- Bragulla, HH & Homberger, DG 2009, ‘Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia’. Journal of Anatomy, vol. 214 no. 4, pp. 516–559, Viewed 30 September 2015 http://doi.org/10.1111/j.1469-7580.2009.01066.
- Coulombe, PA and Lee, C-H 2012, ‘Defining Keratin Protein Function in Skin Epithelia: Epidermolysis Bullosa Simplex and Its Aftermath’, Journal of Investigative Dermatology, vol. 132, pp. 763–775, doi:10.1038/jid.2011.450, viewed 6 September 2015, http://www.nature.com/jid/journal/v132/n3-2/pdf/jid2011450a.pdf
- Eckhart, L, Lippens, S, Tschachler, E & Declercq, W 2013, ‘Cell death by cornification’ vol.1833, no.12 Biochimica et Biophysica Acta (BBA) – Molecular Cell Research doi:10.1016/j.bbamcr.2013.06.010 viewed 30 September 2015, http://www.sciencedirect.com/science/article/pii/S0167488913002334
- Farren, L, Shayler, S & Ennos, AR 2004, ‘The fracture properties and mechanical design of human fingernails’, doi: 10.1242/jeb.00814 J Exp Biol vol. 207, pp. 735-741, viewed 10 September 2015, http://jeb.biologists.org/content/207/5/735.full#ack-1
- Roth, W, Hatzfeld, M, Friedrich, M, Thiering, S & Magin, TM 2012, ‘Keratin function and regulation in tissue homeostasis and pathogenesis’,Biomolecular Concepts, vol. 3, pp. 161–173 DOI 10.1515/BMC.2011.060 viewed 30 September 2015, http://www.degruyter.com/view/j/bmc.2012.3.issue-2/bmc.2011.060/bmc.2011.060.xml
- Shetty, S & Gokul S 2012 ‘Keratinization and its disorders’, Oman Medical Journal, vol. 27, no. 5, pp. 348–357. http://doi.org/10.5001/omj.2012.90 viewed 9 September 2015, http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3472583/
- Tainwala, R & Sharma, Y 2011, ‘Pathogenesis of dermatophytoses’, Indian Journal of Dermatology, vol. 56 no. 3, pp. 259–261. http://doi.org/10.4103/0019-5154.82476 viewed 18 September 2015 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3132899/
- McKittrick, J, Chen, P-Y, Bodde, SG, Yang, W, Novitskaya, EE & Meyers, MA 2012, ‘The structure, functions, and mechanical properties of keratin’, JOM (Journal of The Minerals, Metals & Materials Society), vol. 64, no. 4, DOI: 10.1007/s11837-012-0302-8. Viewed 20 September 2015, http://meyersgroup.ucsd.edu/papers/journals/Meyers%20354.pdf
Jan Riley RN, MNurs(NP) is a specialist dermatology nurse based in regional New South Wales, Australia. Her postgraduate studies include a Certificate in Dermatology Nursing (USA), Master of Nursing (NP) and Certificates in Dermoscopy and Skin Cancer Medicine. Driven by a passion for “all things skin”, Jan is a staunch and passionate mentor and advocate, who is always ready and willing to share knowledge and inspire nurses to understand skin’s impact on daily lives. Her active participation in a range of professional activities has greatly assisted to raise the profile of dermatology and skin disease in the community. Jan currently develops and presents skin education modules through a co-directed nurse education company (Dermatology Nurse Education Australia) for nurses across all areas of care delivery.