WordNet

a fibrous scleroprotein that occurs in the outer layer of the skin and in horny tissues such as hair, feathers, nails, and hooves (同)ceratin
organic process by which keratin is deposited in cells and the cells become horny (as in nails and hair) (同)keratinisation

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/21 22:36:17」(JST)

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Microscopy of keratin filaments inside cells.

Keratin (/ˈkɛrətɪn/^[1]^[2]) is a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human skin. It is the key structural component of hair and nails, and it provides the necessary strength and toughness for masticatory organs, such as the tongue and the hard palate. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized tissues found in reptiles, birds, amphibians, and mammals. The only other biological matter known to approximate the toughness of keratinized tissue is chitin.^[3]^[4]^[5]

Etymology

Keratin derives from Greek κερατίνη from Greek keras (κέρας) (genitive keratos, κέρατος) meaning "horn" originating from the Proto-Indo-European *ḱer- of the same meaning.^[6] Its Greek root is composed of "horn like", i.e., kerato (Greek κέρατο)^[7] to which the chemical suffix -in is appended.^[8]

Examples of uses

Horns such as those of the impala are made up of keratin covering a core of live bone

Keratin filaments are abundant in keratinocytes in the cornified layer of the epidermis; these are cells which have undergone keratinization. In addition, keratin filaments are present in epithelial cells in general. For example, mouse thymic epithelial cells (TECs) are known to react with antibodies for keratin 5, keratin 8, and keratin 14. These antibodies are used as fluorescent markers to distinguish subsets of TECs in genetic studies of the thymus.

the α-keratins in the hair (including wool), horns, nails, claws and hooves of mammals^{[verification needed]}
the harder β-keratins found in nails and in the scales and claws of reptiles, their shells (Testudines, such as tortoise, turtle, terrapin), and in the feathers, beaks, claws of birds and quills of porcupines.^[9] (These keratins are formed primarily in beta sheets. However, beta sheets are also found in α-keratins.)^[10]

The baleen plates of filter-feeding whales are made of keratin.

Keratins (also described as cytokeratins) are polymers of type III and type IV intermediate filaments, which have only been found in the genomes of chordates (vertebrates, Amphioxus, urochordates). Nematodes and many other non-chordate animals seem to only have type VI intermediate filaments, lamins, which have a long rod domain (vs. a short rod domain for the keratins).

Structural details

Keratin (high molecular weight) in bile duct cell and oval cells of horse liver

The first sequences of keratins were determined by Hanukoglu and Fuchs.^[11] ^[12] These sequences revealed that there are two distinct but homologous keratin families which were named as Type I keratin and Type II keratins.^[12] By analysis of the primary structures of these keratins and other intermediate filament proteins, Hanukoglu and Fuchs suggested a model that keratins and intermediate filaments proteins contain a central ~310 residue domain with four segments in α-helical conformation that are separated by three short linker segments predicted to be in beta-turn conformation.^[12] This model has been confirmed by the determination of the crystal structure of a helical domain of keratins.^[13]

Fibrous keratin molecules supercoil to form a very stable, left-handed superhelical motif to multimerise, forming filaments consisting of multiple copies of the keratin monomer.^[14]

The major force that keeps the coiled-coil structure is hydrophobic interactions between apolar residues along the keratins helical segments.^[15]

Limited interior space is the reason why the triple helix of the (unrelated) structural protein collagen, found in skin, cartilage and bone, likewise has a high percentage of glycine. The connective tissue protein elastin also has a high percentage of both glycine and alanine. Silk fibroin, considered a β-keratin, can have these two as 75–80% of the total, with 10–15% serine, with the rest having bulky side groups. The chains are antiparallel, with an alternating C → N orientation.^[16] A preponderance of amino acids with small, nonreactive side groups is characteristic for structural proteins, for which H-bonded close packing is more important than chemical specificity.

Disulfide bridges

In addition to intra- and intermolecular hydrogen bonds, keratins have large amounts of the sulfur-containing amino acid cysteine, required for the disulfide bridges that confer additional strength and rigidity by permanent, thermally stable crosslinking^[17]—a role sulfur bridges also play in vulcanized rubber. Human hair is approximately 14% cysteine. The pungent smells of burning hair and rubber are due to the sulfur compounds formed. Extensive disulfide bonding contributes to the insolubility of keratins, except in dissociating or reducing agents.

The more flexible and elastic keratins of hair have fewer interchain disulfide bridges than the keratins in mammalian fingernails, hooves and claws (homologous structures), which are harder and more like their analogs in other vertebrate classes. Hair and other α-keratins consist of α-helically coiled single protein strands (with regular intra-chain H-bonding), which are then further twisted into superhelical ropes that may be further coiled. The β-keratins of reptiles and birds have β-pleated sheets twisted together, then stabilized and hardened by disulfide bridges.

Filament formation

It was theorized that keratins are combined into 'hard' and 'soft,' or 'cytokeratins' and 'other keratins'^{[clarification needed]}. That model is now understood to be correct. A new nuclear addition in 2006 to describe keratins takes this into account.^[18]

Keratin filaments are intermediate filaments. Like all intermediate filaments, keratin proteins form filamentous polymers in a series of assembly steps beginning with dimerization; dimers assemble into tetramers and octamers and eventually, if the current hypothesis holds, into unit-length-filaments (ULF) capable of annealing end-to-end into long filaments.

Pairing

The neutral-basic keratins are found on chromosome 12 (12q13.13).

While the acidic keratins are found on chromosome 17 (17q21.2).

A (neutral-basic)	B (acidic)	Occurrence
keratin 1, keratin 2	keratin 9, keratin 10	stratum corneum, keratinocytes
keratin 3	keratin 12	cornea
keratin 4	keratin 13	stratified epithelium
keratin 5	keratin 14, keratin 15	stratified epithelium
keratin 6	keratin 16, keratin 17	squamous epithelium
keratin 7	keratin 19	ductal epithelia
keratin 8	keratin 18, keratin 20	simple epithelium

Protein sequence alignment of human Keratin 1, 2A, 3,4, 5, 6A, 7,and 8 (KRT1 - KRT8). Only the first rod domain is shown above. Alignment was created using Clustal Omega (tool available online).

The entries KRT23, KRT24, KRT25, KRT26, KRT27, KRT28, KRT31, KRT32, KRT33A, KRT33B, KRT34, KRT35, KRT36, KRT37, KRT38, KRT39, KRT40, KRT71, KRT72, KRT73, KRT74, KRT75, KRT76, KRT77, KRT78, KRT79, KRT8, KRT80, KRT81, KRT82, KRT83, KRT84, KRT85 and KRT86 have been used to describe keratins past 20.^[18]

Cornification

Cornification is the process of forming an epidermal barrier in stratified squamous epithelial tissue. At the cellular level, cornification is characterised by:

production of keratin
production of small proline-rich (SPRR) proteins and transglutaminase which eventually form a cornified cell envelope beneath the plasma membrane
terminal differentiation
loss of nuclei and organelles, in the final stages of cornification

Metabolism ceases, and the cells are almost completely filled by keratin. During the process of epithelial differentiation, cells become cornified as keratin protein is incorporated into longer keratin intermediate filaments. Eventually the nucleus and cytoplasmic organelles disappear, metabolism ceases and cells undergo a programmed death as they become fully keratinized. In many other cell types, such as cells of the dermis, keratin filaments and other intermediate filaments function as part of the cytoskeleton to mechanically stabilize the cell against physical stress. It does this through connections to desmosomes, cell-cell junctional plaques, and hemidesmosomes, cell-basement membrane adhesive structures.

Cells in the epidermis contain a structural matrix of keratin, which makes this outermost layer of the skin almost waterproof, and along with collagen and elastin, gives skin its strength. Rubbing and pressure cause thickening of the outer, cornified layer of the epidermis and form protective calluses — useful for athletes and on the fingertips of musicians who play stringed instruments. Keratinized epidermal cells are constantly shed and replaced.

These hard, integumentary structures are formed by intercellular cementing of fibers formed from the dead, cornified cells generated by specialized beds deep within the skin. Hair grows continuously and feathers moult and regenerate. The constituent proteins may be phylogenetically homologous but differ somewhat in chemical structure and supermolecular organization. The evolutionary relationships are complex and only partially known. Multiple genes have been identified for the β-keratins in feathers, and this is probably characteristic of all keratins.

Silk

The silk fibroins produced by insects and spiders are often classified as keratins, though it is unclear whether they are phylogenetically related to vertebrate keratins.

Silk found in insect pupae, and in spider webs and egg casings, also has twisted β-pleated sheets incorporated into fibers wound into larger supermolecular aggregates. The structure of the spinnerets on spiders’ tails, and the contributions of their interior glands, provide remarkable control of fast extrusion. Spider silk is typically about 1 to 2 micrometres (µm) thick, compared with about 60 µm for human hair, and more for some mammals. The biologically and commercially useful properties of silk fibers depend on the organization of multiple adjacent protein chains into hard, crystalline regions of varying size, alternating with flexible, amorphous regions where the chains are randomly coiled.^[19] A somewhat analogous situation occurs with synthetic polymers such as nylon, developed as a silk substitute. Silk from the hornet cocoon contains doublets about 10 µm across, with cores and coating, and may be arranged in up to 10 layers, also in plaques of variable shape. Adult hornets also use silk as a glue, as do spiders.

Clinical significance

Some infectious fungi, such as those that cause athlete's foot and ringworm (i.e. the dermatophytes), or Batrachochytrium dendrobatidis (Chytrid fungus), feed on keratin.^{[citation needed]}

Diseases caused by mutations in the keratin genes include

Epidermolysis bullosa simplex
Ichthyosis bullosa of Siemens
Epidermolytic hyperkeratosis
Steatocystoma multiplex
Keratosis pharyngis
Rhabdoid cell formation in Large cell lung carcinoma with rhabdoid phenotype^[20]^[21]

Furthermore, keratin expression is helpful in determining epithelial origin in anaplastic cancers. Tumors that express keratin include carcinomas, thymomas, sarcomas and trophoblastic neoplasms. Furthermore, the precise expression pattern of keratin subtypes allows prediction of the origin of the primary tumor when assessing metastases. For example, hepatocellular carcinomas typically expresse K8 and K18, and cholangiocarcinomas express K7, K8 and K18, while metastases of colorectal carcinomas express K20, but not K7.^[22]

Keratin is highly resistant to digestive acids if it is ingested (Trichophagia). Because of this, cats (which groom themselves with their tongues) regularly ingest hair which will eventually result in the gradual formation of a Hairball that is occasionally vomited when it becomes too big. Rapunzel_syndrome is an extremely rare but potentially fatal intestinal condition in humans that is caused by Tricophagia.

Cosmetic uses

Hydrolysed keratin has become a common cosmetic ingredient. Studies have shown topical application of hydrolysed keratin gives significant increases in skin elasticity and hydration.^[23] Due to its moisturising properties, hydrolysed keratin has also been incorporated into shampoo and conditioner.

Larger keratin structures such as those formed by cornification cannot penetrate the skin so cannot be used as moisturisers. However, there are other uses, from hair loss concealing products using fine hair fibres^[24] to hair thickening accessories like hair extensions.

References

^ OED 2nd edition, 1989 as /ˈkɛrətɪn/.
^ Entry "keratin" in Merriam-Webster Online Dictionary.
^ "Keratin". Webster's Online Dictionary.
^ Vincenta, Julian F.V.; Wegst, Ulrike G.K. (1 July 2004). "Design and mechanical properties of insect cuticle" (PDF). Arthropod Structure & Development 33 (3): 187–199. doi:10.1016/j.asd.2004.05.006.
^ Tombolato L, Novitskaya EE, Chen PY, Sheppard FA, McKittrick J (February 2010). "Microstructure, elastic properties and deformation mechanisms of horn keratin" (PDF). Acta Biomater 6 (2): 319–30. doi:10.1016/j.actbio.2009.06.033. PMID 19577667.
^ "Keratin". Online Etymology Dictionary.
"Horn". Online Etymology Dictionary.
^ "kerato-". Online Etymology Dictionary.
"Horn". Online Etymology Dictionary.
^ "-in/-ine chemical suffix". Online Etymology Dictionary.
^ 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.
^ 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. PMC 1304386. PMID 15240497.
^ Hanukoglu, I.; Fuchs, E. (Nov 1982). "The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins.". Cell 31 (1): 243–52. doi:10.1016/0092-8674(82)90424-X. PMID 6186381.
^ ^a ^b ^c Hanukoglu, I.; Fuchs, E. (Jul 1983). "The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins.". Cell 33 (3): 915–24. doi:10.1016/0092-8674(83)90034-X. PMID 6191871.
^ Lee, CH.; Kim, MS.; Chung, BM.; Leahy, DJ.; Coulombe, PA. (Jul 2012). "Structural basis for heteromeric assembly and perinuclear organization of keratin filaments.". Nat Struct Mol Biol 19 (7): 707–15. doi:10.1038/nsmb.2330. PMID 22705788.
^ Voet, Donald; Voet, Judith; Pratt, Charlotte. "Proteins: Three-Dimensional Structure" (PDF). 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
^ Hanukoglu, I.; Ezra, L. (Jan 2014). "Proteopedia: Coiled-coil structure of keratins.". Biochem Mol Biol Educ 42 (1): 93–94. doi:10.1002/bmb.20746. PMID 24265184.
^ "Secondary Protein". Elmhurst.edu. Retrieved 2010-09-23.
^ "What is Keratin?". WiseGEEK. Retrieved 11 May 2014.
^ ^a ^b 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. PMC 2064177. PMID 16831889.
^ Australia. "Spiders - Silk structure". Amonline.net.au. Retrieved 2010-09-23.
^ Shiratsuchi H, Saito T, Sakamoto A et al. (February 2002). "Mutation analysis of human cytokeratin 8 gene in malignant rhabdoid tumor: a possible association with intracytoplasmic inclusion body formation". Mod. Pathol. 15 (2): 146–53. doi:10.1038/modpathol.3880506. PMID 11850543.
^ Itakura E, Tamiya S, Morita K et al. (September 2001). "Subcellular distribution of cytokeratin and vimentin in malignant rhabdoid tumor: three-dimensional imaging with confocal laser scanning microscopy and double immunofluorescence". Mod. Pathol. 14 (9): 854–61. doi:10.1038/modpathol.3880401. PMID 11557780.
^ 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. PMC 2701867. PMID 19587454.
^ Barba C, Méndez S, Roddick-Lanzilotta A, Kelly R, Parra JL, Coderch L. (May 2008). "Cosmetic effectiveness of topically applied hydrolysed keratin peptides and lipids derived from wool.". Skin Res. Technol. 14 (2): 243–248. doi:10.1111/j.1600-0846.2007.00280. PMID 18412569.
^ Pangaea Laboratories. "Hair Fibres". Retrieved 2014-02-18.

External links

Composition and β-sheet structure of silk
Hair-Science.com's entry on the microscopic elements of hair
Proteopedia page on keratins

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 皮膚の良性病変の概要 overview of benign lesions of the skin
2. 脱毛の評価および診断 evaluation and diagnosis of hair loss
3. Keratosis pilaris
4. ケラトアカントーマ：疫学、危険因子、および診断 keratoacanthoma epidemiology risk factors and diagnosis
5. 上皮成長因子受容体（EGFR）阻害剤投与に続発するざ瘡様発疹 acneiform eruption secondary to epidermal growth factor egfr inhibitors

English Journal

Hemostatic properties and the role of cell receptor recognition in human hair keratin protein hydrogels.

Burnett LR, Rahmany MB, Richter JR, Aboushwareb TA, Eberli D, Ward CL, Orlando G, Hantgan RR, Van Dyke ME.SourceKeraNetics LLC, Winston Salem, NC, USA. Electronic address: lburnett@wakehealth.edu.
Biomaterials.Biomaterials.2013 Apr;34(11):2632-40. doi: 10.1016/j.biomaterials.2012.12.022. Epub 2013 Jan 20.
Driven by new discoveries in stem-cell biology and regenerative medicine, there is broad interest in biomaterials that go beyond basic interactions with cells and tissues to actively direct and sustain cellular behavior. Keratin biomaterials have the potential to achieve these goals but have been in
PMID 23340195

Low-grade and high-grade mammary carcinomas in WAP-T transgenic mice are independent entities distinguished by Met expression.

Otto B, Gruner K, Heinlein C, Wegwitz F, Nollau P, Ylstra B, Pantel K, Schumacher U, Baumbusch LO, Martin-Subero JI, Siebert R, Wagener C, Streichert T, Deppert W, Tolstonog GV.SourceDepartment of Clinical Chemistry/Central Laboratories, Center for Diagnostic, University Medical Center Hamburg-Eppendorf, Hamburg, Germany; I. Department of Internal Medicine, Center for Internal Medicine, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
International journal of cancer. Journal international du cancer.Int J Cancer.2013 Mar 15;132(6):1300-10. doi: 10.1002/ijc.27783. Epub 2012 Sep 26.
Mammary carcinomas developing in SV40 transgenic WAP-T mice arise in two distinct histological phenotypes: as differentiated low-grade and undifferentiated high-grade tumors. We integrated different types of information such as histological grading, analysis of aCGH-based gene copy number and gene e
PMID 22907219

Japanese Journal

羊毛ケラチンの酵素分解における還元剤と界面活性剤の影響

吉村由利香,大江猛
科学と工業 86(8), 260-264, 2012-08
NAID 40019410784

生体材料としてのケラチンタンパク質

澤田和也,藤里俊哉
Fiber = 繊維学会誌 : journal of the Society of Fiber Science and Technology, Japan 68(8), P-232-238, 2012-08
NAID 40019392934

Related Pictures

★リンクテーブル★

リンク元	「ケラチン」「角質」
拡張検索	「keratinosome」

「ケラチン」

　　[★]

英: keratin
ラ: keratinum
関: 中間径フィラメント

ケラチン	主な発現部位	遺伝子異常により発症する疾患
K1, K10	有棘層から顆粒層の角化性表皮細胞	水疱型先天性魚鱗癬様紅皮症
K2e	表皮最外層の細胞	Siemens型水疱性魚鱗癬
K3, K12	角膜上皮細胞	Meesmann型角膜上皮変性症
K4, K13	粘膜	白色海綿状母斑
K5, K14	表皮の基底細胞	単純型表皮水疱症
K6, K16	爪	先天性厚硬爪甲症
K9	掌蹠の表皮の有棘層から顆粒層の細胞	Vörner型先天性掌蹠角化症

臨床関連

ケラチンの欠損により種々の皮膚疾患を呈する。上表参照。
免疫組織化学により発現しているケラチンのパターンで組織型を(ある程度？)鑑別できる。

ケラチンK8, K18　→　乳房外パジェット病

「角質」

　　[★]

英: keratin、corneum、cuticle、horny、cuticular
関: 角質層、角皮、クチクラ

「keratinosome」

　　[★] 層板顆粒。ケラチノソーム

[1] OED 2nd edition, 1989 as /ˈkɛrətɪn/.

[2] Entry "keratin" in Merriam-Webster Online Dictionary.

[3] "Keratin". Webster's Online Dictionary.

[4] Vincenta, Julian F.V.; Wegst, Ulrike G.K. (1 July 2004). "Design and mechanical properties of insect cuticle" (PDF). Arthropod Structure & Development 33 (3): 187–199. doi:10.1016/j.asd.2004.05.006.

[5] Tombolato L, Novitskaya EE, Chen PY, Sheppard FA, McKittrick J (February 2010). "Microstructure, elastic properties and deformation mechanisms of horn keratin" (PDF). Acta Biomater 6 (2): 319–30. doi:10.1016/j.actbio.2009.06.033. PMID 19577667.

[6] "Keratin". Online Etymology Dictionary.
"Horn". Online Etymology Dictionary.

[7] "kerato-". Online Etymology Dictionary.
"Horn". Online Etymology Dictionary.

[8] "-in/-ine chemical suffix". Online Etymology Dictionary.

[9] 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.

[10] 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. PMC 1304386. PMID 15240497.

[Hanukoglu-1982-11] Hanukoglu, I.; Fuchs, E. (Nov 1982). "The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins.". Cell 31 (1): 243–52. doi:10.1016/0092-8674(82)90424-X. PMID 6186381.

[Hanukoglu-1983-12] Hanukoglu, I.; Fuchs, E. (Jul 1983). "The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins.". Cell 33 (3): 915–24. doi:10.1016/0092-8674(83)90034-X. PMID 6191871.

[Lee-2012-13] Lee, CH.; Kim, MS.; Chung, BM.; Leahy, DJ.; Coulombe, PA. (Jul 2012). "Structural basis for heteromeric assembly and perinuclear organization of keratin filaments.". Nat Struct Mol Biol 19 (7): 707–15. doi:10.1038/nsmb.2330. PMID 22705788.

[v.26v1-14] Voet, Donald; Voet, Judith; Pratt, Charlotte. "Proteins: Three-Dimensional Structure" (PDF). 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

[Hanukoglu-2014-15] Hanukoglu, I.; Ezra, L. (Jan 2014). "Proteopedia: Coiled-coil structure of keratins.". Biochem Mol Biol Educ 42 (1): 93–94. doi:10.1002/bmb.20746. PMID 24265184.

[16] "Secondary Protein". Elmhurst.edu. Retrieved 2010-09-23.

[17] "What is Keratin?". WiseGEEK. Retrieved 11 May 2014.

[pmid16831889-18] 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. PMC 2064177. PMID 16831889.

[19] Australia. "Spiders - Silk structure". Amonline.net.au. Retrieved 2010-09-23.

[ShiratsuchiSaito-20] Shiratsuchi H, Saito T, Sakamoto A et al. (February 2002). "Mutation analysis of human cytokeratin 8 gene in malignant rhabdoid tumor: a possible association with intracytoplasmic inclusion body formation". Mod. Pathol. 15 (2): 146–53. doi:10.1038/modpathol.3880506. PMID 11850543.

[ItakuraTamiya-21] Itakura E, Tamiya S, Morita K et al. (September 2001). "Subcellular distribution of cytokeratin and vimentin in malignant rhabdoid tumor: three-dimensional imaging with confocal laser scanning microscopy and double immunofluorescence". Mod. Pathol. 14 (9): 854–61. doi:10.1038/modpathol.3880401. PMID 11557780.

[22] 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. PMC 2701867. PMID 19587454.

[23] Barba C, Méndez S, Roddick-Lanzilotta A, Kelly R, Parra JL, Coderch L. (May 2008). "Cosmetic effectiveness of topically applied hydrolysed keratin peptides and lipids derived from wool.". Skin Res. Technol. 14 (2): 243–248. doi:10.1111/j.1600-0846.2007.00280. PMID 18412569.

[24] Pangaea Laboratories. "Hair Fibres". Retrieved 2014-02-18.

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keratin