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Microscopy of keratin filaments inside cells.

Keratin refers to a family of fibrous structural proteins. Keratin is an intermediate filament; when assembled in bundles, it is tough and insoluble forming hard, unmineralized structures found in reptiles, birds, amphibians, and mammals. They are rivalled as biological matter in toughness only by chitin.

There are various types of keratins within a single bioform. The outer layer of hair is also made of keratin. Notice that if you bend a piece of hair, it does does not break.

Contents

Variety of use

Keratin is the main constituent grown from skin:

Arthropods such as crustaceans often have parts of their armor or exoskeleton made of keratin, some times in combination with chitin.

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

It can be integrated in the chitinophosphatic matter that composes the shell and setae in many brachiopods.

Keratin is also found in the gastrointestinal tracts of many bioforms, including roundworms (which also have outer layers of keratin).

Although it is now difficult to be certain, the scales, claws, some protective armour and the beaks of dinosaurs would, almost certainly, have been composed of keratin.[citation needed]

Cornification

It used to be thought that keratins were separable into 'hard' and 'soft,' or 'cytokeratins' and 'other keratins', but those designations are now understood to be incorrect. A new nomenclature adopted in 2006 to describe keratins takes this into account [3].

Keratins 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, the current hypothesis holds, into unit-length-filaments (ULF) capable of annealing end-to-end into long filaments. 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 under go a programmed death as they become fully keratinized. In many other cells types, such as dermis, keratin functions in the cytoplasm 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 keratin to proliferate with the formation of protective calluses — useful for athletes and on the fingertips of musicians who play stringed instruments. Keratinized epidermal cells are constantly shed and replaced (see dandruff).

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.

Molecular biology and biochemistry

The usefulness of keratins depends on their supermolecular aggregation. These depend on the properties of the individual polypeptide strands, which depend in turn on their amino acid composition and sequence. The α-helix and β-sheet motifs, and disulfide bridges, are crucial to the conformations of globular, functional proteins like enzymes, many of which operate semi-independently, but they take on a completely dominant role in the architecture and aggregation of keratins.

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Glycine and alanine

Keratins contain a high proportion of the two smallest amino acids: glycine (whose "side group" is a single hydrogen atom) and alanine (with a small and noncharged methyl group). In the case of β-sheets, this allows sterically-unhindered hydrogen bonding between the amino and carboxyl groups of peptide bonds on adjacent protein chains, facilitating their close alignment and strong binding. Fibrous keratin molecules can twist around each other to form helical intermediate filaments.

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.[4] 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—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.

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. (Hair, or fur, occurs only in 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.[5] 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.

Pairing

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

The entries KRT23, KRT24, KRT25, KRT26, KRT27, KRT28, KRT31, KRT32, KRT33, KRT33A, 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.[6]

Clinical significance

Some infectious fungi, such as those that cause athlete's foot, ringworm, or the Batrachochytrium dendrobatidis (Chytrid fungus) which is killing amphibians all over the world, feed on keratin.

Diseases caused by mutations in the keratin genes include

See also

Additional images

References

  1. ^ Hickman, Cleveland Pendleton; Roberts, Larry S.; Larson, Allan L. (2003). Integrated principles of zoology. Dubuque, IA: McGraw-Hill. pp. 538. ISBN 0-07-243940-8. 
  2. ^ 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. 
  3. ^ New consensus nomenclature for mammalian keratins. J Cell Biol. 2006 Jul 17;174(2):169-74.
  4. ^ http://elmhurst.edu/~chm/vchembook/566secprotein.html
  5. ^ Spiders - Silk structure
  6. ^ 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. http://www.jcb.org/cgi/pmidlookup?view=long&pmid=16831889. 

Further reading

Ramot Y, Paus R, Tiede S, Zlotogorski A. Endocrine controls of keratin expression. Bioessays. 2009 Apr;31(4):389-99. PMID: 19274655

External links


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