Types of Collagen

Types of Collagen

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Types of Collagen

Collagen is an abundant structural protein in animals. In humans, collagen accounts for one-third of total protein, three-quarters of the dry weight of the skin, and it is the most prevalent component of the extracellular matrix (ECM). Twenty-eight different types of collagen (table 1) [1] have been identified in vertebrates that consist of at least 46 different polypeptide chains, and many other proteins contain collagenous structural domains.

TypeFormCompositionDistributionPathology
IFibrillarα1[I]2α2[I]Abundant and widespread: dermis, bone, tendon, ligamentOI, Ehlers–Danlos syndrome, osteoporosis
IIFibrillarα1[II]3Cartilage, vitreousOsteoarthrosis, chondrodysplasias
IIIFibrillarα1[III]3Skin, blood vessels, intestineEhlers-Danlos syndrome, arterial aneurysms
IVNetworkα1[IV]2α2[IV]
α3[IV]α4[IV]α5[IV]
α5[IV]2α6[IV
Basement membranesAlport syndrome
VFibrillarα1[V]3
α1[V]2α2[V]
α1[V]α2[V]α3[V]
Widespread: bone, dermis, cornea, placentaEhlers-Danlos syndrome
VINetworkα1[VI]α2[VI] α3[VI]
α1[VI]α2[VI] α4[VI]
Widespread: bone, cartilage, cornea, dermisBethlem myopathy
VIIAnchoring fibrilsα1[VII]2α2[VII]Dermis, bladderEpidermolysis bullosa acquisita
VIIINetworkα1[VIII]3
α2[VIII]3
α1[VIII]2α2[VIII]
Widespread: dermis, brain, heart, kidneyFuchs endothelia corneal dystrophy
IXFACITα1[IX]α2[IX]α3[IX]Cartilage, cornea, vitreousOsteoarthrosis, multiple epiphyseal dysplasia
XNetworkα1[X]3CartilageChondrodysplasia
XIFibrillarα1[XI]α2[XI]α3[XI]Cartilage, intervertebral discChondrodysplasia, osteoarthrosis
XIIFACITα1[XII]3Dermis, tendon
XIIIMACITEndothelial cells, dermis, eye, heart
XIVFACITα1[XIV]3Widespread: bone, dermis, cartilage
XVMULTIPLEXINCapillaries, testis, kidney, heart
XVIFACITDermis, kidney
XVIIMACITα1[XVII]3Hemidesmosomes in epitheliaGeneralized atrophic epidermolysis bullosa
XVIIIMULTIPLEXINBasement membrane, liverKnobloch syndrome
XIXFACITBasement membrane
XXFACITCornea (chick)
XXIFACITStomach, kidney
XXIIFACITTissue junctions
XXIIIMACITHeart, retina
XXIVFibrillarBone, cornea
XXVMACITBrain, heart, testis
XXVIFACITTestis, ovary
XXVIIFibrillarCartilage
XXVIIIDermis, sciatic nerve

These different types of collagen carry out specific functions in different tissues and have different supramolecular organization patterns. Some molecules are homotrimers, while others are heterotrimers with two or three distinguishable chain types [2].

Illustration of some of the biological forms of the collagen triple-helix domainsFig. 1 Illustration of some of the biological forms of the collagen triple-helix domains

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References

  1. Shoulders, M. D., & Raines, R. T. Collagen Structure and Stability. Annual Review of Biochemistry, 2009, 78(1), 929–958.
  2. Brodsky, B., & Persikov, A. V. Molecular Structure of the Collagen Triple Helix. Advances in Protein Chemistry, 2005, 301–339.

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