The Collagen Protein
Collagen is the most abundant protein found in mammals and represents around 30% of the body’s total protein content (1). Aptly deriving from the ancient Greek Kolla (“glue”) and gen (“giving birth to”), humans have understood the connective properties of collagen for millennia (2). But, it has only been over the last 50 years that the richness of collagen’s role in the skin has been clarified.
Although beauty labels often refer to collagen in the singular, scientists today know that there are 28 different types of collagen in the body, each with slightly different properties, functions, and compositions. The most relevant to skin appearance are the ‘fibrillar collagens’, so called because they play important roles in the tensile strength of the skin tissue. Although an oversimplification, these collagens form fiber-like elements that are woven together to form larger structural constructs, such as those found in the skin’s extracellular matrix (ECM). The ECM is a kind of under-armor that provides structural and biomechanical support for the skin, as well as performs other functions. Fibrillar collagen includes collagen types 1, 2, 3, 5, 11, 24, and 27. Of these, collagen type 1 is most important as it makes up 90% of the body’s collagen content and is critical in providing structure to the skin within the ECM, as well as various other components of the body such as bones, tendons, and ligaments (1). Collagen type 3 is also a well-known fibrillar collagen that contributes to skin tensile strength, particularly during fetal development where it accounts for over half of total collagen (3).
Other collagens are also important for skin appearance through their roles in the natural processes of healthy skin. Beaded filament-forming collagens (types 6, 16, and 18) are important for aiding the formation of filaments in skin; of these, collagen type 6 is known to play an important role in the ECM through interaction with other ECM constituents, like hyaluronic acid (4). Network forming collagen (type 4, 8, 10) and anchoring fibrils (type 7) play important roles in the structure of collagen in the ECM. Other collagen types help to link collagen fibers to ECM components, act as cell surface receptors, and can act as signaling components within skin.
Collagen Groups and Function
| Collagen Category | Predominant function | Collagen Types |
|---|---|---|
| Fibrillar | Provides tensile strength though formation of collagen fibers that are used as components within skin macro-structures | 1, 2, 3, 5, 11, 24, 27 |
| Network-Forming | Supports the formation of the collagen structures in the skin | 4, 8, 10 |
| Filament-Forming | Plays an important role in structural formation and connection with ECM components | 6, 26, 28 |
| Anchoring | Acts to connect or anchor collagen fibrils in tissue | 7 |
| Fibril-Associated | Help to link collagen fibers together and with other ECM moldecules | 9. 11.14. 19. 20. 21. 22 |
| Membrane-Associated | Acts as cell surface receptors involved in specific cellular processes | 13, 17, 23, 25 |
| Endostatin-Producing | Promotes adhesion of certain cellular components and can be cleaved to release endostatins | 15, 18 |
Collagen as a Hero of the Skin’s Appearance
References
1. The Cleveland Clinic. Collagen. Cleveland Clinic. [Online] [Cited: July 18, 2023.] https://my.clevelandclinic.org/health/articles/23089-collagen.
2. Douglas Harper. Collagen. Online Etymology Dictionary. [Online] January 18, 2018. [Cited: July 18, 2023.] https://www.etymonline.com/word/collagen#etymonline_v_15820
3. alpha1(III)3 human skin collagen, release by pepsin digestion and preponderance in fetal life. EH, Epstein. s.l. : J Biol Chem, 1974, Vol. 249.
4. Extrcellular Matrix of the Skin: 50 Years of Progress. Uitto J, Olsen D, Fazio M. 4, s.l. : J Invest Derm, 1989, Vol. 92.
5. Grand View Research. Aroma Chemicals Market SIze, Industry Report 2020-2027. Grand View Research. [Online] 09 1, 2020. [Cited: 06 20, 2021.] https://www.grandviewresearch.com/industry-analysis/aroma-chemicals-market.
6. Collagen fibrillogenesis in human skin. Fleischmajer R, Perlish JS, Timpl R. s.l. : NY Acad Sci, 1985, Vol. 460.