Alongside Type I, a core type studied in skin health. It is abundant in the intestinal wall and is critical for elasticity and tensile strength. In a Col3a1 transgenic mouse model, mutations in Type III collagen were shown to impair vascular collagen fibrillogenesis and tissue integrity.

The Type IV listed here is the form placed in the fibril-forming classification. It plays a structural role in the health of hair and lung tissue.

By regulating the organization and arrangement of collagen fibrils in tendon and cartilage, it contributes to the biomechanical properties of these tissues.

A collagen type mainly expressed in arterial remodeling and atherosclerotic plaques. While direct antioxidant effects have not been shown, it is associated more with extracellular matrix remodeling and plaque structure than with the regulation of oxidative stress.

Known as a type specific to the hypertrophic cartilage zone, playing a role in cartilage calcification and ossification processes.

It is thought to help preserve moisture and elasticity in skin and cartilage health. However, its specific role in reducing wrinkles and visible signs of aging has not yet been clearly established; the available evidence comes mainly from studies using mixed collagen preparations.

It supports the extracellular matrix by interacting with Type I collagen fibers. Altered Type XII collagen expression has been reported to be associated with disruptions in tissue repair and matrix organization; however, its direct role in skin hydration and wound healing in humans has not yet been clarified.

By interacting with fibril-forming collagens (Types I–III), it can regulate matrix organization during adipose tissue expansion.

A collagen associated with the basement membrane, with structural and biological roles in various tissues. Its specific role in skin structure, aging, or clinical skin outcomes has not been clearly demonstrated to date.

A FACIT collagen prominent during embryonic development and the subject of limited research in adult tissues.

A FACIT type localized in the blood vessel wall and studied in vascular tissue organization.

Concentrating in skin fibroblasts and focal adhesions, it may enhance cell adhesion and support the extracellular matrix. It has also been shown to be widely expressed in the optic nerve and neural retina. While oral collagen supplementation has been reported to broadly support skin elasticity and appearance, Type XIII's specific contribution to these effects has not yet been isolated in clinical studies.

It contributes to collagen fibril organization and the preservation of tissue integrity in many tissues. Its specific role in skin aging and any potential anti-aging effects have not yet been shown in clinical studies.

Acting like an adaptor protein, it links and organizes fibrillar networks, enhancing the integrity and stability of the extracellular matrix, which is critical for skin elasticity and overall skin structure. Hydrolyzed collagen supplementation has been reported to show promising effects in reducing signs of aging.

Owing to its presence in the basement membrane and its role in tissue regeneration, it is considered potentially effective in improving hydration and reducing wrinkles, though the findings are not clear. It may contribute to tissue integrity.

By interacting with matrix collagens and structural proteins, it provides structural integrity to tissue scaffolds. It acts as a regulator of collagen fibrillogenesis. Type V collagen deficiency is associated with loss of corneal transparency and classic Ehlers-Danlos syndrome. In in vitro studies, Type V collagen peptides derived from pearl oyster mantle collagen hydrolysates have shown antioxidant activity.

It serves as a cell adhesion ligand for skin epithelial cells and fibroblasts, contributing to the preservation of tissue junctions, elasticity, and hydration. It plays an important role in the structure of the extracellular matrix. It has been reported to potentially offer benefits by easing skin aging and related skin conditions.

Recent genetic and functional studies have shown that collagen XXIII variants and overexpression (COL23A1) are associated with increased susceptibility to eczema herpeticum in patients with atopic dermatitis. However, its direct role in more common skin conditions such as wrinkles and intrinsic skin aging has not yet been clarified in clinical studies.

These types share similar functions, such as preserving skin structure, elasticity, and hydration. However, their specific role in slowing age-related skin changes has not yet been clearly defined in clinical studies. This represents an important research gap in the literature.