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The mysterious role of collagen XVII: Why is it so important for skin adhesion?
Collagen XVII, originally called BP180, is a transmembrane protein that plays an important role in maintaining the connection between structural elements inside and outside the cell. Since its discovery by Diaz et al. in 1990, this protein has played an integral role in the adhesion mechanism of the skin. COL17A1 is the official name of the gene, which encodes the alpha chain of collagen XVII. As a structural component, collagen XVII is present in semiadhesive structures of the skin that help keratinocytes attach to the basement membrane. In addition to this major role, collagen XVII has also been shown to be critical in maintaining the integrity of the corneal epithelium.
Collagen XVII is a transmembrane protein whose structure and function are essential for healthy skin.
Structure and function of collagen XVII
The structure of collagen XVII consists of three alpha1(XVII) chains, each chain is approximately 180 kD. Each α chain contains a globular intracellular region of approximately 70 kDa that interacts with β4 integrin, plectin, and BP230, which is key to the stable connection between hemiadhesions and cutin intermediate filaments. In addition, its C-terminal ectodomain weighs approximately 120 kDa and is composed of 15 collagen subdomains that exhibit typical collagen repeat sequences. The flexible structure of this outer domain improves its thermal stability.
The majority collagen domain (Col15) of collagen XVII is responsible for the stability of its trimer.
Pathological significance
Mutations in the COL17A1 gene lead to structural variations in collagen XVII, which have serious effects on the overall function of the skin. Specifically, biallelic mutations cause a condition called junctional epidermolysis bullosa, an autosomal recessive skin disease characterized by easy onset of blisters and lesions on the skin. In addition, collagen XVII also plays an important role as an autoantigen in acquired skin diseases such as herpes simplex virus and herpes gravidarum.
Clinical features often include blisters, erosions, nail deformities, and dental abnormalities.
Collagen XVII and Cancer Association
The COL17A1 gene is abnormally expressed in a variety of cancers, especially five types of epithelial cancers, including breast cancer and cervical cancer. In these cases, expression was significantly reduced in breast cancer, while expression was increased in other cancers.
Secretion and Regulation of Collagen XVII
Collagen XVII is continuously released from the surface of keratinocytes to the extracellular space, and the release process involves transforming growth factor cleaving enzyme (TACE). This process depends on the presence of lipid rafts, and phosphorylation of the NC16A region negatively regulates release.
Association with other diseases
The SPARC gene is associated with mutations in collagen XVII, and these mutations may lead to a disease called osteogenesis imperfecta. In addition, collagen XVII also exhibits interactions with a variety of other proteins, demonstrating its multiple roles in cell structure and function.
Scientific prospects and future research directions
The unique properties of collagen XVII and its role in skin adhesion and structural integrity make it an important target for biomedical research. Future research could focus on its potential therapeutic applications in skin lesions and cancer.
As we gain a deeper understanding of collagen XVII, this protein may reveal new secrets to skin health. But today, we should also think about whether collagen XVII can become a breakthrough in the treatment of skin diseases in the future. Woolen cloth?
