Mutations of the CELA1 gene were suspected to be associated with diffuse nonepidermolytic palmoplantar keratoderma (diffuse NEPPK). However the suspected sequence variant was fully functional and did not strongly associate with the disease. More recently, a specific mutation in the KRT6C gene has been linked to some cases of diffuse NEPPK. A possible polymorphism of the CELA1 gene coding this protein was found. On a secondary structure level, this polymorphism manifests itself in an excision of a short sequence of CELA1. The disappeared sequence carries the key amino acid residues Val-227 and Thr-239, which contribute to the substrate specificity of elastase I (highlighted in Figure 3), as well as five of the eight amino acids involved in the primary contact of the elafin(inhibitor)/elastase complex formation. These observations imply that the sequence variant might modify the substrate specificity of the enzyme and abolish the inhibitor binding capability. Though there were no obvious pathogenic epidermal abnormalities associated with the truncated ELA1 variant, it is possible that carriers of the polymorphism may be at greater risk of developing the common skin diseases such as psoriasis and eczema (genetic and histologic studies will be required to investigate the role of ELA1 in these common epidermal disorders.).
Pancreatic elastase
Alpha-amylase
Cholecystokinin
Intrinsic factor
Lactase
Neutrophil elastase
Gastric inhibitory polypeptide
Butyrate esterase