Olfactomedin 1 was first identified in the olfactory neuroepithelium of the bullfrog, where it was found to be secreted into the nasal lumen and associated with chemosensory dendritic cilia . The protein forms disulfide-linked aggregates and is believed to serve as a differentiation signal for chemosensory neurons .
Structurally, Olfactomedin 1 exists in multiple isoforms due to alternative promoter usage and splicing . These isoforms, referred to as AMY, BMY, AMZ, and BMZ, are differentially expressed in various brain regions and during different developmental stages . The long isoform BMZ forms a disulfide-linked tetramer with a V-shaped architecture, where each tip of the “V” consists of two C-terminal β-propeller domains enclosing a calcium-binding site .
Olfactomedin 1 is highly expressed in the brain and retina, indicating its significant role in nervous system development and function . The protein is involved in various processes, including:
Human recombinant Olfactomedin 1 is produced using recombinant DNA technology, which involves inserting the OLFM1 gene into an expression system, such as bacteria or mammalian cells, to produce the protein in large quantities. This recombinant protein can be used for various research purposes, including structural and functional studies .
Research on Olfactomedin 1 has provided insights into its structural and functional properties, which are essential for understanding its role in the nervous system . The protein’s involvement in synaptic function and cell adhesion makes it a potential target for studying neurological disorders and developing therapeutic interventions .
In conclusion, Olfactomedin 1 is a critical protein in the nervous system, with diverse roles in synaptic function, cell adhesion, and neurodevelopment. The recombinant production of this protein enables further research into its functions and potential clinical applications.