Interphotoreceptor matrix proteoglycan 2 (IMPG2)

Interphotoreceptor matrix proteoglycan 2 (IMPG2) is a heavily glycosylated, retinal-specific transmembrane proteoglycan and a prominent structural component of the interphotoreceptor matrix (IPM), the specialized extracellular matrix that envelopes the inner and outer segments of rod and cone photoreceptors. IMPG2 contains distinct SEA (sperm protein, enterokinase, and agrin) domains, including a proteolytic SEA-2 domain that allows the protein to undergo maturation-associated autoproteolysis, generating membrane-bound and extracellular subunits. Together with IMPG1, it underpins the architecture and function of the IPM, supporting the transport of nutrients, matrix stability, and possibly cell-cell communication. Mutations in IMPG2 are a cause of autosomal recessive retinitis pigmentosa and other hereditary retinal dystrophies, frequently leading to early-onset, severe degeneration of photoreceptors and associated vision loss. IMPG2 is not currently considered a pharmacological target, and there are no existing drugs directed at this molecule[1][2][3].

Other names

Interphotoreceptor matrix proteoglycan 2IMPG2IPM200IPM 200SpacrcanRP56SPACRCANInterphotoreceptor matrix proteoglycan of 200 kDaSialoprotein associated with cones and rods proteoglycanVMD5