High impact information on Olfm1

• Interestingly, extracellular domain of latrophilin is homologous to olfactomedin, a soluble neuronal protein thought to participate in odorant binding [1].
• In a recent paper (Brissette, L., and Noël, S.-P. (1986) J. Biol. Chem. 261, 6847-6852), we have demonstrated that human low density lipoproteins and high density lipoproteins-3 can totally prevent the specific binding of rat IDL to the low affinity binding sites [2].
• Agene encoding olfactomedin-related glycoprotein was isolated from rat glomerulus despite its prior identification as a neuron-specific gene [3].
• Immunogold electron microscopy revealed selective localization of olfactomedin-related glycoprotein at the Golgi apparatus in podocytes [3].
• The AMZ and BMZ proteins show significant sequence similarity with olfactomedin, an extracellular matrix protein of bullfrog olfactory epithelium, suggesting the possibility of a matrix-related function for these rat glycoproteins in neurons and neurosecretory cells [4].

Anatomical context of Olfm1

• Localization of olfactomedin-related glycoprotein isoform (BMZ) in the golgi apparatus of glomerular podocytes in rat kidneys [3].
• Therefore, HepG2 cells have on their surface a binding site that resembles or is identical to the lipoprotein binding site (LBS) that we found on rat liver membranes (Brissette and Noël (1986) J. Biol. Chem. 261, 6847-6852) [5].

References