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Background  Paralemmin (Palm) is a prenyl-palmitoyl anchored membrane protein that can drive membrane and process formation in neurons. Earlier studies have shown brain preferred  Palm  expression, although this protein is a major water insoluble protein in chicken lens fiber cells and the  Palm  gene may be regulated by Pax6.    Methods  The expression profile of Palm protein in the embryonic, newborn and adult mouse eye as well as dissociated retinal neurons was determined by confocal immunofluorescence. The relative mRNA levels of  Palm, Palmdelphin (PalmD)  and  paralemmin2 (Palm2)  in the lens and retina were determined by real time rt-PCR.    Results  In the lens, Palm is already expressed at 9.5 dpc in the lens placode, and this expression is maintained in the lens vesicle throughout the formation of the adult lens. Palm is largely absent from the optic vesicle but is detectable at 10.5 dpc in the optic cup. In the developing retina, Palm expression transiently upregulates during the formation of optic nerve as well as in the formation of both the inner and outer plexiform layers. In short term dissociated chick retinal cultures, Palm protein is easily detectable, but the levels appear to reduce sharply as the cultures age.  Palm  mRNA was found at much higher levels relative to  Palm2  or  PalmD  in both the retina and lens.    Conclusion   Palm  is the major paralemmin family member expressed in the retina and lens and its expression in the retina transiently upregulates during active neurite outgrowth. The expression pattern of Palm in the eye is consistent with it being a Pax6 responsive gene. Since Palm is known to be able to drive membrane formation in brain neurons, it is possible that this molecule is crucial for the increase in membrane formation during lens fiber cell differentiation.

Palm is expressed in both developing and adult mouse lens and retina