|Budget Amount *help
¥2,000,000 (Direct Cost : ¥2,000,000)
Fiscal Year 1995 : ¥700,000 (Direct Cost : ¥700,000)
Fiscal Year 1994 : ¥1,300,000 (Direct Cost : ¥1,300,000)
The L1 molecule was first described in the mouse broin as a large membrane glycoprotein. L1 is involved in Ca^<+1>-independent cell adhesion between neurons, in Contrast to the Cadherins, afamily of molecules for Ca^<+1>-dependent adhesion. These molecules have keen implicated in such events as neurite outgrowth, growth Cone guidance, axonal fasciculation, neuroral migration, and myelination. The all interactions of the molecules maytrigger intracellular events, including chages in Calcium Concentration, followed by expression of the functions described above. While some binding properties of L1 have been characterized, the intracellular consequences of adhesion have remained largely Unknown. The complete form of L1 is a large 200KDa molecule of the Ig Superfamily. It contains six Ig domains and five fibronectin type III demains. We determined the complete sequence of rat L1 and analyzed the functions by transfectants. We examined the distribution of Complete L1 and its isoform by PCR methods. while rat and mouse brains contained only the complete form L1, the short isoformot L1 is found in their sciatic nerves. The short form L1 is formed by alternative splicing of L1 mRNA.The deletion segmentot four avnino oeids in the intra cellular dowair contains two possible phosohorylation sites by casein kinase II and I,suggesting a change of L1 function.