Abstract
Degenerate oligonucleotide primers were employed in PCRs to clone protein tyrosine kinases that may play potential roles in the development of the mammalian CNS. Using one PCR clone to screen a mouse eye cDNA library, a full-length cDNA of a cytoplasmic tyrosine kinase, the homolog of human JAK1, was obtained. The murine JAK1 kinase belongs to a new family of cytoplasmic kinases that contain two tandem catalytic domains. Northern analyses indicated that murine JAK1 mRNA is expressed in a variety of tissues and cell lines. In the adult mouse eye, in situ hybridization and immunohistochemistry showed that JAK1 mRNA and protein were expressed in the retinal ganglion cell layer and the inner part of the inner nuclear layer, presumably in amacrine cells. JAK1 protein was also detected in horizontal cells and in the two synaptic layers of the adult retina. During retinal development, JAK1 protein was first detected in retinal ganglion cells and in their axons as early as embryonic day 14. Expression of JAK1 protein in amacrine cells and horizontal cells occurred only postnatally. This pattern of expression was also observed in the chick retina, suggesting an evolutionarily conserved function of JAK1 kinase in vertebrate retinal development and/or function. Immunohistochemical staining against JAK1 was detected in two areas of the adult mouse brain, the olfactory bulb and a group of cells in the hypothalamus. Together, these expression studies suggest a role for JAK1 kinase in the differentiation or function of a subset of CNS neurons.