Abstract
Neuroleukin is a neurotrophic factor of relative molecular mass (Mr) 56,000 (56K) found in skeletal muscle, brain, heart and kidneys which supports the survival of embryonic spinal neurones, skeletal motor neurones and sensory neurons1. Neuroleukin is also a lymphokine product of lectin-stimulated T cells and induces immunoglobulin secretion by cultured human peripheral blood mononuclear cells2>. Mouse neuroleukin has been cloned, the complete nucleotide sequence has been determined1 and its complementary DNA has been transiently expressed in monkey COS-1 cells. The serum-free supernatant of the transfected, but not of control mock-transfected, cells was shown to mimic the properties of neuroleukin isolated from mouse salivary glands. In our work on the molecular genetics of carbohydrate metabolism3 we have recently isolated a mouse glucose-6-phosphate isomerase (or phos-phoglucose isomerase, PGI) cDNA clone using the yeast PGI gene (PGI I) 4 as a probe. We report here that there is complete sequence identity between the 759 nucleotides at the 3′ end of this clone (coding and non-coding) and the sequence of mouse neuroleukin.
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Faik, P., Walker, J., Redmill, A. et al. Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3′ sequences . Nature 332, 455–456 (1988). https://doi.org/10.1038/332455a0
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DOI: https://doi.org/10.1038/332455a0
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