Julia B Jernberg

Interests

Research

ClimateEnvironmentOne Health

Teaching

Interested in problem solving and creative thinking, within the context of critical analysesClimate Environment Public Health/One Health

Courses

Scholarly Contributions

Journals/Publications

• Klotz, S. A., Jernberg, J. B., & Robbins, R. A. (2023). Turn Healthcare Workers Loose with Outpatient Telemedicine-Let Them Decide Its Fate; No Top-Down Decisions on What It Can and Cannot Do. The American journal of medicine, 136(10), 955-957.
• Najjar, S. M., Accili, D., Philippe, N., Jernberg, J., Margolis, R., & Taylor, S. I. (1993). pp120/ecto-ATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isoforms. The Journal of biological chemistry, 268(2), 1201-6.
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  The insulin receptor possesses tyrosine kinase activity which is thought to mediate the biological effects of insulin upon target cells. pp120 is a liver-specific glycoprotein of apparent molecular size of 120 kDa that is phosphorylated on tyrosine residues by the receptors for insulin, insulin-like growth factor-I, and epidermal growth factor. Previously, we demonstrated that pp120 is identical to a liver-specific ecto-ATPase. In the present study, we have cloned the rat gene encoding pp120/ecto-ATPase. The gene is contained within approximately 15 kilobases of genomic DNA, and consists of nine exons interrupted by eight introns. Using the reverse transcriptase/polymerase chain reaction, we isolated cDNA clones complementary to rat liver mRNA encoding pp120/ecto-ATPase. Sequence analysis indicated the presence of two populations of cDNA's that differ by the presence or absence of a 53-base pair (bp) fragment encoding the juxta-membrane region of the cytoplasmic domain. By cloning the corresponding region of the ecto-ATPase gene, we demonstrated that the 53-bp represents exon 7 of the gene. This 53-bp exon undergoes alternative splicing, thereby giving rise to two mRNA variants. Deletion of this 53-bp cassette exon introduces a frameshift, and results in a premature chain termination codon that truncates the cytoplasmic domain. The truncated cytoplasmic domain contains 10 rather than 71 amino acid residues. Because the short isoform of ecto-ATPase lacks the putative sites for tyrosine- and serine-specific phosphorylation, this alternative splicing may have a major effect upon the physiological function of the enzyme.
• Ambrosino, D. M., Siber, G. R., Chilmonczyk, B. A., Jernberg, J. B., & Finberg, R. W. (1987). An immunodeficiency characterized by impaired antibody responses to polysaccharides. The New England journal of medicine, 316(13), 790-3.