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Peptide:MHC Tetramer-based Enrichment of Epitope-specific T cells
Published on: October 22, 2012
Quantification of hemokinin-1 peptide production and secretion from mouse B cells
Daniel A Nelson1, Kenneth L Bost
1Department of Biology, 9201 University City Boulevard, University of North Carolina at Charlotte, Charlotte, NC 28223, USA. danelson@email.uncc.edu
Abstract:
Hemokinin-1 is a recent addition to the family of mammalian tachykinins and is thought to play an important role in B cell and T cell lymphopoiesis. The mRNA coding for this peptide was expressed in some B lymphocyte cell lines including 70Z/3.12, ABE-8.1/2, and RAW8.1 cells, suggesting the possibility that hemokinin-1 may function in an autocrine or paracrine manner in these cells. Therefore, we quantified secretion of this peptide from the 70Z/3.12 cell line expressing hemokinin-1 mRNA. Despite a sensitive radioimmunoassay, we were surprised to find that hemokinin-1 secretion from confluent cells was below the level of detection of this assay. Furthermore, cell lysates routinely demonstrated a low or undetectable immunoreactive peptide. Collectively these studies show a limited production of hemokinin-1 peptide by transformed B cells.
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