Functional characterization of Pactolus, a beta-integrin-like protein preferentially expressed by neutrophils - PubMed (original) (raw)
. 2001 Sep 21;276(38):35500-11.
doi: 10.1074/jbc.M104369200. Epub 2001 Jul 18.
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- PMID: 11461913
- DOI: 10.1074/jbc.M104369200
Free article
Functional characterization of Pactolus, a beta-integrin-like protein preferentially expressed by neutrophils
S Garrison et al. J Biol Chem. 2001.
Free article
Abstract
Murine Pactolus is a beta-integrin-like molecule expressed exclusively on the surface of granulocytes. Cell surface expression of Pactolus is dramatically increased following activation of bone marrow neutrophils with known agonists, and cross-linking of cell surface Pactolus, suggesting the bulk of the protein is in intracellular stores. The mature protein is found in two forms depending upon the extent of N-linked glycosylation. There is no evidence to suggest that Pactolus requires an associated alpha chain for expression. In some mouse strains, a truncated form of the protein is predicted based upon alternative splicing: this form, however, is unstable and rapidly degraded after synthesis. Differences in the quantities of these Pactolus mRNA isoforms have defined two alleles. BALB/c and C3H/HeJ mice possess allele B and preferentially express the truncated, unstable product, whereas C57BL/6 mice possess allele A and only produce the membrane-bound form. Sequence analysis has shown the difference between these two alleles is due to a single base pair difference at the splice acceptor site for the truncated product. The increased expression of the membrane form of Pactolus by granulocytes of C57BL/6 mice suggests a compensatory adhesion function that is reduced in cells from the low producing strains.
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