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Characterization of G-protein α subunits in the Gq class: expression in murine tissues and in stromal and hematopoietic cell lines

Wilkie, Thomas M. and Scherle, Peggy A. and Strathmann, Michael P. and Slepak, Vladlen Z. and Simon, Melvin I. (1991) Characterization of G-protein α subunits in the Gq class: expression in murine tissues and in stromal and hematopoietic cell lines. Proceedings of the National Academy of Sciences of the United States of America, 88 (22). pp. 10049-10053. ISSN 0027-8424. PMCID PMC52865. doi:10.1073/pnas.88.22.10049.

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Murine Gα14 and Gα15 cDNAs encode distinct α subunits of heterotrimeric guanine nucleotide-binding proteins (G proteins). These alpha subunits are related to members of the Gq class and share certain sequence characteristics with Gαq, Gα11, and Gα16, such as the absence of a pertussis toxin ADP-ribosylation site. Gα11 and Gαq are ubiquitously expressed among murine tissues but G alpha 14 is predominantly expressed in spleen, lung, kidney, and testis whereas Gα15 is primarily restricted to hematopoietic lineages. Among hematopoietic cell lines, Gα11 mRNA is found in all cell lines tested, Gαq is expressed widely but is not found in most T-cell lines, Gα15 is predominantly expressed in myeloid and B-cell lineages, and Gα14 is expressed in bone marrow adherent (stromal) cells, certain early myeloid cells, and progenitor B cells. Polyclonal antisera produced from synthetic peptides that correspond to two regions of Gα15 react with a protein of 42 kDa expressed in B-cell membranes and in Escherichia coli transformed with Gα15 cDNA. The expression patterns that were observed in mouse tissues and cell lines indicate that each of the alpha subunits in the Gq class may be involved in pertussis toxin-insensitive signal-transduction pathways that are fundamental to hematopoietic cell differentiation and function.

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Additional Information:© 1991 National Academy of Sciences. Contributed by Melvin I. Simon, July 26, 1991. We thank Owen Witte, Cindy Guidos, Jane Danska, Pontelis Tsoulfas, and David Scott for their contributions of RNA isolated from hematopoietic and stromal cell lines; Andy McMahon for ES and yolk sac RNA; Willie Born for providing a series of BW5147 cell lines; Jane Johnson and Dianqing Wu for RNA from nonhematopoietic cell lines; and Tom Amatruda for affinity-purified antisera. We thank Lee Kozar and Carol Lee for computor and technical assistance, Mike Lochrie for the expression plasmid pML52, and the California Institute of Technology Microchemical Facility for peptides and oligonucleotides. We thank Owen Witte and Karen Chaffin for their comments on the manuscript. This work was supported by a National Institutes of Health postdoctoral fellowship to T.M.W. (GM11576), a Howard Hughes Medical Institute fellowship to P.A.S. while in the O. Witte Laboratory, and a National Institutes of Health grant to M.I.S. (GM34236). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
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NIH Postdoctoral FellowshipUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Subject Keywords:PTX, pertussis toxin; PLC, phospholipase C; ES cells, embryonic stem cells.
Issue or Number:22
PubMed Central ID:PMC52865
Record Number:CaltechAUTHORS:20120418-145940578
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:30180
Deposited On:18 Apr 2012 22:25
Last Modified:09 Nov 2021 19:38

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