@article{schmit_pondenis_barger_borst_garrett_wypij_neumann_fan_2012, title={Cathepsin K Expression and Activity in Canine Osteosarcoma}, volume={26}, ISSN={["1939-1676"]}, DOI={10.1111/j.1939-1676.2011.00834.x}, abstractNote={BackgroundCathepsin K (CatK) is a lysosomal protease with collagenolytic activity, and its secretion by osteoclasts is responsible for degrading organic bone matrix. People with pathologic bone resorption have higher circulating CatK concentrations.HypothesisCanine osteosarcoma (OS) cells will possess CatK, and its secretion will be cytokine inducible. Circulating CatK concentrations will be increased in dogs with OS, and will be a surrogate marker of bone resorption.AnimalsFifty‐one dogs with appendicular OS and 18 age‐ and weight‐matched healthy control dogs.MethodsIn a prospective study, expressions of CatK mRNA and protein were investigated in OS cells. The inducible secretion and proteolytic activity of CatK from OS cells was assessed in vitro. Serum CatK concentrations were quantified in normal dogs and dogs with OS and its utility as a bone resorption marker was evaluated in dogs with OS treated with palliative radiation and antiresorptive agents.ResultsCanine OS cells contain preformed CatK within cytoplasmic vesicles. In OS cells, TGFβ1 induced the secretion of CatK, which degraded bone‐derived type I collagen in vitro. CatK concentrations were higher in dogs with OS than healthy dogs (11.3 ± 5.2 pmol/L versus 8.1 ± 5.0 pmol/L, P = .03). In a subset of dogs with OS, pretreatment CatK concentrations gradually decreased after palliative radiation and antiresorptive treatment, from 9.3 ± 3.2 pmol/L to 5.0 ± 3.1 pmol/L, P = .03.Conclusions and Clinical ImportanceCanine OS is associated with pathologic bone resorption, and CatK inhibitors might aid in the management of canine OS‐related malignant osteolysis.}, number={1}, journal={JOURNAL OF VETERINARY INTERNAL MEDICINE}, author={Schmit, J. M. and Pondenis, H. C. and Barger, A. M. and Borst, L. B. and Garrett, L. D. and Wypij, J. M. and Neumann, Z. L. and Fan, T. M.}, year={2012}, pages={126–134} }
 @article{birkenheuer_whittington_neel_large_barger_levy_breitschwerdt_2006, title={Molecular characterization of a Babesia species identified in a North American raccoon}, volume={42}, ISSN={["1943-3700"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-33748280658&partnerID=MN8TOARS}, DOI={10.7589/0090-3558-42.2.375}, abstractNote={Piroplasmosis was first described in raccoons (Procyon lotor) in 1926, and the official description of a small piroplasm as Babesia lotori was done in 1981. Babesia microti-like gene sequences have been characterized in raccoons in both North American and Japan. It is well documented that the microscopic appearance of piroplasms does not always accurately predict the genotype and phylogenetic classification. Discrepancies using phenotype to predict genotype have been reported most frequently when evaluating small piroplasms. We amplified and sequenced the full-length 18S rRNA gene from a small piroplasm identified in a raccoon and used this sequence for phylogenetic analyses. Based on these analyses, the organism was placed in the Babesia sensu stricto clade, confirming that it is a true Babesia sp. This documents that at least two Babesia spp. can infect raccoons. The data generated in this study can be used to design molecular diagnostic tests for detection of this Babesia sp., which will be useful for epidemiologic and comparative phylogenetic studies. As piroplasmosis has been documented with increased frequency in humans in recent years, the results of this study will aid in the recognition of zoonotic babesiosis.}, number={2}, journal={JOURNAL OF WILDLIFE DISEASES}, author={Birkenheuer, Adam J. and Whittington, Julia and Neel, Jennifer and Large, Edward and Barger, Anne and Levy, Michael G. and Breitschwerdt, Edward B.}, year={2006}, month={Apr}, pages={375–380} }
 @article{dean_barger_lavoy_2005, title={Cloning and expression of feline interleukin 15}, volume={29}, ISSN={["1096-0023"]}, DOI={10.1016/j.cyto.2004.09.012}, abstractNote={A cDNA encoding feline interleukin 15 (IL15) was cloned from the lymph node of a cat infected with feline infectious peritonitis virus. The cDNA is 486 bp in length and encodes a protein of 162 amino acids. Recombinant protein was readily expressed as a GST fusion in Escherichia coli and purified by glutathione affinity chromatography. Expression of recombinant protein in mammalian cells was only accomplished by eliminating the 5′ and 3′ UTR, replacing the IL15 signal peptide with the tissue plasminogen activator signal peptide, and adding 3′ sequence to disrupt presumptive secondary structure of the mRNA. Biologically active feline IL15 was expressed in HEK293T cells and was shown to sustain primary feline lymphocytes, a feline T cell line, and mouse CTLL-2 cells. Proliferation of CTLL-2 cells was induced by the recombinant protein in a dose-dependent manner. Monoclonal and polyclonal antibodies against human IL15 recognized feline IL15 in immunofluorescence and Western blot assays. Additionally, feline IL15 was detectable using a commercially available human IL15 ELISA kit.}, number={2}, journal={CYTOKINE}, author={Dean, GA and Barger, A and LaVoy, A}, year={2005}, month={Jan}, pages={77–83} }
 @article{barger_grindem_2000, title={Analyzing the results of a complete blood cell count}, volume={95}, number={7}, journal={Veterinary Medicine}, author={Barger, A. M. and Grindem, C. B.}, year={2000}, pages={534} }
 @article{barger_grindem_1997, title={What is your diagnosis? A seven-year-old mixed breed dog - Bromide toxicity}, volume={26}, ISSN={["0275-6382"]}, DOI={10.1111/j.1939-165X.1997.tb00728.x}, abstractNote={Veterinary Clinical PathologyVolume 26, Issue 4 p. 164-164 A Seven-Year-Old Mixed Breed Dog Anne Barger, Anne Barger Department of Microbiology, Pathology and Parasitology, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, North Carolina 27606Search for more papers by this authorCarol B. Grindem, Carol B. Grindem Department of Microbiology, Pathology and Parasitology, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, North Carolina 27606Search for more papers by this author Anne Barger, Anne Barger Department of Microbiology, Pathology and Parasitology, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, North Carolina 27606Search for more papers by this authorCarol B. Grindem, Carol B. Grindem Department of Microbiology, Pathology and Parasitology, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, North Carolina 27606Search for more papers by this author First published: 23 February 2009 https://doi.org/10.1111/j.1939-165X.1997.tb00728.xCitations: 2AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article.Citing Literature Volume26, Issue4December 1997Pages 164-164 RelatedInformation}, number={4}, journal={VETERINARY CLINICAL PATHOLOGY}, author={Barger, A and Grindem, CB}, year={1997}, pages={164-+} }