@article{mozdziak_wu_bradford_pardue_borwornpinyo_giamario_petitte_2006, title={Identification of the lacZ insertion site and beta-galactosidase expression in transgenic chickens}, volume={324}, ISSN={["1432-0878"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-33644623527&partnerID=MN8TOARS}, DOI={10.1007/s00441-005-0060-9}, abstractNote={The quail:chick chimera system is a classical research model in developmental biology. An improvement over the quail:chick chimera system would be a line of transgenic chickens expressing a reporter gene. Transgenic chickens carrying lacZ and expressing bacterial beta-galactosidase have been generated, but complete characterization of the insertion event and characterization of beta-galactosidase expression have not previously been available. The genomic sequences flanking the retroviral insertion site have now been identified by using inverse polymerase chain reaction (PCR), homozygous individuals have been identified by using PCR-based genotyping, and beta-galactosidase expression has been evaluated by using Western analysis and histochemistry. Based upon the current draft of the chicken genome, the viral insertion carrying the lacZ gene has been located on chromosome 11 within the predicted gene for neurotactin/fractalkine (CX3CL1); neurotactin mRNA expression appears to be missing from the brain of homozygous individuals. When Generation 2 (G2) lacZ-positive individuals were inter-mated, they generated 361 G3 progeny; 82 were homozyous for lacZ (22.7%), 97 were wild-type non-transgenic (26.9%), and 182 (50.4%) were hemizygous for lacZ. Western analysis revealed the highest expression in the muscle and liver. With the identification of homozygous birds, the line of chickens is now designated NCSU-Blue1.}, number={1}, journal={CELL AND TISSUE RESEARCH}, author={Mozdziak, PE and Wu, Q and Bradford, JM and Pardue, SL and Borwornpinyo, S and Giamario, C and Petitte, JN}, year={2006}, month={Apr}, pages={41–53} }
 @article{borwornpinyo_brake_mozdziak_petitte_2005, title={Culture of chicken embryos in surrogate eggshells}, volume={84}, ISSN={["1525-3171"]}, url={http://europepmc.org/abstract/med/16206571}, DOI={10.1093/ps/84.9.1477}, abstractNote={The chick embryo is a classical model to study embryonic development. However, most researchers have not studied the effect of embryonic manipulation on chick hatchability. The objective of this study was to determine the effect of egg orientation and type of sealing film on the hatchability of cultured embryos. Windows were made in the small end of recipient surrogate chicken eggshells, and donor embryos were placed into the recipient eggshell for the first 3 d of incubation. Survival over the first 3 d was maximized (P < 0.05) when windowed eggs sealed with Saran Wrap were positioned with the window-end down compared with window-end up. Three-day-old cultured embryos were transferred into recipient turkey eggshells, sealed with cling film, and cultured until hatch. Water weight loss of the surrogate eggshell cultures regardless of cling film type was not significantly different from control intact eggs. The embryos cultured in turkey eggshells and sealed with Handi Wrap exhibited higher hatchability (75% +/- 10.2%) than cultures sealed with Saran Wrap (45.2% +/- 13.8%). Hatchability of control intact eggs (86.4% +/- 5.3%) was not significantly (P > 0.05) different from the hatchability of eggs sealed with Handi Wrap, which suggested that Handi Wrap was an excellent sealant for chick embryos cultured after 3 d of incubation.}, number={9}, journal={POULTRY SCIENCE}, author={Borwornpinyo, S and Brake, J and Mozdziak, PE and Petitte, JN}, year={2005}, month={Sep}, pages={1477–1482} }
 @article{wang_borwornpinyo_odetallah_shih_2005, title={Enzymatic degradation of a prion-like protein, Sup35NM-His6}, volume={36}, ISSN={["1879-0909"]}, DOI={10.1016/j.enzmictec.2004.12.023}, abstractNote={Recent studies indicate that enzymatic treatment of the infectious PrPSc prion under defined conditions could be an effective method to inactivate infectious prions. However, field studies on prion inactivation are hampered by restricted access to the dangerous and expensive infectious prion material. Hence, a surrogate marker for infectious prions would facilitate more practical prion inactivation research. Protein Sup35p, a non-pathogenic prion-like protein produced in yeast, has physical and chemical properties very similar to the BSE prion. Sup35NM-His6, a derivative of Sup35p, was produced from Escherichia coli by gene cloning, protein expression and purification. Monomeric Sup35NM-His6 is soluble. When aggregated, it forms prion-like amyloid, insoluble and resistant to proteases. Similar to BSE prion, a pre-heating step renders this protein digestible by proteinase K, subtilisin and keratinase but not collagenase and elastase. These results indicated that Sup35NM-His6, being simple and inexpensive to produce and non-pathogenic, can be a potential ideal candidate of prion surrogate protein in the study of prion inactivation and prevention of prion diseases.}, number={5-6}, journal={ENZYME AND MICROBIAL TECHNOLOGY}, author={Wang, JH and Borwornpinyo, R and Odetallah, N and Shih, JCH}, year={2005}, month={Apr}, pages={758–765} }
 @article{mozdziak_borwornpinyo_mccoy_petitte_2003, title={Development of transgenic chickens expressing bacterial beta-galactosidase}, volume={226}, ISSN={["1097-0177"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0037370171&partnerID=MN8TOARS}, DOI={10.1002/dvdy.10234}, abstractNote={Abstract}, number={3}, journal={DEVELOPMENTAL DYNAMICS}, author={Mozdziak, PE and Borwornpinyo, S and McCoy, DW and Petitte, JN}, year={2003}, month={Mar}, pages={439–445} }
 @article{mozdziak_pophal_borwornpinyo_petitte_2003, title={Transgenic chickens expressing beta-galactosidase hydrolyze lactose in the intestine}, volume={133}, ISSN={["1541-6100"]}, url={http://europepmc.org/abstract/med/14519787}, DOI={10.1093/jn/133.10.3076}, abstractNote={Chickens do not possess the necessary enzymes to efficiently hydrolyze lactose into glucose and galactose. The bacterial enzyme beta-galactosidase can convert lactose into glucose and galactose. Transgenic chickens that carry the E. coli lacZ gene and express beta-galactosidase could potentially utilize lactose as an energy source. The objective of this study was to determine the ability of the transgenic chicken small intestinal mucosa to hydrolyze lactose into glucose and galactose. Lactase activity was examined in the intestinal muscosa from wild-type chickens and two lines of chickens that carry the lacZ gene and express beta-galactosidase. Lactase activity was significantly higher in both transgenic lines compared with wild-type birds (P < 0.05). The presence of the beta-galactosidase enzyme was revealed by X-gal staining in the intestine of transgenic chickens, whereas it was not present in the wild-type chickens. Overall, it appears that inserting the lacZ gene, which encodes beta-galactosidase, has resulted in a chicken that can utilize lactose as an energy source. This study demonstrates that transgenic technology can be used to modify nutrient utilization in domestic poultry.}, number={10}, journal={JOURNAL OF NUTRITION}, author={Mozdziak, PE and Pophal, S and Borwornpinyo, S and Petitte, JN}, year={2003}, month={Oct}, pages={3076–3079} }