@article{teng_gladwell_beard_walmer_teng_brenner_2002, title={Lactoferrin gene expression is estrogen responsive in human and rhesus monkey endometrium}, volume={8}, ISSN={["1360-9947"]}, DOI={10.1093/molehr/8.1.58}, abstractNote={We have previously shown that the estrogen responsiveness of the human lactoferrin gene in a transient transfection system is mediated through an imperfect estrogen response element (ERE) and a steroidogenic factor 1 binding element (SFRE) 26 bp upstream from ERE. Reporter constructs containing SFRE and ERE respond to estrogen stimulation in a dose-dependent manner, whereas mutations at either one of the response elements severely impaired the estrogen responsiveness. In this study, we demonstrated that estrogen receptor (ERalpha) binds to the human lactoferrin gene ERE and forms two complexes in an electrophoresis mobility shift assay (EMSA). These complexes could be supershifted by an antibody to ERalpha. We also showed that in normal cycling women, lactoferrin gene expression in the endometrium increases during the proliferative phase and diminishes during the luteal phase. This in-vivo study thus supported the finding from transient transfection experiments that the human lactoferrin gene expression is elevated in an environment with a high level of estrogen. The estrogen effect on lactoferrin gene expression in the rhesus monkey endometrium was studied by Western blotting and immunohistochemistry. The immunohistochemistry results showed that immunoreactive lactoferrin protein was not detectable in the untreated ovariectomized monkey endometrium, was elevated by estrogen treatment, and was suppressed by sequential, combined estrogen plus progesterone treatment. In conclusion, this study has shown that lactoferrin gene expression is responsive to estrogen in primate endometrium.}, number={1}, journal={MOLECULAR HUMAN REPRODUCTION}, author={Teng, CT and Gladwell, W and Beard, C and Walmer, D and Teng, CS and Brenner, R}, year={2002}, month={Jan}, pages={58–67} }
 @article{teng_2001, title={Differential activation of MAPK during Mullerian duct growth and apoptosis: JNK and p38 stimulation by DES blocks tissue death}, volume={306}, ISSN={["0302-766X"]}, DOI={10.1007/s004410100426}, abstractNote={To investigate the involvement of the mitogen-activated protein kinases (MAPKs) in c-Jun-mediated Müllerian duct (MD) differentiation, Western immunoblot with antibodies against c-Jun N-terminal kinase (JNK), extracellular signal-regulated kinases (ERK1 and 2), p38, phosphorylated JNK (p-JNK), and p-ERK were used to investigate these kinases in the left and right MDs (LMD and RMD, respectively) of female chicks. The content of these kinases in the LMD and RMD of various stages of embryos was detected by measuring their density in autoradiograms by a Spot-denso-program with Alpha Ease software. In the LMD, the growing embryonic sex tract, the amount of JNK increased from the 8th to 10th embryonic day and reached its highest at the 12th to 18th day. The content of ERK1, ERK2, and p38 remained at the same level throughout development. In the RMD, the apoptotic embryonic sex tract, the level of these four MAPKs showed a linear increase from the 8th to 10th day and then declined at the 12th day. Before the RMD entered the apoptotic stages (10th day of incubation), MAPKs were overexpressed. The findings following the application of p-MAPK antibodies, e.g., p-JNK and p-ERK, mirrored the result showing that differential activation of MAPKs existed in the LMD and RMD. When the RMD entered the apoptotic stages (13th to 18th day of incubation), the reduction in JNK activity was higher than that of the other three kinases. The apoptotic death of RMD was prevented by in vivo diethylstilbestrol treatment, which restored the level of JNK, p-JNK, and p38. No stimulatory effect was found for ERK and p-ERK.}, number={1}, journal={CELL AND TISSUE RESEARCH}, author={Teng, CS}, year={2001}, month={Oct}, pages={27–34} }
 @inproceedings{teng_2001, title={JNK modulates the effect of Bcl-2 on the growth or apoptosis of chick Mullerian ducts}, volume={12}, number={2001 Nov}, booktitle={Molecular Biology of the Cell}, author={Teng, C. S.}, year={2001}, pages={124} }
 @article{teng_2000, title={Differential expression of c-Jun proteins during Mullerian duct growth and apoptosis: caspase-related tissue death blocked by diethylstilbestrol}, volume={302}, ISSN={["0302-766X"]}, DOI={10.1007/s004410000288}, abstractNote={To elucidate whether the differentiation of the Müllerian duct (MD) is mediated by c-Jun proteins, Western immunoblot with c-Jun/sc-45 antibody was used to investigate these proteins in female chick left and right MDs (LMD and RMD, respectively). The content of these proteins (e.g., the 66-kDa, 45-kDa, and 39-kDa forms) in the LMD or RMD of various stages of embryos was detected by measuring their density in autoradiograms by a Spot-denso-program with Alpha Ease software. In the LMD, the growing embryonic sex tract, the content of the 66-kDa and 39-kDa proteins increased to their highest level in 9th to 12th day embryos and then declined thereafter. In the RMD, the apoptotic embryonic sex tract, the content of these proteins also showed a linear increase from the 9th to 10th day and then declined at the 13th day. When the RMD entered the apoptosis stages (14th to 18th day of incubation), these proteins were persistently overexpressed. Another protein (45 kDa) was detected in both ducts only at the 9th to 13th days, and its content was higher in RMD than in the LMD. In parallel to this finding, high caspase-3 activity (determined by the measurement of the fragmented 85-kDa poly ADP-ribose polymerase) was found in the RMD during apoptosis. The apoptotic death of RMD was prevented by in vivo diethylstilbestrol treatment, which inhibited the overexpression of the 66-kDa and 45-kDa proteins, the fragmentation of DNA, and the activity of caspase-3. No inhibitory effect was found for the 39-kDa protein.}, number={3}, journal={CELL AND TISSUE RESEARCH}, author={Teng, CS}, year={2000}, month={Dec}, pages={377–385} }
 @article{teng_2000, title={Protooncogenes as mediators of apoptosis}, volume={197}, number={2000}, journal={International Review of Cytology}, author={Teng, C. S.}, year={2000}, pages={137–202} }
 @article{teng_vilagrasa_1998, title={Biphasic c-Myc protein expression during gossypol-induced apoptosis in rat spermatocytes}, volume={57}, ISSN={["0010-7824"]}, DOI={10.1016/S0010-7824(98)00010-9}, abstractNote={The presence of protooncogene products such as c-Myc proteins in rat spermatocytes has been quantitatively detected by Western immunoblot and a computer-controlled Spot-denso-program with an IS-1000 digital imaging system. Cellular levels of c-Myc proteins in response to gossypol were measured in spermatocytes during the process of gossypol-induced apoptosis. Within 0.5 to 2 h of the addition of gossypol, levels of c-Myc proteins fall dramatically and remain at a low level for the next several hours. The reduction in c-Myc proteins occurs 4.5–6 h before the apoptosis of spermatocytes in the presence of gossypol. Between 3 and 5 h after exposure to gossypol, the c-Myc protein content returns to preexposure (or higher) levels. In addition, the increase in c-Myc proteins occurs 1.5–4 h before the apoptotic death of spermatocytes. An identical pattern of c-Myc protein response to gossypol was also found in total testicular tissue in vitro. These results suggest that spermatocyte apoptosis induced by gossypol is correlated with biphasic c-Myc protein expression. This article presents some hypothetical models with which to explain c-Myc protein-mediated apoptosis.}, number={2}, journal={CONTRACEPTION}, author={Teng, CS and Vilagrasa, X}, year={1998}, month={Feb}, pages={117–123} }
 @article{teng_1998, title={c-fos protein expression in apoptotic rat spermatocytes induced by gossypol}, volume={57}, ISSN={["0010-7824"]}, DOI={10.1016/S0010-7824(98)00023-7}, abstractNote={Proto-oncogene products such as c-fos protein with a molecular weight of 62 kDa have been identified in rat spermatocytes. In this study, cellular levels of c-fos proteins in spermatocyte, either with or without gossypol exposure, were quantitatively detected by Western immunoblot and a computer-controlled Spot-denso-program with an IS-1000 Digital Imaging System. Within 0.5-3.5 h (an average of 2 h) of the addition of gossypol, levels of c-fos proteins fell dramatically. The reduction in c-fos proteins occurred 6 h before the apoptosis of spermatocytes in the presence of gossypol. Four hours after exposure to gossypol, the c-fos protein content was overexpressed. The period of c-fos up-regulation lasted for approximately 8 h. The increase in c-fos protein coincided with a high rate of apoptotic cell death. Morphologic structure of the dying cell was revealed by electron microscopy. These results suggest that spermatocyte apoptosis induced by gossypol correlates with biphasic c-fos protein-mediated apoptosis.}, number={4}, journal={CONTRACEPTION}, author={Teng, CS}, year={1998}, month={Apr}, pages={281–286} }
 @article{teng_1997, title={Reversible changes in the content of cellular and microtubular tubulin in spermatogenic cells after gossypol treatment}, volume={55}, ISSN={["0010-7824"]}, DOI={10.1016/S0010-7824(96)00240-5}, abstractNote={After exposure of young male rats to gossypol acetic acid for various times, a reduction in the content of cellular and microtubular β-tubulin was found in spermatocytes and spermatids. The content of tubulin was measured by enzyme-linked immunosorbent assay (ELISA). The results were expressed as micrograms tubulin/100 μg total protein and compared with those of the control rats. After drug treatment for 2, 6, 12, and 20 weeks, the content of total cell tubulin in spermatocyte was reduced by 2.4%, 8.8%, 52%, and 61%, respectively; whereas the content of tubulin in spermatid was reduced by 7.4%, 36%, 70%, and 72%, respectively. At the same time length of drug treatment, the content of microtubular tubulin in spermatocyte was reduced by 1.6% 13%, 58%, and 61% in comparison to the reduction rate of 5%, 37%, 69%, and 77%, respectively, for spermatid. These results indicated that the tubulin associated with spermatids were more vulnerable to gossypol than that of the spermatocytes. Eight weeks after withdrawal of the drug treatment, the content of tubulin in spermatocytes and spermatids was recovered.}, number={1}, journal={CONTRACEPTION}, author={Teng, CS}, year={1997}, month={Jan}, pages={41–46} }
 @article{teng_1993, title={BIOLOGICAL-ACTIVITY IN THE REPOPULATING RAT SPERMATOCYTE AFTER THE WITHDRAWAL OF GOSSYPOL TREATMENT .4. THE ACTIVITY FOR THE MODIFICATION OF CORE HISTONES}, volume={48}, ISSN={["0010-7824"]}, DOI={10.1016/0010-7824(93)90007-T}, abstractNote={Mature male rats were treated with gossypol for 8 weeks. Afterwards, treatment was halted to allow the arrested spermatogonia to revive. Fifteen days after the withdrawal of the drug treatment, the repopulating pachytene spermatocyte (RPS) had a lower level of core histone H3 and H4 acetylation (40 and 55% reduction, respectively) than that of the control pachytene spermatocyte (CPS). The reduction in core histone acetylation was found in histone H3 and H4 but not in H2A and H2B. Forty-five days after the withdrawal of the drug treatment, the inhibitory effect on core histone acetylation was recovered. Both dot-blot and standard liquid assays were used to detect the nuclear histone acetylase activity in RPS and CPS. Fifteen days after the withdrawal of gossypol treatment, the acetylase type A activity in RPS was reduced by 42% when compared to CPS. It has been concluded that after gossypol treatment, the activity for nucleosomal core histones acetylation was selectively inhibited. This effect is related to an inhibitory effect on the histone acetylase activity.Mature male rats were treated with gossypol for 8 weeks. Then treatment was halted to allow the arrested spermatogonia to revive. 15 days after the withdrawal of the drug treatment, the repopulating pachytene spermatocytes (RPS) had a lower level of core histone H3 and H4 acetylation (40 and 55% reduction, respectively) than that of the control pachytene spermatocytes (CPS). The reduction in core histone acetylation was found in histones H3 and H4, but not in H2A and H2B. 45 days after the withdrawal of the drug treatment, the inhibitory effect on core histone acetylation was recovered. Both dot-blot and standard liquid assays were used to detect the nuclear histone acetylase activity in RPS and CPS. 15 days after the withdrawal of gossypol treatment, the acetylase type A activity in RPS was reduced by 42% when compared to CPS. It was concluded that after gossypol treatment the activity for nucleosomal core histone acetylation was selectively inhibited. This effect is reacted to an inhibitory effect on the histone acetylase activity.}, number={2}, journal={CONTRACEPTION}, author={TENG, CS}, year={1993}, month={Aug}, pages={168–177} }
 @misc{teng_1991, title={CORRELATION OF PLASMA GROWTH-HORMONE LEVEL WITH WASTING SYNDROME IN FELINE AIDS}, volume={5}, ISSN={["0269-9370"]}, DOI={10.1097/00002030-199112000-00026}, abstractNote={Department of Anatomy, Physiological Sciences and Radiology, North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St, Raleigh, NC 27606, USA}, number={12}, journal={AIDS}, author={TENG, CS}, year={1991}, month={Dec}, pages={1542–1543} }