Search

Your search keyword '"Krajewska, Maryla"' showing total 288 results
Start Over Author "Krajewska, Maryla"
288 results on '"Krajewska, Maryla"'

5. Expression of multiple apoptosis-regulatory genes in human breast cancer cell lines and primary tumors

Author

Zapata, Juan M., Krajewska, Maryla, Krajewski, Stanislaw, Huang, Ruo-Pan, Takayama, Shinichi, Wang, Hong-Gang, Adamson, Eileen, and Reed, John C.

Abstract

The expression of several apoptosis-regulating genes was evaluated in 9 human breast cancer cell lines, 2 immortalized human mammary epithelial lines, 1 normal breast tissue biopsy, and 3 primary breast tumors, using a multiple antigen detection (MAD) immunoblotting method. The anti-apoptotic proteins Bcl-2, Bcl-XL, Mcl-1, and BAG-1 were present at immunodetectable levels in 7, 10, 10, and 9 of the 11 lines. Comparing these 11 cell lines among themselves revealed that steady-state levels of Bcl-2, Bcl-XL, Mcl-1, and BAG-1 were present at relatively higher levels in 4, 6, 5, and 5 of the lines, respectively. In contrast, the pro-apoptotic proteins Bax and Bak were detected in all 11 cell lines, and were present at relatively higher levels in 10 and 5 of the 11 lines, respectively. The Interleukin-1β converting enzyme (ICE) homolog CPP32 (Caspase-3) was expressed in 10/11 breast cell lines. High levels of p53 protein, indicative of mutant p53, were found in 8 of the 11 lines and correlated inversely with Bax expression (p=0.01). Bcl-2 and BAG-1 protein levels were positively correlated (p = 0.03). Immunoblot analysis of primary adenocarcinomas revealed expression of the anti-apoptotic proteins Bcl-2, Bcl-XL, Mcl-1, and BAG-1, as well as the pro-apoptotic proteins Bax, Bak, and CPP32, in at least 2 of the 3 tumors examined. Immunohistochemical analysis was also performed for all of these proteins using 20 paraffin-embedded breast cancer biopsy specimens that all contained residual normal mammary epithelium in combination with both invasive cancer and carcinoma in situ. All of these apoptosis-regulating proteins were detected in primary breast cancers, though the percentage of immunopositive tumor cells varied widely in some cases. Comparisons of the intensity of immunostaining in normal mammary epithelium and invasive carcinoma suggested that Bcl-2 immunointensity tends to be lower in cancers than normal breast epithelium (p=0.03), whereas CPP32 immunointensity was generally higher in invasive cancers (p < 0.0001). Taken together, the results demonstrate expression of multiple apoptosis-modulating proteins in breast cancer cell lines and primary tumors, suggesting complexity in the regulation of apoptosis in these neoplasms of mammary epithelial origin.

Published
1998

8. Supplementary Data from Expression of p21 Protein Predicts Clinical Outcome in DLBCL Patients Older than 60 Years Treated with R-CHOP but not CHOP: A Prospective ECOG and Southwest Oncology Group Correlative Study on E4494

Author

Winter, Jane N., primary, Li, Shuli, primary, Aurora, Vikas, primary, Variakojis, Daina, primary, Nelson, Beverly, primary, Krajewska, Maryla, primary, Zhang, Lijun, primary, Habermann, Thomas M., primary, Fisher, Richard I., primary, Macon, William R., primary, Chhanabhai, Mukesh, primary, Felgar, Raymond E., primary, Hsi, Eric D., primary, Medeiros, L. Jeffrey, primary, Weick, James K., primary, Weller, Edie A., primary, Melnick, Ari, primary, Reed, John C., primary, Horning, Sandra J., primary, and Gascoyne, Randy D., primary

Published
2023
Full Text
View/download PDF

14. A Pan-BCL2 Inhibitor Renders Bone-Marrow-Resident Human Leukemia Stem Cells Sensitive to Tyrosine Kinase Inhibition

Author

Goff, Daniel J., Recart, Angela Court, Sadarangani, Anil, Chun, Hye-Jung, Barrett, Christian L., Krajewska, Maryla, Leu, Heather, Low-Marchelli, Janine, Ma, Wenxue, Shih, Alice Y., Wei, Jun, Zhai, Dayong, Geron, Ifat, Pu, Minya, Bao, Lei, Chuang, Ryan, Balaian, Larisa, Gotlib, Jason, Minden, Mark, Martinelli, Giovanni, Rusert, Jessica, Dao, Kim-Hien, Shazand, Kamran, Wentworth, Peggy, Smith, Kristen M., Jamieson, Christina A.M., Morris, Sheldon R., Messer, Karen, Goldstein, Lawrence S.B., Hudson, Thomas J., Marra, Marco, Frazer, Kelly A., Pellecchia, Maurizio, Reed, John C., and Jamieson, Catriona H.M.

Published
2013
Full Text
View/download PDF

29. TNF receptor-associated factor (TRAF) domain and Bcl-2 cooperate to induce small B cell lymphoma/ chronic lymphocytic leukemia in transgenic mice

Author

Zapata, Juan M., Krajewska, Maryla, Morse, Herbert C., III, Choi, Yongwon, and Reed, John C.

Subjects
Lymphocytes -- Research, Genetically modified mice -- Research, Science and technology
Abstract

Transgenic mice overexpressing in B lymphocytes either Bcl-2 or a TNF receptor-associated factor (TRAF)2 mutant lacking the N-terminal RING and zinc finger domains located at the N terminus of the molecule (TRAF2DN), which mimics TRAF1, developed lymphadenopathy and splenomegaly due to polyclonal B cell expansion. Remarkably, TRAF2DN/Bcl-2 double-transgenic mice contained B cell populations similar to those observed in TRAF2DN mice. However, over time, they developed severe splenomegaly and lymphadenopathy, and most animals also developed leukemia, pleural effusion, and, in some cases, ascites associated with monoclonal and oligoclonal B cell neoplasms. The life span of TRAF2DN/Bcl-2 mice was markedly reduced compared with Bcl-2 and TRAF2DN single-transgenics or wild-type littermates. The expanded B cell population of TRAF2DN/Bcl-2 double-transgenic mice was primarily comprised of small/medium-size noncycling [B220.sup.M]/[IgM.sup.H]/[IgD.sup.L]/ [CD21.sup.L]/[CD23.sup.NULL]/[CD11b.sup.+]/[CD5.sup.+] cells that were Bcl-6-negative, consistent with a B-1 phenotype. The cells also expressed high levels of CD54 and other adhesion molecules. In vitro, these B cells showed comparable proliferation rates to those of wild-type counterparts but exhibited markedly increased survival and were resistant to apoptosis induced by chemotherapeutic agents and glucocorticoids. Histopathologic features were consistent with mouse small B cell lymphoma progressing to leukemia with many similarities to human chronic lymphocytic leukemia. Given that many human chronic lymphocytic leukemias overexpress TRAF1 and Bcl-2, our findings suggest that cooperation between Bcl-2 and TRAF pathways contributes to the development of this type of leukemia.

Published
2004

41. BAG1 Over-expression in Brain Protects Against Stroke

Author

Kermer, Pawel, Digicaylioglu, Murat H., Kaul, Marcus, Zapata, Juan M., Krajewska, Maryla, Stenner-Liewen, Frank, Takayama, Shinichi, Krajewski, Stanistan, Lipton, Stuart A., and Reed, John C.

Published
2003

48. BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins

Author

Zhang, Hong, Xu, Qunli, Krajewski, Stanislaw, Krajewska, Maryla, Xie, Zhihua, Fuess, Sally, Kitada, Shinichi, Pawlowski, Krzysztof, Godzik, Adam, and Reed, John C.

Subjects
Cell death -- Physiological aspects, Proteins -- Research, Science and technology, National Academy of Sciences -- Research
Abstract

Two major pathways for induction of apoptosis have been identified--intrinsic and extrinsic. The extrinsic pathway is represented by tumor necrosis factor family receptors, which utilize protein interaction modules known as death domains and death effector domains (DEDs) to assemble receptor signaling complexes that recruit and activate certain caspase-family cell death proteases, namely procaspases-8 and -10. The intrinsic pathway for apoptosis involves the participation of mitochondria, which release caspase-activating proteins. Bcl-2 family proteins govern this mitochondria-dependent apoptosis pathway, with proteins such as Bax functioning as inducers and proteins such as Bcl-2 and Bcl-[X.sub.L] serving as suppressors of cell death. An apoptosis regulator, BAR, was identified by using a yeast-based screen for inhibitors of Bax-induced cell death. The BAR protein contains a SAM domain, which is required for its interactions with Bcl-2 and Bcl-[X.sub.L] and for suppression of Bax-induced cell death in both mammalian cells and yeast. In addition, BAR contains a DED-like domain responsible for its interaction with DED-containing procaspases and suppression of Fas-induced apoptosis. Furthermore, BAR can bridge procaspase-8 and Bcl-2 into a protein complex. The BAR protein is anchored in intracellular membranes where Bcl-2 resides. BAR therefore may represent a scaffold protein capable of bridging two major apoptosis pathways.

Published
2000

Catalog

Books, media, physical & digital resources
See catalog results