scholarly journals Polyclonal rabbit anti-human ovarian cancer globulins inhibit tumor growth through apoptosis involving the caspase signaling

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Shuang Zhang ◽  
Min Yu ◽  
Hongxin Deng ◽  
Guobo Shen ◽  
Yuquan Wei

2007 ◽  
Vol 6 (11) ◽  
pp. 2959-2966 ◽  
Author(s):  
Hung Huynh ◽  
Ching Ching Melissa Teo ◽  
Khee Chee Soo


2021 ◽  
Vol 6 (57) ◽  
pp. eabh3184
Author(s):  
Andrew Lichtman

Intratumoral B cells in ovarian cancers produce IgA, which binds tumor antigens and inhibit tumor growth through myeloid cell–dependent mechanisms or by neutralization of secreted factors, and by antigen-nonspecific binding to poly-Ig receptor on cancer cells leading to transcytosis, which sensitizes the cells for CTL killing.





2021 ◽  
Vol 8 (1) ◽  
pp. 141-155
Author(s):  
Enrique Ortega ◽  
Francisco J. Ballester ◽  
Alba Hernández-García ◽  
Samanta Hernández-García ◽  
M. Alejandra Guerrero-Rubio ◽  
...  

Novel Os(ii) arene complexes with a deprotonated ppy or ppy-CHO C^N ligand have been synthesized to selectively act on cancer cells as proteosynthesis inhibitors in vitro and exert antitumor activity in vivo in C. elegans models.



IUBMB Life ◽  
2012 ◽  
Vol 64 (7) ◽  
pp. 636-643 ◽  
Author(s):  
Kristal Duncan ◽  
Henriette Uwimpuhwe ◽  
Akos Czibere ◽  
Devanand Sarkar ◽  
Towia A. Libermann ◽  
...  


2003 ◽  
Vol 384 (7) ◽  
pp. 1097-1102 ◽  
Author(s):  
J. Krol ◽  
C. Kopitz ◽  
A. Kirschenhofer ◽  
M. Schmitt ◽  
U. Magdolen ◽  
...  

AbstractSeveral proteolytic systems are involved in (anti)adhesive, migratory, and proteolytic processes, necessary for tumor progression and metastasis. We analyzed whether multifunctional inhibitors of different tumor-associated proteolytic systems reduce tumor growth and spread of human ovarian cancer cells in vivo. Bifunctional inhibitors are composed of the N-terminal domain of either the human matrix metalloproteinase inhibitors TIMP-1 or TIMP-3 and the cysteine protease inhibitor chicken cystatin (chCysWT); trifunctional inhibitors are composed of N-TIMP-1 or -3 and a chicken cystatin variant harboring the uPAR binding site of uPA, chCys-uPA19-31, which in addition to its inhibitory activity toward cysteine proteases interferes with the interaction of the serine protease uPA with its receptor. OV-MZ-6#8 cancer cells, stably transfected with plasmids expressing the multifunctional inhibitors, displayed similar proliferative and adhesive features as the vector-transfected control, but showed significant reduction in their invasive behavior in vitro. The cell lines expressing the multifunctional inhibitors were inoculated into the peritoneum of nude mice. Expression of three of the four inhibitor variants (NhTIMP-1-chCysWT, N-hTIMP-1- chCys-uPA19-31, and N-hTIMP-3-chCysWT) resulted in a significant reduction of tumor burden compared to the vector-control cell line. These compact and small inhibitors may represent promising agents for gene therapy of solid malignant tumors.



1998 ◽  
Vol 89 (7) ◽  
pp. 733-740 ◽  
Author(s):  
Hideyuki Nakata ◽  
Yoshihiro Kikuchi ◽  
Takehiko Tode ◽  
Junko Hirata ◽  
Tsunekazu Kita ◽  
...  


2013 ◽  
Vol 62 (5) ◽  
pp. 889-895 ◽  
Author(s):  
Mingjun Liu ◽  
Jinbao Zong ◽  
Zimin Liu ◽  
Ling Li ◽  
Xu Zheng ◽  
...  


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