scholarly journals Colorectal Cancer Cell Surface Protein Profiling Using an Antibody Microarray and Fluorescence Multiplexing

Author(s):  
Jerry Zhou ◽  
Larissa Belov ◽  
Michael J. Solomon ◽  
Charles Chan ◽  
Stephen J. Clarke ◽  
...  
Tumor Biology ◽  
2017 ◽  
Vol 39 (3) ◽  
pp. 101042831769168 ◽  
Author(s):  
U Subrahmanyeswara Rao ◽  
Prema S Rao

One long-term complication of chronic intestinal inflammation is the development of colorectal cancer. However, the mechanisms linking inflammation to the colorectal tumorigenesis are poorly defined. Previously, we have demonstrated that galectin-4 is predominantly expressed in the luminal epithelia of the gastrointestinal tract, and its loss of expression plays a key role in the colorectal tumorigenesis. However, the mechanism by which galectin-4 regulates inflammation-induced tumorigenesis is unclear. Here, we show that galectin-4 secreted by the colorectal cancer cell lines was bound to the cell surface. Neutralization of surface-bound galectin-4 with anti-galectin-4 antibody resulted in increased cell proliferation with concomitant secretion of several chemokines into the extracellular medium. Neutralization of the surface-bound galectin-4 also resulted in the up-regulation of transcription of 29 genes, several of which are components of multiple inflammation signaling pathways. In an alternate experiment, binding of recombinant galectin-4 protein to cell surface of the galectin-4-negative colorectal cancer cells resulted in increased p27, and decreased cyclin D1 and c-Myc levels, leading to cell cycle arrest and apoptosis. Together, these data demonstrated that surface-bound galectin-4 is a dual function protein—down-regulating cell proliferation and chemokine secretion in galectin-4-expressing colorectal cancer cells on one hand and inducing apoptosis in galectin-4-negative colorectal cancer cells on the other hand.


2017 ◽  
Vol 20 (6) ◽  
pp. 874-890.e7 ◽  
Author(s):  
Amanda J. Collier ◽  
Sarita P. Panula ◽  
John Paul Schell ◽  
Peter Chovanec ◽  
Alvaro Plaza Reyes ◽  
...  

2015 ◽  
Vol 14 (10) ◽  
pp. 2692-2700 ◽  
Author(s):  
Tao Bing ◽  
Dihua Shangguan ◽  
Yinsheng Wang

2016 ◽  
Vol 7 (2) ◽  
pp. 263-278 ◽  
Author(s):  
Akiyoshi Uezumi ◽  
Masashi Nakatani ◽  
Madoka Ikemoto-Uezumi ◽  
Naoki Yamamoto ◽  
Mitsuhiro Morita ◽  
...  

Author(s):  
G.L. Decker ◽  
M.C. Valdizan

A monoclonal antibody designated MAb 1223 has been used to show that primary mesenchyme cells of the sea urchin embryo express a 130-kDa cell surface protein that may be directly involved in Ca2+ uptake required for growth of skeletal spicules. Other studies from this laboratory have shown that the 1223 antigen, although in relatively low abundance, is also expressed on the cell surfaces of unfertilized eggs and on the majority of blastomeres formed prior to differentiation of the primary mesenchyme cells.We have studied the distribution of 1223 antigen in S. purpuratus eggs and embryos and in isolated egg cell surface complexes that contain the cortical secretory vesicles. Specimens were fixed in 1.0% paraformaldehyde and 1.0% glutaraldehyde and embedded in Lowicryl K4M as previously reported. Colloidal gold (8nm diameter) was prepared by the method of Mulpfordt.


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