| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
*
University of Rochester Medical Center, Rochester, NY 14642; and
Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, CT 06030
In mammals, the heat shock protein gp96 complexed to antigenic peptides elicits T cell adaptive immunity. By itself, however, gp96 can evoke responses that are characteristic of innate immunity. Interestingly, this protein, which resides in the endoplasmic reticulum, is expressed on the surface of certain mouse tumor cells. Given that heat shock proteins are highly conserved, we investigated whether the cell surface expression of gp96 is also evolutionarily conserved. Our data reveal that gp96, most likely containing the endoplasmic reticulum retention motif (KDEL), is expressed on the surface of three different Xenopus lymphoid tumor cell lines, each derived from a different spontaneously arising thymic tumor. Levels of expression differ among the tumor lines tested, with more immunogenic tumors expressing greater amounts of surface gp96. Moreover, a high level of gp96 surface expression is detectable on a subset of Xenopus normal nontransformed splenic lymphocytes (mainly surface IgM+ B cells) but not on other normal cells, including macrophages and nucleated erythrocytes. Surface expression of a gp96 protein homologue occurs also on some, but not all, T and B cell clones derived from peripheral blood cells of the channel catfish, as well as on lymphocyte-like cells, but not on erythrocytes from the hagfish, a primitive agnathan vertebrate lacking markers of an adaptive immune system. gp96 is actively directed to and retained on the plasma membrane of Xenopus lymphocytes and tumor cells and hagfish lymphocyte-like cells by a process that requires vesicular transport. This selective surface expression of gp96 on some immune cells from different vertebrate classes is consistent with an ancestral immunological role of gp96 as danger-signaling molecule.
This article has been cited by other articles:
|
|
 |
|
  R. M. Srivastava, C. Varalakshmi, and A. Khar The Ischemia-Responsive Protein 94 (Irp94) Activates Dendritic Cells through NK Cell Receptor Protein-2/NK Group 2 Member D (NKR-P2/NKG2D) Leading to Their Maturation J. Immunol., January 15, 2008; 180(2): 1117 - 1130. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Q. Lu, E. O. Harrington, J. Newton, M. Jankowich, and S. Rounds Inhibition of ICMT Induces Endothelial Cell Apoptosis through GRP94 Am. J. Respir. Cell Mol. Biol., July 1, 2007; 37(1): 20 - 30. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. V. Prasadarao, P. K. Srivastava, R. S. Rudrabhatla, K. S. Kim, S.-h. Huang, and S. K. Sukumaran Cloning and Expression of the Escherichia coli K1 Outer Membrane Protein A Receptor, a gp96 Homologue Infect. Immun., April 1, 2003; 71(4): 1680 - 1688. [Abstract] [Full Text]
|
|
|
|
|
|
P. P. Banerjee, D. S. Vinay, A. Mathew, M. Raje, V. Parekh, D. V. R. Prasad, A. Kumar, D. Mitra, and G. C. Mishra Evidence That Glycoprotein 96 (B2), a Stress Protein, Functions as a Th2-Specific Costimulatory Molecule J. Immunol., October 1, 2002; 169(7): 3507 - 3518. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Liu, A. M. DeFilippo, and Z. Li Overcoming Immune Tolerance to Cancer by Heat Shock Protein Vaccines Mol. Cancer Ther., October 1, 2002; 1(12): 1147 - 1151. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. V. Prasadarao Identification of Escherichia coli Outer Membrane Protein A Receptor on Human Brain Microvascular Endothelial Cells Infect. Immun., August 1, 2002; 70(8): 4556 - 4563. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
