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Gene Review

Gzme  -  granzyme E

Mus musculus

Synonyms: CCP3, CTL serine protease 2, Ccp3, Ctla-6, Ctla6, ...
 
 
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Disease relevance of Gzme

  • Each was positive with greater than 47% of the gliomas tested (C12, 9 of 17; D12, 8 of 17); and with 1 of 3 medulloblastomas, 1 of 2 melanomas, and cell lines derived from 12- and 16-week-gestation human fetal brain [1].
  • Whether isolated from day 9 (D9) or day 12 (D12) TDLN, 5 million L-selectin(low) T(E) could be culture activated and adoptively transferred to achieve complete rejection of established intradermal, pulmonary, and brain tumors [2].
  • Analysis of toxinogenic functions associated with the RTX repeat region and monoclonal antibody D12 epitope of Escherichia coli hemolysin [3].
 

High impact information on Gzme

  • The putative mature proteins of MCSP-2 and MCSP-3 are each composed of 228 amino acids with molecular weights of 25,477 and 25,360, respectively [4].
  • Three new cDNA clones (designated MCSP-1, MCSP-2, and MCSP-3) encoding mouse serine proteases were isolated from cloned cytolytic T lymphocytes (CTL) by a modified differential screening procedure [4].
  • Two Mabs, C12 and D12, which localized specifically to tumors in athymic mouse-human glioma xenograft paired label localization assays, are IgG3 antibodies; both bind readily to staphylococcal protein A in column purification and radioimmunoprecipitation procedures [1].
  • Following immunoprecipitation of [3H]leucine labeled cell membrane preparations, Mabs C12 and D12 have consistently yielded unique bands in the Mr 180,000 and Mr 88,000 regions respectively [1].
  • Notable extraneuroectodermal reactivity included that of Mab D12 for splenic trabeculae and the spermatids and Sertoli cells in the testes [1].
 

Biological context of Gzme

  • Fgf9 maps to chromosome 14 near the Ctla6 locus [5].
  • However, suppression of D12 expression caused rapid appearance of lipofuscin granules, accompanied by apoptotic cell death without the apparent activation of the unfolded protein response [6].
  • B6 and D12 have additional reactivities with some immunoglobulins (Ig) encoded by the V3-11 and V3-7 genes; D12 also reacts with some V3-43 gene Ig [7].
 

Anatomical context of Gzme

  • Hence, we suggest that D12 participates in the degradative function of lysosomes [6].
  • The CRI-negative B cell population yielded 54 cell lines, of which 20% secreted SPA-reactive Ig, as might be anticipated because a majority of VHIII Ig+ B cells will be CRI-. SAC stimulation of CRI+ and CRI- populations showed preferential stimulation of the D12 population [8].
  • Although the majority of D12 is located in the endoplasmic reticulum and endoplasmic reticulum-Golgi intermediate compartments at steady state, overexpression or knockdown of D12 had no obvious effects on membrane trafficking in the early secretory pathway [6].
  • The typical cause of lipofuscin formation is the impaired degradation of mitochondria by lysosomal degradative enzymes, and, consistent with this, we found that proper post-Golgi maturation of cathepsin D was impaired in D12-deficient cells [6].
  • Cells present in the medial region of the mouse symphysis in cycling and at D12 displayed ultrastructural features characteristic of a typical fibroblast [9].
 

Associations of Gzme with chemical compounds

  • NH2-terminal amino acids of MCSP-2- and MCSP-3-predicted proteins were identical to those reported for granzyme E and F, respectively [4].
  • The ratio of chondroitin sulfate/dry weight of symphysis showed two phases of increase: between D12 and D 15, and between D 17 and D 18 [10].
 

Analytical, diagnostic and therapeutic context of Gzme

  • This highly reproducible treatment failure was due to cotransfer of tumor-induced, L-selectin(high) suppressor T cells (T(S)) which were also present in D12 TDLN [2].

References

  1. Production and characterization of two human glioma xenograft-localizing monoclonal antibodies. Wikstrand, C.J., McLendon, R.E., Bullard, D.E., Fredman, P., Svennerholm, L., Bigner, D.D. Cancer Res. (1986) [Pubmed]
  2. Tumor-induced L-selectinhigh suppressor T cells mediate potent effector T cell blockade and cause failure of otherwise curative adoptive immunotherapy. Peng, L., Kjaergäard, J., Plautz, G.E., Awad, M., Drazba, J.A., Shu, S., Cohen, P.A. J. Immunol. (2002) [Pubmed]
  3. Analysis of toxinogenic functions associated with the RTX repeat region and monoclonal antibody D12 epitope of Escherichia coli hemolysin. Rowe, G.E., Pellett, S., Welch, R.A. Infect. Immun. (1994) [Pubmed]
  4. Isolation and sequence analysis of serine protease cDNAs from mouse cytolytic T lymphocytes. Kwon, B.S., Kestler, D., Lee, E., Wakulchik, M., Young, J.D. J. Exp. Med. (1988) [Pubmed]
  5. Genomic organization and embryonic expression of the mouse fibroblast growth factor 9 gene. Colvin, J.S., Feldman, B., Nadeau, J.H., Goldfarb, M., Ornitz, D.M. Dev. Dyn. (1999) [Pubmed]
  6. Involvement of a novel Q-SNARE, D12, in quality control of the endomembrane system. Okumura, A.J., Hatsuzawa, K., Tamura, T., Nagaya, H., Saeki, K., Okumura, F., Nagao, K., Nishikawa, M., Yoshimura, A., Wada, I. J. Biol. Chem. (2006) [Pubmed]
  7. Molecular analysis of human immunoglobulin heavy chain variable region associated determinants recognized by anti-VH3 antibodies 7B4, B6 and D12. Suleyman, S., Thompson, K.M., Mageed, R.A., Natvig, J.B. Scand. J. Immunol. (2000) [Pubmed]
  8. Expression of VHIII-associated cross-reactive idiotype on human B lymphocytes. Association with staphylococcal protein A binding and Staphylococcus aureus Cowan I stimulation. Shokri, F., Mageed, R.A., Maziak, B.R., Jefferis, R. J. Immunol. (1991) [Pubmed]
  9. Phenotypic modulation of fibroblastic cells in mice pubic symphysis during pregnancy, partum and postpartum. Moraes, S.G., Campos Pinheiro, M., Toledo, O.M., Joazeiro, P.P. Cell Tissue Res. (2004) [Pubmed]
  10. Ultrastructural, immunohistochemical and biochemical analysis of glycosaminoglycans and proteoglycans in the mouse pubic symphysis during pregnancy. Pinheiro, M.C., Mora, O.A., Caldini, E.G., Battlehner, C.N., Joazeiro, P.P., Toledo, O.M. Cell Biol. Int. (2005) [Pubmed]
 
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