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Gene Review

PSMA1  -  proteasome (prosome, macropain) subunit,...

Homo sapiens

Synonyms: 30 kDa prosomal protein, HC2, HEL-S-275, MGC14542, MGC14575, ...
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Disease relevance of PSMA1

  • Our animal study showed that the expression of H2Kd/scPSMA in B16F0/PSMA5, a B16F0 cell line expressing human PSMA, significantly inhibited tumor growth as demonstrated in the pulmonary metastasis assay and tumor growth study and improved overall survival [1].
  • PSMA is a cell-surface glycoprotein expressed on prostate cancer cells and the neovascular endothelium of multiple carcinomas [2].
  • The aptamer portion of the chimeras mediates binding to PSMA, a cell-surface receptor overexpressed in prostate cancer cells and tumor vascular endothelium, whereas the siRNA portion targets the expression of survival genes [3].
  • These Dtxl-encapsulated nanoparticle-aptamer bioconjugates (Dtxl-NP-Apt) bind to the PSMA protein expressed on the surface of LNCaP prostate epithelial cells and get taken up by these cells resulting in significantly enhanced in vitro cellular toxicity as compared with nontargeted nanoparticles that lack the PSMA aptamer (Dtxl-NP) (P < 0.0004) [4].
  • The anti-PSMA mAbs reacted with the neoplastic cells of prostatic adenocarcinoma (12 of 12 cases) but not with the neoplastic cells of any other tumor type, including those of benign and malignant vascular tumors (0 of 3 hemangiomas, 0 of 1 hemangioendothelioma, and 0 of 1 angiosarcoma) [5].

Psychiatry related information on PSMA1


High impact information on PSMA1

  • When applied to cells expressing PSMA, these RNAs are internalized and processed by Dicer, resulting in depletion of the siRNA target proteins and cell death [3].
  • When stimulated by cell-surface PSMA, retrovirally transduced lymphocytes undergo robust proliferation, expanding by more than 2 logs in three weeks, and produce large amounts of interleukin-2 (IL-2) [7].
  • Prostate-specific membrane antigen (PSMA) is a type 2 integral membrane glycoprotein that serves as an attractive target for cancer immunotherapy by virtue of its abundant and restricted expression on the surface of prostate carcinomas and the neovasculature of most other solid tumors [8].
  • A truncated PSMA protein, lacking transmembrane and cytoplasmic domains, also formed homodimers, indicating that the extracellular domain is sufficient for dimerization [8].
  • We show that PSMA inhibition, knockdown, or deficiency decreases endothelial cell invasion in vitro via integrin and PAK, thus abrogating angiogenesis [9].

Chemical compound and disease context of PSMA1


Biological context of PSMA1

  • The genes Hs PROS-27 and Hs PROS-30 were mapped to chromosomes 14 (14q13) and 11 (11p15.1), respectively [15].
  • Psc2 expression in vivo during embryogenesis and in the adult mouse demonstrated tight spatial and temporal regulation, with the highest levels of expression in the epithelial lining of distal convoluted tubules in embryonic and adult kidneys [16].
  • The Psc2 cDNA contained an open reading frame homologous to CP2 family proteins [16].
  • PSES is a chimeric enhancer containing enhancer elements from prostate-specific antigen (PSA) and prostate-specific membrane antigen (PSMA) genes that are prevalently expressed in androgen-independent prostate cancers [10].
  • Aptamer:toxin conjugates have an IC50 of 27 nmol/L and display an increased potency of at least 600-fold relative to cells that do not express PSMA [17].

Anatomical context of PSMA1

  • Functional analysis demonstrated that PSC2 repressed transcription 2.5-15-fold when bound to a heterologous promoter in ES, 293T, and COS-1 cells [16].
  • Having established a culture system using fibroblasts that express PSMA, we next show that T cells expressing the Pz-1 receptor release cytokines in response to cell-bound PSMA [2].
  • Here we show that angiogenesis is severely impaired in PSMA-null animals and that this angiogenic defect occurs at the level of endothelial cell invasion through the extracellular matrix barrier [9].
  • PSMA is highly expressed in prostate secretory-acinar epithelium and prostate cancer as well as in several extraprostatic tissues [5].
  • A subset of skeletal muscle cells was positive with 7E11 (7 of 7 cases) and negative with the other four anti-PSMA mAbs [5].

Associations of PSMA1 with chemical compounds

  • ITI is a glycoprotein composed of three polypeptides: two heavy chains (HC1 and HC2) and one light chain (bikunin) [18].
  • The coupling to HC2 has an isotropic component smaller than usual, evidently an indication that the bonds to C2 are nonplanar [19].
  • Recent studies have shown that HC1 and HC2 are linked in vivo and in vitro to hyaluronic acid [18].
  • R2 was the product of net hydrogen loss from N7, equivalent to the one-electron oxidation product of neutral hypoxanthine, and exhibited alpha-proton hyperfine couplings to HC2 and HC8 [19].
  • Cells on the chitosan scaffolds incorporated with hydroxyapatite powders (HC2) exhibited lower ALP activity during the 11-day culture period and OC secretion during the first 7 days, in comparison with that on HC1 [20].

Other interactions of PSMA1

  • Sequence comparisons show that the Hs PROS-27 and Hs PROS-30 genes belong to the gene family that encodes the prosome--MCP (multicatalytic proteinase)--proteasome proteins [15].
  • These results, as confirmed by the polymerase chain reaction, establish the existence of two distinct Hs PROS-30 mRNAs, differing in their 5'-noncoding regions and in the N-terminal six aa of their protein products [21].
  • HC3 was less likely than HC2 to test positive for untargeted PCR-detected single infections with HPV53 (P = 0.001) and HPV66 (P = 0.01) [22].
  • R2, which also decayed on warming to 50 K, exhibited nearly equal couplings to HC2 and HC8 [23].

Analytical, diagnostic and therapeutic context of PSMA1

  • HC3 was less likely than HC2 to test positive for specimens that tested positive by PCR for any untargeted types (P < 0.001) [22].
  • In Hep G2 cells in culture, a quantification of mRNAs based on the in situ hybridization technique shows that their relative quantities, in decreasing order, are those of L, HC2, HC3 and HC1 [24].
  • These findings on PSMA structure and biology may have important implications for active and passive immunotherapy of prostate and other cancers [8].
  • An innovative protein biochip immunoassay was used to quantitate and compare serum PSMA levels in healthy men and patients with either benign or malignant prostate disease [25].
  • Localization of the anti-PSMA mAbs to tumor-associated neovasculature was confirmed by CD34 immunohistochemistry in sequential tissue sections [5].


  1. Targeting foreign major histocompatibility complex molecules to tumors by tumor cell specific single chain antibody (scFv). Li, J., Franek, K.J., Patterson, A.L., Holmes, L.M., Burgin, K.E., Ji, J., Yu, X., Wagner, T.E., Wei, Y. Int. J. Oncol. (2003) [Pubmed]
  2. Cancer patient T cells genetically targeted to prostate-specific membrane antigen specifically lyse prostate cancer cells and release cytokines in response to prostate-specific membrane antigen. Gong, M.C., Latouche, J.B., Krause, A., Heston, W.D., Bander, N.H., Sadelain, M. Neoplasia (1999) [Pubmed]
  3. Cell type-specific delivery of siRNAs with aptamer-siRNA chimeras. McNamara, J.O., Andrechek, E.R., Wang, Y., Viles, K.D., Rempel, R.E., Gilboa, E., Sullenger, B.A., Giangrande, P.H. Nat. Biotechnol. (2006) [Pubmed]
  4. Targeted nanoparticle-aptamer bioconjugates for cancer chemotherapy in vivo. Farokhzad, O.C., Cheng, J., Teply, B.A., Sherifi, I., Jon, S., Kantoff, P.W., Richie, J.P., Langer, R. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. Five different anti-prostate-specific membrane antigen (PSMA) antibodies confirm PSMA expression in tumor-associated neovasculature. Chang, S.S., Reuter, V.E., Heston, W.D., Bander, N.H., Grauer, L.S., Gaudin, P.B. Cancer Res. (1999) [Pubmed]
  6. Influence of radioimmunoscintigraphy on postprostatectomy radiotherapy treatment decision making. Jani, A.B., Blend, M.J., Hamilton, R., Brendler, C., Pelizzari, C., Krauz, L., Vijayakumar, S., Sapra, B., Awan, A., Weichselbaum, R.R. J. Nucl. Med. (2004) [Pubmed]
  7. Human T-lymphocyte cytotoxicity and proliferation directed by a single chimeric TCRzeta /CD28 receptor. Maher, J., Brentjens, R.J., Gunset, G., Rivière, I., Sadelain, M. Nat. Biotechnol. (2002) [Pubmed]
  8. The homodimer of prostate-specific membrane antigen is a functional target for cancer therapy. Schülke, N., Varlamova, O.A., Donovan, G.P., Ma, D., Gardner, J.P., Morrissey, D.M., Arrigale, R.R., Zhan, C., Chodera, A.J., Surowitz, K.G., Maddon, P.J., Heston, W.D., Olson, W.C. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  9. Prostate-specific membrane antigen regulates angiogenesis by modulating integrin signal transduction. Conway, R.E., Petrovic, N., Li, Z., Heston, W., Wu, D., Shapiro, L.H. Mol. Cell. Biol. (2006) [Pubmed]
  10. Gene therapy for prostate cancer by controlling adenovirus E1a and E4 gene expression with PSES enhancer. Li, X., Zhang, Y.P., Kim, H.S., Bae, K.H., Stantz, K.M., Lee, S.J., Jung, C., Jiménez, J.A., Gardner, T.A., Jeng, M.H., Kao, C. Cancer Res. (2005) [Pubmed]
  11. Successful in vivo tumor targeting of prostate-specific membrane antigen with a highly efficient J591/PEI/DNA molecular conjugate. Moffatt, S., Papasakelariou, C., Wiehle, S., Cristiano, R. Gene Ther. (2006) [Pubmed]
  12. Prostate specific membrane antigen (PSMA) expression gives prostate cancer cells a growth advantage in a physiologically relevant folate environment in vitro. Yao, V., Bacich, D.J. Prostate (2006) [Pubmed]
  13. Comparison of the CMV brite turbo assay and the digene hybrid capture CMV DNA (Version 2.0) assay for quantitation of cytomegalovirus in renal transplant recipients. Ho, S.K., Li, F.K., Lai, K.N., Chan, T.M. J. Clin. Microbiol. (2000) [Pubmed]
  14. Prostate-specific suicide gene therapy using the prostate-specific membrane antigen promoter and enhancer. O'Keefe, D.S., Uchida, A., Bacich, D.J., Watt, F.B., Martorana, A., Molloy, P.L., Heston, W.D. Prostate (2000) [Pubmed]
  15. The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family. Bey, F., Silva Pereira, I., Coux, O., Viegas-Péquignot, E., Recillas Targa, F., Nothwang, H.G., Dutrillaux, B., Scherrer, K. Mol. Gen. Genet. (1993) [Pubmed]
  16. CRTR-1, a developmentally regulated transcriptional repressor related to the CP2 family of transcription factors. Rodda, S., Sharma, S., Scherer, M., Chapman, G., Rathjen, P. J. Biol. Chem. (2001) [Pubmed]
  17. Aptamer:toxin conjugates that specifically target prostate tumor cells. Chu, T.C., Marks, J.W., Lavery, L.A., Faulkner, S., Rosenblum, M.G., Ellington, A.D., Levy, M. Cancer Res. (2006) [Pubmed]
  18. Inter-alpha-trypsin inhibitor proteoglycan family--a group of proteins binding and stabilizing the extracellular matrix. Bost, F., Diarra-Mehrpour, M., Martin, J.P. Eur. J. Biochem. (1998) [Pubmed]
  19. EPR and ENDOR study of radiation-induced radical formation in purines: hypoxanthine hydrochloride monohydrate crystals X-irradiated at 10 K. Tokdemir, S., Nelson, W.H. The journal of physical chemistry. A, Molecules, spectroscopy, kinetics, environment & general theory. (2005) [Pubmed]
  20. Calcium phosphate-chitosan composite scaffolds for bone tissue engineering. Zhang, Y., Ni, M., Zhang, M., Ratner, B. Tissue engineering. (2003) [Pubmed]
  21. Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes. Silva Pereira, I., Bey, F., Coux, O., Scherrer, K. Gene (1992) [Pubmed]
  22. Comparison between prototype hybrid capture 3 and hybrid capture 2 human papillomavirus DNA assays for detection of high-grade cervical intraepithelial neoplasia and cancer. Castle, P.E., Lorincz, A.T., Scott, D.R., Sherman, M.E., Glass, A.G., Rush, B.B., Wacholder, S., Burk, R.D., Manos, M.M., Schussler, J.E., Macomber, P., Schiffman, M. J. Clin. Microbiol. (2003) [Pubmed]
  23. EPR and ENDOR study of radiation-induced radical formation in purines: sodium inosine crystals X-irradiated at 10 K. Tokdemir, S., Nelson, W.H. The journal of physical chemistry. A, Molecules, spectroscopy, kinetics, environment & general theory. (2006) [Pubmed]
  24. Light microscopical detection of inter-alpha-trypsin inhibitor and its different mRNAs in cultured hepatoma Hep G2 cells using immunocytochemical and in situ hybridization techniques. Borghi, H., Callé, A., Sesboüé, R., Bourguignon, J., Diarra-Mehrpour, M., Martin, J.P. Histochem. J. (1994) [Pubmed]
  25. Quantitation of serum prostate-specific membrane antigen by a novel protein biochip immunoassay discriminates benign from malignant prostate disease. Xiao, Z., Adam, B.L., Cazares, L.H., Clements, M.A., Davis, J.W., Schellhammer, P.F., Dalmasso, E.A., Wright, G.L. Cancer Res. (2001) [Pubmed]
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