Utilizing a GnRH-based chimeric protein for the detection of adenocarcinoma

Lichtenstein, Michal; Ben‐Yehudah, Ahmi; Belostotsky, Ruth; Eaveri, Ronen; Sabag, Ofra; Grodzovski, Inna; Lorberboum-Galski, Haya

doi:10.3892/ijo.27.1.143

Cited by 3 publications

(4 citation statements)

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“…Human T cell lymphoma HUT102 cells (Deutsche Sammlung von Microorganismen and Zellkulturen, Braunschweig, Germany (DSMZ)), ARH-77 plasma cells (American Type Culture Collection, Manassas, Virginia, USA (ATCC)), mouse L1210 lymphocytic leukaemia cells (ATCC), mouse B16 melanoma cells (kindly provided by O Mendelboum, Hebrew University, Israel), KB31 human cervix carcinoma (ATCC) and LNCaP human prostate adenocarcinoma cells (ATCC) were grown and maintained as described previously 9 – 13…”

Section: Methodsmentioning

confidence: 99%

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Therapeutic potency of IL2-caspase 3 targeted treatment in a murine experimental model of inflammatory bowel disease

Shteingart

Rapoport

Grodzovski

et al. 2008

Gut

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Section: Methodsmentioning

confidence: 99%

“…However, in the last few years we used human pro-apoptotic proteins as the killing moiety. The pro-apoptotic proteins were from the Bcl-2 family (Bax, Bak, Bik)9 – 11 as well as the DNase–DFF4012 and a caspase such as caspase 3 13…”

mentioning

confidence: 99%

Therapeutic potency of IL2-caspase 3 targeted treatment in a murine experimental model of inflammatory bowel disease

Shteingart

Rapoport

Grodzovski

et al. 2008

Gut

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“…The proapoptotic proteins are from the B-cell chronic lymphocytic leukemia/lymphoma 2 (Bcl2) family (Bcl2-associated X protein [Bax], Bcl2 homologous antagonist killer [Bak], and Bcl2-interacting killer [Bik]) [5][6][7][8] as well as the caspaseactivated DNase DNA fragmentation factor, 40 kDa, beta polypeptide (DFF40), 9 and caspases like as Caspase 3. [10][11][12] Caspase 3 is a key protease in apoptosis, acting on multiple substrates within the cell. Its activity is especially significant in lymphoid cells.…”

Section: Introductionmentioning

confidence: 99%

Soluble CD40 ligand (sCD40L) provides a new delivery system for targeted treatment

Kedar¹,

Sabag²,

Licthenstein³

et al. 2012

Cancer

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sCD40L-based chimeric proteins were able to bind and internalize into B cells that expressed the CD40 receptor and specifically and efficiently induced apoptotic death. Moreover, the current results validated for the first time the ability of sCD40L to serve as a direct delivery system for targeted molecules. sCD40L-based chimeric cytotoxic proteins offer a new weapon in the everlasting war against cancer.

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“…In the last few years, we have used human proapoptotic proteins as the killing moiety. These proapoptotic proteins are from the Bcl‐2 family (Bax, Bak, and Bik)3–6 as well as the DNase DFF407 and caspases, such as caspase 3 8…”

Section: Introductionmentioning

confidence: 99%

Eliminating the six N‐terminal amino acids of the caspase 3 large subunit improved production of a biologically active IL2‐Caspase3 chimeric protein

Glantz¹,

Sabag²,

Lichtenstein³

et al. 2012

Biotechnology Progress

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Designing a chimeric protein and developing a procedure for its stable production as a biologically active protein, are key steps in its potential application to clinical trails. IL2-Caspase3 chimeric protein designed to target activated T lymphocytes was found to be a promising molecule for targeted treatment, however was found to be difficult to produce as a biological active molecule. Thus, we designed a new version of the molecule, IL2-Caspase3s, in which six amino acids (aa 29-34) from the N-terminus of the large subunit of caspase 3 were excluded. Repeated expressions, productions, and partial purifications of the IL2-Caspase3s yielded reproducible batches with consistent results. We found that IL2-Caspase3s causes cell death in a specific, dose-, and time-dependent manner. Cell death due to IL2-Caspase3s is caused by apoptosis. This improved and biologically stable IL2-Caspase3s chimeric protein may be developed in the future for clinical trails as a promising therapy for several pathologies involving activated T-cells. Moreover, this truncated caspase 3 sequence, lacking the N-terminal six amino acids of its large subunit, may be used in other caspase 3-based chimeric proteins targeted against various human diseases, using the appropriate targeting moiety.

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Utilizing a GnRH-based chimeric protein for the detection of adenocarcinoma

Cited by 3 publications

References 0 publications

Therapeutic potency of IL2-caspase 3 targeted treatment in a murine experimental model of inflammatory bowel disease

Therapeutic potency of IL2-caspase 3 targeted treatment in a murine experimental model of inflammatory bowel disease

Soluble CD40 ligand (sCD40L) provides a new delivery system for targeted treatment

Eliminating the six N‐terminal amino acids of the caspase 3 large subunit improved production of a biologically active IL2‐Caspase3 chimeric protein

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