Calcium Phosphate Powder for Cancer Vaccination

Cancer cells synthesize abnormal proteins and peptides which are associated to heat shock proteins being overproduced by these cells due to the stress induced by the particular biology of cancer tissue. We have purified on hydroxylapatite powder heat shock proteins using the HAparticles as purification bed, vectors for the proteins and vaccination adjuvant. The powder make possible that the purified HSPs and their associated peptides are transfected to the antigen presenting cells and presented to the T cells for the destruction of the cancer cells bearing the antigens.

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Heat Shock Proteins, Autoimmunity, and Cancer Treatment

Autoimmune Diseases ◽

10.1155/2012/486069 ◽

2012 ◽

Vol 2012 ◽

pp. 1-10 ◽

Cited By ~ 20

Author(s):

Stuart K. Calderwood ◽

Mary Ann Stevenson ◽

Ayesha Murshid

Keyword(s):

T Cells ◽

Heat Shock ◽

Heat Shock Proteins ◽

Molecular Chaperone ◽

Antigen Processing ◽

Inflammatory Diseases ◽

Antigen Presenting Cells ◽

Processing Pathways ◽

Shock Proteins ◽

Antigen Presenting

Heat shock proteins (HSPs) have been linked to the therapy of both cancer and inflammatory diseases, approaches that utilize contrasting immune properties of these proteins. It would appear that HSP family members Hsp60 and Hsp70, whether from external sources or induced locally during inflammation, can be processed by antigen-presenting cells and that HSP-derived epitopes then activate regulatory T cells and suppress inflammatory diseases. These effects also extend to the HSP-rich environments of cancer cells where elevated HSP concentrations may participate in the immunosuppressive tumor milieu. However, HSPs can also be important mediators of tumor immunity. Due to their molecular chaperone properties, some HSPs can bind tumor-specific peptides and deliver them deep into the antigen-processing pathways of antigen-presenting cells (APCs). In this context, HSP-based vaccines can activate tumor-specific immunity, trigger the proliferation and CTL capabilities of cancer-specific CD8+ T cells, and inhibit tumor growth. Further advances in HSP-based anticancer immunotherapy appear to involve improving the properties of the molecular chaperone vaccines by enhancing their antigen-binding properties and combating the immunosuppressive tumor milieu to permit programming of active CTL capable of penetrating the tumor milieu and specifically targeting tumor cells.

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Polyclonal Responses of γδ T Cells to Heat Shock Proteins

Stress Proteins in Medicine ◽

10.1201/9781003067474-36 ◽

2020 ◽

pp. 557-569

Author(s):

Willi Born ◽

Mary Ann DeGroote ◽

Fu Yang-Xin ◽

Christina Ellis Roark ◽

Kent Heyborne ◽

...

Keyword(s):

T Cells ◽

Heat Shock ◽

Heat Shock Proteins ◽

Γδ T Cells ◽

Shock Proteins

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Hsps responsible for apoptosis induction failure in cervical cancer cells upon osthole and tamoxifen treatment

Postępy Higieny i Medycyny Doświadczalnej ◽

10.5604/01.3001.0013.5447 ◽

2019 ◽

Vol 73 ◽

pp. 563-571

Author(s):

Joanna Jakubowicz-Gil ◽

Roman Paduch ◽

Krystyna Skalicka-Woźniak ◽

Joanna Sumorek-Wiadro ◽

Adrian Zając ◽

...

Keyword(s):

Cervical Cancer ◽

Heat Shock ◽

Heat Shock Proteins ◽

Cancer Cells ◽

Cell Lines ◽

Tamoxifen Treatment ◽

Hpv 16 ◽

Cervical Cancer Cells ◽

Shock Proteins ◽

Human Cervical Cancer

Aim: The aim of the present study was to investigate the efficacy of osthole (7-metoxy-8-isopenthenocoumarin) alone and combined with tamoxifen (TAM) in the elimination of human cervical cancer cells via programmed death. The involvement of heat shock proteins, i.e. well-known molecular chaperones, will be investigated. Material/Methods: Three human cervical cancer cell lines, infected with human papilloma virus (HPV), i.e. HeLa (HPV 18), SiHa (HPV 16), and CaSki (HPV 16 and 18), were used in the experiments. After osthole and TAM treatment, cells stained with fluorochromes were analyzed microscopically according to apoptotic, autophagic, and necrotic morphology. Hsp27, Hsp72, and Hsp90 levels were analyzed by immunoblotting. Transfection with specific siRNA was used for blocking of Hsp expression. Results: In the HeLa, CaSki, and SiHa cell lines, osthole and TAM applied alone had no significant effect on cell death induction. This was correlated with an overexpression of heat shock proteins 27, 72, and 90. In the case of a combination of both drugs, the level of apoptosis was elevated only in SiHa cells. Preincubation with osthole followed by TAM addition as well as simultaneous incubation with both drugs was the most effective. This was correlated with the inhibition of Hsp27, Hsp72, and Hsp90 expression. Blocking of Hsp expression with specific siRNA increased the sensitivity of the studied cell lines to the induction of apoptosis, but not to autophagy or necrosis. Conclusions: Our results indicated that the elimination of heat shock proteins from cervical cancer cells sensitized them to initiation of apoptosis after osthole and tamoxifen treatment.

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