Sources/Clones
Only clones of Hsp 27, Hsp 60 and Hsp 70 are listed.
Hsp 27
Biogenex (G3.1), Immunotech (G3.1) and Stress Gen (G3.1)
Hsp 60
Accurate (LK1, LK2), Affinity Bio (4B9/89, 2E1/53), Sanbio (LK1, LK2), Sigma (LK2) and Stress Gen (LK1, LK2, polyclonal).
Hsp 70
Affinity Bio (3a3, 5A5, 4G4, 7.10), Amersham, Biogenex (BRM22), Dako (polyclonal), Diagnostic Biosystems (polyclonal), Pharmingen (5G10), Sigma (BRM11) and Stress Gen (N27F3-4, 1B5, C92F3A-5).
Fixation/Preparation
Some of the antibodies are immunoreactive in fixed paraffin-embedded tissue sections, others are immunoreactive only in cryostat sections and fresh cell preparations. HIER produces enhancement of immunoreactivity.
Background
When prokaryotic or eukaryotic cells are submitted to a transient rise in temperature or to other proteolytic treatments, the synthesis of a set of proteins called heat shock proteins (Hsps) is induced. The structure of these proteins has been highly conserved during evolution. The signal leading to the transcriptional activation of the corresponding genes is the accumulation of denatured and/or aggregated proteins inside the cells after being subjected to stress. The expression of a subset of Hsp is also induced during early embryogenesis and many differentiation processes. Two different functions have been ascribed to Hsps: a molecular chaperone function whereby they mediate the folding, assembly or translocation across the intracellular membranes of other polypeptides, and a role in protein degradation. Some of the essential components of the cytoplasmic ubiquitin-dependent degradative pathway are Hsps (Mayer et al, 1991). These functions of Hsps are essential in every living cell and are required for repairing the damage that results from stress. In addition, the Hsps may also have a number of biological functions apparently distinct from their role during stress, such as in tyrosine kinase and steroid hormone function (Welch 1987; Pratt & Welsh 1994).
Applications
Current interest in Hsps lies in their role as prognostic markers in various tumors and in tumor resistance to chemotherapy, overexpression of Hsps allowing tumor cells to resist stressful situations and agents, including cytotoxic drugs. In endometrial cancers, expression of Hsp 27 has been correlated with the degree of tumor differentiation as well as with the presence of estrogen and progesterone receptors. In patients with cervical cancer, Hsp 27 is predominantly expressed in well-differentiated and moderately differentiated squamous cell carcinomas but the expression of this protein seems to be a negative prognostic factor for gastric cancer (Ciocca et al, 1993b). In the case of malignant fibrous histiocytoma, the expression of Hsp 27 was found to be the strongest prognostic factor, correlating with longer disease-free intervals and overall survival, independent of tumor size, necrosis and histological subtype (Tetu et al, 1992). Different isoforms of Hsp (Tetu et al, 1992). Different isoforms of Hsp 27 have been found in lymphoid tissue of patients with acute lymphoblastic leukemia and the protein has been associated with viral infections.
The presence of Hsp 70 appears to be associated with breast cancers of high histological grades (Lazaris et al, 1997) and it has been suggested that high levels of the protein identify a subset of patients with node-negative breast cancer who show a high risk for disease recurrence (Ciocca et al, 1993a). Increased Hsp 70 expression has also been correlated with low levels of differentiation in colorectal cancer (Lazaris et al, 1995).
Immunostaining for Hsp 27 and Hsp 90 has been studied in a variety of central nervous system tumors (Kato et al, 1992, 1995).
Comments
The Hsps show immunolocalization in the cytoplasm as diffuse or finely granular staining.
References
•Ciocca DR, Clark GM, Tandon AK et al 1993a. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. Journal of the National Cancer Institutes 85: 570-574.
•Ciocca DR, Oesterreich S, Chamness GC et al 1993b. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. Journal of the National Cancer Institutes 85:1558-1570.
•Kato M, Herz F, Kato S, Hirano A 1992. Expression of stress-response (heat-shock) protein 27 in human brain tumors: an immunohistochemical study. Acta Neuropathologica (Berlin) 83: 420-422.
•Kato S, Morita T, Takenaka T et al 1995. Stress-response (heat-shock) protein 90 expression in tumors of the central nervous system: an immunohistochemical study. Acta Neuropathologica (Berlin) 89: 184-188.
•Lazaris AC, Theodoropoulos GE, Davaris PS et al 1995. Heat shock protein 70 and HLA-DR molecules tissue expression. Prognostic implications in colorectal carcinoma. Diseases of Colon and Rectum 38:739-745.
•Lazaris AC, Chatzigianni EB, Panoussopoulos D et al 1997. Proliferating cell nuclear antigen and heat shock protein 70 immunolocalization in invasive ductal breast cancer not otherwise specified. Breast Cancer Research and Treatment 43:43-51.
•Mayer RJ, Lowe J, Landon M et al 1991. Ubiquitin and the lysosome system: molecular immunopathology reveals the connection. Biomedicine Biochemia Acta 50:333-341.
•Pratt WB, Welsh MJ 1994. Chaperone functions of the heat shock proteins associated with steroid receptors. Seminars in Cell Biology 5:83-93.
•Tetu B, Lacasse B, Bouchard HL et al 1992. Prognostic influence of HSP-27 expression in malignant fibrous histiocytoma: a clinicopathological and immunohistochemical study. Cancer Research 52:2325-2328.
•Welch WJ 1987. The mammalian heat shock (or stress) response: a cellular defense mechanism. Advances in Experimental Medicine and Biology 225:287-304.
Bibliografía
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
Only clones of Hsp 27, Hsp 60 and Hsp 70 are listed.
Hsp 27
Biogenex (G3.1), Immunotech (G3.1) and Stress Gen (G3.1)
Hsp 60
Accurate (LK1, LK2), Affinity Bio (4B9/89, 2E1/53), Sanbio (LK1, LK2), Sigma (LK2) and Stress Gen (LK1, LK2, polyclonal).
Hsp 70
Affinity Bio (3a3, 5A5, 4G4, 7.10), Amersham, Biogenex (BRM22), Dako (polyclonal), Diagnostic Biosystems (polyclonal), Pharmingen (5G10), Sigma (BRM11) and Stress Gen (N27F3-4, 1B5, C92F3A-5).
Fixation/Preparation
Some of the antibodies are immunoreactive in fixed paraffin-embedded tissue sections, others are immunoreactive only in cryostat sections and fresh cell preparations. HIER produces enhancement of immunoreactivity.
Background
When prokaryotic or eukaryotic cells are submitted to a transient rise in temperature or to other proteolytic treatments, the synthesis of a set of proteins called heat shock proteins (Hsps) is induced. The structure of these proteins has been highly conserved during evolution. The signal leading to the transcriptional activation of the corresponding genes is the accumulation of denatured and/or aggregated proteins inside the cells after being subjected to stress. The expression of a subset of Hsp is also induced during early embryogenesis and many differentiation processes. Two different functions have been ascribed to Hsps: a molecular chaperone function whereby they mediate the folding, assembly or translocation across the intracellular membranes of other polypeptides, and a role in protein degradation. Some of the essential components of the cytoplasmic ubiquitin-dependent degradative pathway are Hsps (Mayer et al, 1991). These functions of Hsps are essential in every living cell and are required for repairing the damage that results from stress. In addition, the Hsps may also have a number of biological functions apparently distinct from their role during stress, such as in tyrosine kinase and steroid hormone function (Welch 1987; Pratt & Welsh 1994).
Applications
Current interest in Hsps lies in their role as prognostic markers in various tumors and in tumor resistance to chemotherapy, overexpression of Hsps allowing tumor cells to resist stressful situations and agents, including cytotoxic drugs. In endometrial cancers, expression of Hsp 27 has been correlated with the degree of tumor differentiation as well as with the presence of estrogen and progesterone receptors. In patients with cervical cancer, Hsp 27 is predominantly expressed in well-differentiated and moderately differentiated squamous cell carcinomas but the expression of this protein seems to be a negative prognostic factor for gastric cancer (Ciocca et al, 1993b). In the case of malignant fibrous histiocytoma, the expression of Hsp 27 was found to be the strongest prognostic factor, correlating with longer disease-free intervals and overall survival, independent of tumor size, necrosis and histological subtype (Tetu et al, 1992). Different isoforms of Hsp (Tetu et al, 1992). Different isoforms of Hsp 27 have been found in lymphoid tissue of patients with acute lymphoblastic leukemia and the protein has been associated with viral infections.
The presence of Hsp 70 appears to be associated with breast cancers of high histological grades (Lazaris et al, 1997) and it has been suggested that high levels of the protein identify a subset of patients with node-negative breast cancer who show a high risk for disease recurrence (Ciocca et al, 1993a). Increased Hsp 70 expression has also been correlated with low levels of differentiation in colorectal cancer (Lazaris et al, 1995).
Immunostaining for Hsp 27 and Hsp 90 has been studied in a variety of central nervous system tumors (Kato et al, 1992, 1995).
Comments
The Hsps show immunolocalization in the cytoplasm as diffuse or finely granular staining.
References
•Ciocca DR, Clark GM, Tandon AK et al 1993a. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. Journal of the National Cancer Institutes 85: 570-574.
•Ciocca DR, Oesterreich S, Chamness GC et al 1993b. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. Journal of the National Cancer Institutes 85:1558-1570.
•Kato M, Herz F, Kato S, Hirano A 1992. Expression of stress-response (heat-shock) protein 27 in human brain tumors: an immunohistochemical study. Acta Neuropathologica (Berlin) 83: 420-422.
•Kato S, Morita T, Takenaka T et al 1995. Stress-response (heat-shock) protein 90 expression in tumors of the central nervous system: an immunohistochemical study. Acta Neuropathologica (Berlin) 89: 184-188.
•Lazaris AC, Theodoropoulos GE, Davaris PS et al 1995. Heat shock protein 70 and HLA-DR molecules tissue expression. Prognostic implications in colorectal carcinoma. Diseases of Colon and Rectum 38:739-745.
•Lazaris AC, Chatzigianni EB, Panoussopoulos D et al 1997. Proliferating cell nuclear antigen and heat shock protein 70 immunolocalization in invasive ductal breast cancer not otherwise specified. Breast Cancer Research and Treatment 43:43-51.
•Mayer RJ, Lowe J, Landon M et al 1991. Ubiquitin and the lysosome system: molecular immunopathology reveals the connection. Biomedicine Biochemia Acta 50:333-341.
•Pratt WB, Welsh MJ 1994. Chaperone functions of the heat shock proteins associated with steroid receptors. Seminars in Cell Biology 5:83-93.
•Tetu B, Lacasse B, Bouchard HL et al 1992. Prognostic influence of HSP-27 expression in malignant fibrous histiocytoma: a clinicopathological and immunohistochemical study. Cancer Research 52:2325-2328.
•Welch WJ 1987. The mammalian heat shock (or stress) response: a cellular defense mechanism. Advances in Experimental Medicine and Biology 225:287-304.
Bibliografía
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
