› Forums › General Melanoma Community › Is it true that all malignant melanomas contain s-100 protein?
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JerryfromFauq.
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- October 3, 2014 at 2:20 am
I have been told that all malignant melanoma tissue sent for biopsey contain s-100 protein, and that almost all non melanoma tissue does not. Is this true?
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- October 3, 2014 at 4:32 am
Read the following:
http://www.ncbi.nlm.nih.gov/pubmed/7943629
Result Filters
Am J Dermatopathol. 1994 Jun;16(3):233-40.S-100 protein-negative malignant melanoma: fact or fiction? A light-microscopic and immunohistochemical study.
Abstract
S-100 protein is considered a characteristic immunohistochemical marker for all nevomelanocytic lesions, in which it is expected to be present consistently. We reviewed 17 cases of malignant melanomas that previously tested negative for S-100 protein. They were reevaluated by light microscopy, a broad panel of immunohistochemical reagents including monoclonal and polyclonal antibodies to S-100 protein, and electron microscopy. On reexamination, five of the 17 cases were reclassified as non-melanoma tumors, and eight of the 17 cases were found to be positive for S-100 protein (six with monoclonal and eight with polyclonal antibodies) and HMB-45 antigen, consistent with melanoma. The remaining four cases repeatedly tested negative for S-100 protein despite various antigen enhancement methods, but they were positive for HMB-45 antigen and contained premelanosomes or melanosome-like structures by electron microscopy. Two of these repeatedly S-100 negative melanomas were acrally located; although the numbers are small, a possible relationship to a specific anatomic location cannot be excluded. These findings suggest that in a small subset of melanomas S-100 protein is either not fully expressed or is below the level that can be detected by routine immunohistochemistry. We also conclude that in the majority of the initially S-100-negative cases of melanomas, the misdiagnosis may occur due to the use of an incomplete immunohistochemical panel, technical reasons, or the inherent variability of tissue expression of S-100 protein.
AND :
http://www.nordiqc.org/Epitopes/s-100/s-100.htm
S-100 protein (S-100)
Characteristics
S100 is a 21kDa highly acidic and water soluble protein first isolated from brain but later shown to be produced by a wide variety of normal and neoplastic cells of mesodermal, neuroectodermal, and epithelial origin. S-100 protein may be found in the cell membranes, cytoplasm and nuclei. The protein is a dimer, having two subunits, alpha and beta, with extensive sequence homology. There are 3 forms of S-100 protein: alpha-alpha, known as S-100A0; alpha-beta, known as S-100A and beta-beta, known as S-100B. The S-100 alpha gene is assigned to chromosome 1q21. At present, 10 types of alpha chains have been identified. The S100 beta gene is assigned to chromosome 21q22. Only one type of beta chain has been identified. As most cells containing S-100 protein also express the beta chain (marked exceptions being neurones and histiocytes), this has become almost synonymous with the protein.
S100 has varying affinity to calcium and other metals. Its properties are related to many basic cell functions such as cation diffusion across lipid membranes, microtubule assembly, and RNA polymerase activity. In neurones, S100 is involved in the plasma membrane function as well as interaction with chromosomes and synaptosomes.
S100 (beta protein) is present in glial cells, Schwann cells and satellite cells (but not perineurial cells), melanocytes, myoepithelial cells, some glandular epithelia (breast, kidney), skeletal and heart muscle cells, fat cells and chondrocytes, and follicular dendritic cells.
Cerebral overexpression of S100 appears to be neurotoxic and is of pathogenetic importance in Alzheimer disease and Down syndrome (trisomy 21).
Neoplasms
The following neoplasms express S100 in more than 90% of the cases: Astrocytoma, glioblastoma, oligodendroglioma, ependymoma and other glial tumours, schwannoma, neurofibroma, benign and malignant melanocytic tumours, granular cell tumour, myoepithelial tumours, polymorphous low grade adenocarcinoma, Langerhans cell histiocytosis, xanthogranuloma, chordoma, and most types of benign and malignant lipomatous tumours.
The following express the protein in 50-90% of the cases: Primitive neuroectodermal tumours (neuroblastoma and others), malignant peripheral nerve sheath tumour, clear cell sarcoma, rhabdomyosarcoma, benign and malignant chondroid tumours, sweat gland carcinoma, serous and endometrioid cystadenoma and carcinoma, renal cell carcinoma, papillary and follicular thyroid carcinoma, and acute monoblastic/monocytic leukaemia.
S-100 protein is found in 10-50% of the following: Granulosa cell tumour, Sertoli-Leydig cell tumours, alveolar soft part sarcoma, synovial sarcoma, Ewing sarcoma, vascular tumours, gastrointestinal stromal tumour, meningioma, adenocarcinomas of breast and gastrointestinal tract, carcinoids and other neuroendocrine tumours, anaplastic thyroid carcinoma.
The following rarely or never express S100: adenocarcinomas of the alimentary tract, lung, and prostate, transitional cell carcinoma, malignant mesothelioma, fibromatosis, fibrohistiocytic tumours, smooth muscle tumours, malignant lymphomas and germinal cell tumours.
In some tumours, the S-100 protein positivity is restricted to so-called sustentacular cells: phaeochromocytoma/paraganglioma (particularly when benign), and medullary thyroid carcinoma. S-100 positive dendritic cells are particularly numerous in sclerosing variant of papillary carcinoma.
Application
The immunohistochemical evaluation of S-100 (beta) protein expression is important in the diagnosis of undifferentiated malignant tumours of unknown primary origin and should be included in the so-called primary panel.
S100 is a very sensitive marker for malignant melanoma of all types, a negative staining is exceedingly rare. Because of its low specificity, other markers should be included in a panel for malignant melanoma, such as vimentin and Melan-A. S100 may be used in the differential diagnosis of sarcomas (e.g., the distinction between liposarcoma and other myxoid tumours) and spindle cell tumours (e.g., the distinction between schwannoma, leiomyoma and gastrointestinal stromal tumour).
The polyclonal antibody from DakoCytomation is frequently used. The optimal antigen retrieval is not settled. Generally, HIER in an alkaline buffer enhances the staining. However, in some cases a staining is seen after HIER that cannot be revealed with proteolytic demasking, even in a high antibody concentration. The cause of this discrepancy is unknown at present. S100 is difficult to visualize in frozen sections, possibly due to extraction of this small molecule.
For control tissue, an appendix is appropriate.
-
- October 3, 2014 at 4:32 am
Read the following:
http://www.ncbi.nlm.nih.gov/pubmed/7943629
Result Filters
Am J Dermatopathol. 1994 Jun;16(3):233-40.S-100 protein-negative malignant melanoma: fact or fiction? A light-microscopic and immunohistochemical study.
Abstract
S-100 protein is considered a characteristic immunohistochemical marker for all nevomelanocytic lesions, in which it is expected to be present consistently. We reviewed 17 cases of malignant melanomas that previously tested negative for S-100 protein. They were reevaluated by light microscopy, a broad panel of immunohistochemical reagents including monoclonal and polyclonal antibodies to S-100 protein, and electron microscopy. On reexamination, five of the 17 cases were reclassified as non-melanoma tumors, and eight of the 17 cases were found to be positive for S-100 protein (six with monoclonal and eight with polyclonal antibodies) and HMB-45 antigen, consistent with melanoma. The remaining four cases repeatedly tested negative for S-100 protein despite various antigen enhancement methods, but they were positive for HMB-45 antigen and contained premelanosomes or melanosome-like structures by electron microscopy. Two of these repeatedly S-100 negative melanomas were acrally located; although the numbers are small, a possible relationship to a specific anatomic location cannot be excluded. These findings suggest that in a small subset of melanomas S-100 protein is either not fully expressed or is below the level that can be detected by routine immunohistochemistry. We also conclude that in the majority of the initially S-100-negative cases of melanomas, the misdiagnosis may occur due to the use of an incomplete immunohistochemical panel, technical reasons, or the inherent variability of tissue expression of S-100 protein.
AND :
http://www.nordiqc.org/Epitopes/s-100/s-100.htm
S-100 protein (S-100)
Characteristics
S100 is a 21kDa highly acidic and water soluble protein first isolated from brain but later shown to be produced by a wide variety of normal and neoplastic cells of mesodermal, neuroectodermal, and epithelial origin. S-100 protein may be found in the cell membranes, cytoplasm and nuclei. The protein is a dimer, having two subunits, alpha and beta, with extensive sequence homology. There are 3 forms of S-100 protein: alpha-alpha, known as S-100A0; alpha-beta, known as S-100A and beta-beta, known as S-100B. The S-100 alpha gene is assigned to chromosome 1q21. At present, 10 types of alpha chains have been identified. The S100 beta gene is assigned to chromosome 21q22. Only one type of beta chain has been identified. As most cells containing S-100 protein also express the beta chain (marked exceptions being neurones and histiocytes), this has become almost synonymous with the protein.
S100 has varying affinity to calcium and other metals. Its properties are related to many basic cell functions such as cation diffusion across lipid membranes, microtubule assembly, and RNA polymerase activity. In neurones, S100 is involved in the plasma membrane function as well as interaction with chromosomes and synaptosomes.
S100 (beta protein) is present in glial cells, Schwann cells and satellite cells (but not perineurial cells), melanocytes, myoepithelial cells, some glandular epithelia (breast, kidney), skeletal and heart muscle cells, fat cells and chondrocytes, and follicular dendritic cells.
Cerebral overexpression of S100 appears to be neurotoxic and is of pathogenetic importance in Alzheimer disease and Down syndrome (trisomy 21).
Neoplasms
The following neoplasms express S100 in more than 90% of the cases: Astrocytoma, glioblastoma, oligodendroglioma, ependymoma and other glial tumours, schwannoma, neurofibroma, benign and malignant melanocytic tumours, granular cell tumour, myoepithelial tumours, polymorphous low grade adenocarcinoma, Langerhans cell histiocytosis, xanthogranuloma, chordoma, and most types of benign and malignant lipomatous tumours.
The following express the protein in 50-90% of the cases: Primitive neuroectodermal tumours (neuroblastoma and others), malignant peripheral nerve sheath tumour, clear cell sarcoma, rhabdomyosarcoma, benign and malignant chondroid tumours, sweat gland carcinoma, serous and endometrioid cystadenoma and carcinoma, renal cell carcinoma, papillary and follicular thyroid carcinoma, and acute monoblastic/monocytic leukaemia.
S-100 protein is found in 10-50% of the following: Granulosa cell tumour, Sertoli-Leydig cell tumours, alveolar soft part sarcoma, synovial sarcoma, Ewing sarcoma, vascular tumours, gastrointestinal stromal tumour, meningioma, adenocarcinomas of breast and gastrointestinal tract, carcinoids and other neuroendocrine tumours, anaplastic thyroid carcinoma.
The following rarely or never express S100: adenocarcinomas of the alimentary tract, lung, and prostate, transitional cell carcinoma, malignant mesothelioma, fibromatosis, fibrohistiocytic tumours, smooth muscle tumours, malignant lymphomas and germinal cell tumours.
In some tumours, the S-100 protein positivity is restricted to so-called sustentacular cells: phaeochromocytoma/paraganglioma (particularly when benign), and medullary thyroid carcinoma. S-100 positive dendritic cells are particularly numerous in sclerosing variant of papillary carcinoma.
Application
The immunohistochemical evaluation of S-100 (beta) protein expression is important in the diagnosis of undifferentiated malignant tumours of unknown primary origin and should be included in the so-called primary panel.
S100 is a very sensitive marker for malignant melanoma of all types, a negative staining is exceedingly rare. Because of its low specificity, other markers should be included in a panel for malignant melanoma, such as vimentin and Melan-A. S100 may be used in the differential diagnosis of sarcomas (e.g., the distinction between liposarcoma and other myxoid tumours) and spindle cell tumours (e.g., the distinction between schwannoma, leiomyoma and gastrointestinal stromal tumour).
The polyclonal antibody from DakoCytomation is frequently used. The optimal antigen retrieval is not settled. Generally, HIER in an alkaline buffer enhances the staining. However, in some cases a staining is seen after HIER that cannot be revealed with proteolytic demasking, even in a high antibody concentration. The cause of this discrepancy is unknown at present. S100 is difficult to visualize in frozen sections, possibly due to extraction of this small molecule.
For control tissue, an appendix is appropriate.
-
- October 3, 2014 at 4:32 am
Read the following:
http://www.ncbi.nlm.nih.gov/pubmed/7943629
Result Filters
Am J Dermatopathol. 1994 Jun;16(3):233-40.S-100 protein-negative malignant melanoma: fact or fiction? A light-microscopic and immunohistochemical study.
Abstract
S-100 protein is considered a characteristic immunohistochemical marker for all nevomelanocytic lesions, in which it is expected to be present consistently. We reviewed 17 cases of malignant melanomas that previously tested negative for S-100 protein. They were reevaluated by light microscopy, a broad panel of immunohistochemical reagents including monoclonal and polyclonal antibodies to S-100 protein, and electron microscopy. On reexamination, five of the 17 cases were reclassified as non-melanoma tumors, and eight of the 17 cases were found to be positive for S-100 protein (six with monoclonal and eight with polyclonal antibodies) and HMB-45 antigen, consistent with melanoma. The remaining four cases repeatedly tested negative for S-100 protein despite various antigen enhancement methods, but they were positive for HMB-45 antigen and contained premelanosomes or melanosome-like structures by electron microscopy. Two of these repeatedly S-100 negative melanomas were acrally located; although the numbers are small, a possible relationship to a specific anatomic location cannot be excluded. These findings suggest that in a small subset of melanomas S-100 protein is either not fully expressed or is below the level that can be detected by routine immunohistochemistry. We also conclude that in the majority of the initially S-100-negative cases of melanomas, the misdiagnosis may occur due to the use of an incomplete immunohistochemical panel, technical reasons, or the inherent variability of tissue expression of S-100 protein.
AND :
http://www.nordiqc.org/Epitopes/s-100/s-100.htm
S-100 protein (S-100)
Characteristics
S100 is a 21kDa highly acidic and water soluble protein first isolated from brain but later shown to be produced by a wide variety of normal and neoplastic cells of mesodermal, neuroectodermal, and epithelial origin. S-100 protein may be found in the cell membranes, cytoplasm and nuclei. The protein is a dimer, having two subunits, alpha and beta, with extensive sequence homology. There are 3 forms of S-100 protein: alpha-alpha, known as S-100A0; alpha-beta, known as S-100A and beta-beta, known as S-100B. The S-100 alpha gene is assigned to chromosome 1q21. At present, 10 types of alpha chains have been identified. The S100 beta gene is assigned to chromosome 21q22. Only one type of beta chain has been identified. As most cells containing S-100 protein also express the beta chain (marked exceptions being neurones and histiocytes), this has become almost synonymous with the protein.
S100 has varying affinity to calcium and other metals. Its properties are related to many basic cell functions such as cation diffusion across lipid membranes, microtubule assembly, and RNA polymerase activity. In neurones, S100 is involved in the plasma membrane function as well as interaction with chromosomes and synaptosomes.
S100 (beta protein) is present in glial cells, Schwann cells and satellite cells (but not perineurial cells), melanocytes, myoepithelial cells, some glandular epithelia (breast, kidney), skeletal and heart muscle cells, fat cells and chondrocytes, and follicular dendritic cells.
Cerebral overexpression of S100 appears to be neurotoxic and is of pathogenetic importance in Alzheimer disease and Down syndrome (trisomy 21).
Neoplasms
The following neoplasms express S100 in more than 90% of the cases: Astrocytoma, glioblastoma, oligodendroglioma, ependymoma and other glial tumours, schwannoma, neurofibroma, benign and malignant melanocytic tumours, granular cell tumour, myoepithelial tumours, polymorphous low grade adenocarcinoma, Langerhans cell histiocytosis, xanthogranuloma, chordoma, and most types of benign and malignant lipomatous tumours.
The following express the protein in 50-90% of the cases: Primitive neuroectodermal tumours (neuroblastoma and others), malignant peripheral nerve sheath tumour, clear cell sarcoma, rhabdomyosarcoma, benign and malignant chondroid tumours, sweat gland carcinoma, serous and endometrioid cystadenoma and carcinoma, renal cell carcinoma, papillary and follicular thyroid carcinoma, and acute monoblastic/monocytic leukaemia.
S-100 protein is found in 10-50% of the following: Granulosa cell tumour, Sertoli-Leydig cell tumours, alveolar soft part sarcoma, synovial sarcoma, Ewing sarcoma, vascular tumours, gastrointestinal stromal tumour, meningioma, adenocarcinomas of breast and gastrointestinal tract, carcinoids and other neuroendocrine tumours, anaplastic thyroid carcinoma.
The following rarely or never express S100: adenocarcinomas of the alimentary tract, lung, and prostate, transitional cell carcinoma, malignant mesothelioma, fibromatosis, fibrohistiocytic tumours, smooth muscle tumours, malignant lymphomas and germinal cell tumours.
In some tumours, the S-100 protein positivity is restricted to so-called sustentacular cells: phaeochromocytoma/paraganglioma (particularly when benign), and medullary thyroid carcinoma. S-100 positive dendritic cells are particularly numerous in sclerosing variant of papillary carcinoma.
Application
The immunohistochemical evaluation of S-100 (beta) protein expression is important in the diagnosis of undifferentiated malignant tumours of unknown primary origin and should be included in the so-called primary panel.
S100 is a very sensitive marker for malignant melanoma of all types, a negative staining is exceedingly rare. Because of its low specificity, other markers should be included in a panel for malignant melanoma, such as vimentin and Melan-A. S100 may be used in the differential diagnosis of sarcomas (e.g., the distinction between liposarcoma and other myxoid tumours) and spindle cell tumours (e.g., the distinction between schwannoma, leiomyoma and gastrointestinal stromal tumour).
The polyclonal antibody from DakoCytomation is frequently used. The optimal antigen retrieval is not settled. Generally, HIER in an alkaline buffer enhances the staining. However, in some cases a staining is seen after HIER that cannot be revealed with proteolytic demasking, even in a high antibody concentration. The cause of this discrepancy is unknown at present. S100 is difficult to visualize in frozen sections, possibly due to extraction of this small molecule.
For control tissue, an appendix is appropriate.
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