Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “sarcoma”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources
PubMed1999

Expression of neural cell adhesion molecules and neurofilament protein isoforms in Ewing's sarcoma of bone and soft tissue sarcomas other than rhabdomyosarcoma.

In a previous study, it was shown that rhabdomyosarcomas widely express "neural" markers, such as neural cell adhesion molecules (N-CAM) and neurofilament protein isoforms. In the current study, a series of Ewing's sarcomas of bone and soft tissue sarcomas other than rhabdomyosarcoma was probed for the same antigens. It was found that N-CAM was widely expressed in the various sarcoma types, except Ewing's sarcomas, though less than in rhabdomyosarcomas. Similar to rhabdomyosarcomas, neurofilament isoforms were found throughout all sarcoma types but were largely restricted to those expressed early in neurogenesis, that is, poorly phosphorylated medium-weight isoforms. Neurofilament expression was most extensive in Ewing's sarcomas. It was concluded that the expression of "neural" markers (N-CAM, neurofilaments) is widespread in sarcomas and does not signify a neural tumor. The absence of N-CAM expression in Ewing's sarcoma may be helpful in its distinction from other sarcomas.

Adolescent↗
PubMed2003

Latent and lytic HHV-8 mRNA expression in PBMCs and Kaposi's sarcoma skin biopsies of AIDS Kaposi's sarcoma patients.

Human herpes virus 8 (HHV-8) is associated with all clinical forms of Kaposi's sarcoma. HHV-8 DNA is present in Kaposi's sarcoma biopsies and is observed regularly in saliva and less consistently in blood of Kaposi's sarcoma patients. The expression pattern of latent (ORF 73) and lytic (vGCR, vBcl-2, and vIL-6) HHV-8 mRNA was studied in peripheral blood mononuclear cell (PBMC) samples and Kaposi's sarcoma skin biopsies from 11 AIDS Kaposi's sarcoma patients with four different nucleic acid sequence-based amplification (NASBA) assays. Patients were divided into groups according to the clinical stage of Kaposi's sarcoma (stage I-IV). All biopsies were positive for two or more of the mRNA measured. No clear difference could be seen in the expression pattern in the lesions of the different clinical stages. In the corresponding PBMC samples, very little or no mRNA was measurable in the patients with Kaposi's sarcoma stage I or II, whereas patients with more advanced Kaposi's sarcoma (stage III or IV) had more detectable mRNA in the PBMCs. Thus, the HHV-8 DNA load in the PBMCs increases in more advanced Kaposi's sarcoma, as does the frequency of mRNA detection in PBMCs.

AIDS-Related Opportunistic Infections↗
PubMedDate not supplied

[Cooperative Ewing's Sarcoma Studies 81/86: pathologico-anatomic and immunohistochemical findings and differential diagnosis of Ewing sarcoma].

158 cases of the Cooperative Ewing's Sarcoma Trials (CESS 81/86), which have been documented at the Pediatric Tumor Registry, Kiel, were studied by conventional light microscopy and immunohistochemistry. There were 77 cases of typical Ewing's sarcoma with 70 cases being located in the skeleton and 7 in soft tissues. Of the 14 cases of atypical Ewing's sarcoma 7 cases each were localized in bone and in soft tissue, respectively. In contrast to typical Ewing's sarcoma, cells of atypical Ewing's sarcoma were larger and displayed more heterochromatin. Both, typical and atypical Ewing's sarcoma reacted positively for vimentin. Other stains were negative, notably the neuron specific enolase (NSE). In 55 cases a diagnosis of malignant peripheral neuroectodermal tumor (MPNT) was made. Histologically most of these tumors resembled atypical Ewing's sarcoma. By immunohistochemistry positive reactions were found for NSE, vimentin, protein S-100, neurofilaments and glial fibrillary acidic protein. In 3 cases a diagnosis of small cell osteosarcoma was made. There were 2 cases of undifferentiated sarcoma of bone, 2 cases of soft tissue sarcoma of undetermined histogenesis and 2 cases of rhabdomyosarcoma. Of the 4 tumors which could be investigated for response to polychemotherapy, 1 each corresponded to grade II and III, respectively, and 2 to grade IV according to the classification of histologic grade of regression established by Salzer-Kuntschik et al. (1983).

Adolescent↗
PubMed1998

Immunohistochemical analysis of Fas ligand expression in sarcomas. Sarcomas express high level of FasL in vivo.

Fas ligand (FasL) and its receptor, Fas, play a key role in the regulation of apoptosis within the immune system. Several prior experimental studies of Fas ligand expression in tumors have suggested a mechanism that enables tumors to evade immune destruction by inducing apoptosis in activated lymphocytes near the tumor cells. Many types of carcinomas have been shown to express FasL, but at present nothing is known about the range of sarcomas capable of expressing FasL in vivo. The aim of this study was to determine the in vivo patterns of FasL expression in human sarcomas. Archival paraffin-embedded tissues of 57 sarcomas and 30 carcinomas were analyzed by immunohistochemistry for the expression of FasL. FasL immunoreactivity was seen in 39 of 57 (68%) sarcomas, including 10 of 10 rhabdomyosarcomas, 5 of 5 malignant schwannomas, 2 of 2 Ewing's sarcomas, 8 of 11 malignant fibrous histiocytomas, 4 of 5 angiosarcomas, 2 of 5 synovial sarcomas, 2 of 5 liposarcomas, 3 of 5 leiomyosarcomas, 2 of 6 osteosarcomas, and 1 of 3 chondrosarcomas. All carcinomas tested (10 gastric adenocarcinomas, 10 hepatocellular carcinomas, and 10 renal cell carcinomas) were positive for FasL. These results demonstrate that FasL expression in sarcomas, although less frequent than in carcinomas, is widespread among the sarcoma types, and suggest that FasL might contribute to the immune escape of sarcomas through killing Fas-bearing lymphocytes.

Apoptosis↗
PubMed1999

H-ras and K-ras mutations in soft tissue sarcoma: comparative studies of sarcomas from Korean and American patients.

BACKGROUND: The authors' recent investigation of Korean patients with sarcoma has suggested that ras gene activation may play a role in oncogenesis. The authors attempted to extend the mutation analysis to sarcomas in American patients to determine whether there were racial or geographic factors relevant to the initiation or progression of sarcoma. METHODS: H-ras and K-ras genes were examined in sarcomas obtained from patients in the midwestern U. S. using the polymerase chain reaction technique and direct automated sequencing analysis. Tumors studied included 29 malignant fibrous histiocytomas, 7 liposarcomas, 5 rhabdomyosarcomas, and 9 leiomyosarcomas. RESULTS: Of the 50 sarcomas evaluated, only 1 (2%) definable mutation was found; a GGC to AGC transition at codon 12 of H-ras was found in a rhabdomyosarcoma. None of the patients had a K-ras mutation. The rates of incidence of ras point mutations in these samples were much lower (H-ras: 2%; 95% confidence interval [95% CI], 0-11.5% and K-ras: 0%) than described for both genes in Korean studies (H-ras: 16%; 95% CI, 5.2-26.8% and K-ras: 44%; 95% CI, 29.5-58.5%). CONCLUSIONS: Although the reason for this discrepancy is not clear, there were no major differences found in histology or clinical stages. Based on this study of 50 sarcoma samples from American patients and the authors' previous study of 45 Korean tumor samples, the authors conclude that differing genetic and/or environmental mechanisms can affect sarcoma development or progression. Mutation of the H-ras and K-ras genes appears to be uncommon in sarcomas occurring in American patients, suggesting that the activation by point mutations of the H-ras and K-ras genes does not play a significant role in the pathogenesis or progression of sarcoma in these patients.

Adolescent↗
PubMed1998

Expression of c-Met receptor and hepatocyte growth factor/scatter factor in synovial sarcoma and epithelioid sarcoma.

Overexpression of c-Met receptor/hepatocyte growth factor (scatter factor) system (c-Met/HGF/SF) as a physiologically paracrine cellular signaling system is thought to be involved in the progression of malignant tumours. In 26 synovial sarcomas and epithelioid sarcomas, c-Met and HGF/SF expression was analysed immunohistochemically. There were 10 biphasic synovial sarcomas, 7 of which showed moderate to strong c-Met expression in epithelial areas compared with the fibrous component, with corresponding expression of HGF/SF. Six of 9 monophasic fibrous synovial sarcomas showed only very faint c-Met and corresponding HGF/SF expression. In 7 epithelioid sarcomas strong expression of c-Met and HGF/SF was observed within epithelioid tumour cells. Non-radioactive in situ hybridization demonstrated the synthesis of c-Met receptor in tumor cells by detecting c-met-mRNA. This analysis shows that in synovial sarcomas and epithelioid sarcomas, tumour entities with epithelial and mesenchymal structures, c-Met and HGF/SF overexpression can be detected, indicating a role of this signaling system in these subtypes of sarcoma, and especially in the more epithelioid tumour phenotype. An autocrine interaction between overexpressed c-Met receptor and HGF/SF may be hypothesized.

Hepatocyte Growth Factor↗
PubMed2006

Cluster analysis of immunohistochemical profiles in synovial sarcoma, malignant peripheral nerve sheath tumor, and Ewing sarcoma.

As a result of overlapping morphologic and immunohistochemical features, it can be difficult to distinguish synovial sarcoma, malignant peripheral nerve sheath tumor, and Ewing sarcoma/primitive neuroectodermal tumor in core biopsies. To analyze and compare immunohistochemical profiles, we stained tissue microarrays of 23 synovial sarcomas, 23 malignant peripheral nerve sheath tumors, and 27 Ewing sarcomas with 22 antibodies potentially useful in the differential diagnosis, and analyzed the data with cluster analysis. Stain intensity was scored as none, weak, or strong. For CD99, tumors with membranous accentuation were independently categorized. Cluster analysis sorted five groups, with like tumors clustering together. Synovial sarcoma clustered into two groups: one cytokeratin and EMA positive (n = 11), the other mostly cytokeratin negative, EMA positive, bcl-2 positive and mostly CD56 positive (n = 9). Malignant peripheral nerve sheath tumor clustered into two groups: one S100 positive, with nestin and NGFR positivity in most (n = 10), the other mostly S100 negative, and variably but mostly weakly positive for nestin and NGFR (n = 11). Ewing sarcomas clustered into a single group driven by membranous CD99 staining. Thirteen cases failed to cluster (outliers), while three Ewing sarcomas clustered into groups of other tumor types. Paired antibodies for each tumor type determined by visual assessment of cluster analysis data and statistical calculations of specificity, sensitivity, and predictive values showed that EMA/CK7 for synovial sarcoma, nestin/S100 for malignant peripheral nerve sheath tumor, and membranous CD99/Fli-1 for Ewing sarcoma yielded high specificity and positive predictive values. Cluster analysis also highlighted aberrant staining reactions and diagnostic pitfalls in these tumors. Hierarchical cluster analysis is an effective method for analyzing high-volume immunohistochemical data.

12E7 Antigen↗
PubMed1978

The "sarcoma-specific" region of Moloney murine sarcoma virus 124.

Labeled, purified 30S RNA from Moloney murine sarcoma virus was annealed to an excess of Moloney murine leukemia virus complementary DNA. Upon treatment of the resulting DNA.RNA hybrids with RNase H followed by sucrose gradient sedimentation, and undigested 18S RNA molecule was recovered. This RNA molecule was shown to represent the "sarcoma-specific" region of the virus. The unintegrated linear DNA provirus of murine sarcoma virus 124 was isolated from newly infected cells and a physical map of the sarcoma-specific region was obtained. First, unintegrated full-length linear proviral DNA molecules were cleaved by several restriction endonucleases. The reciprocal position and orientation with respect to the viral RNA of the resulting fragments were established. The location of the sarcoma-specific region was determined by competition-hybridization with 125I-labeled viral genomic RNAs and proviral DNA fragments. A 1500-base-pair fragment was obtained by cleavage with HindIII + Bgl II. This fragment mapped between 750 and 2250 base pairs from the right end of the proviral DNA (corresponding th the 3' terminus of the viral RNA) and contained the whole set of the sarcoma-specific information. This murine sarcoma virus proviral restriction fragment is approximately of the same size and map position as the isolated 18S sarcoma-specific RNA.

Animals↗
PubMed1989

Pathologic analysis of advanced adult soft tissue sarcomas, bone sarcomas, and mesotheliomas. The Eastern Cooperative Oncology Group (ECOG) experience.

A total of 488 tumors entered in the Eastern Cooperative Oncology Group (ECOG) Study EST 3377 were evaluated histologically by a panel of pathologists from member institutions for quality control purposes. The overall agreement rate between the eligible submitting diagnosis and the pathology review panel's diagnosis was 74% (312/424). In 10% (44/424), the case was excluded because it was deemed to be nonsarcoma. In the other 16%, the disagreement concerned the type of sarcoma. The histologic type with the lowest agreement rate was rhabdomyosarcoma (17%), followed by sarcoma not otherwise specified (NOS) (27%), angiosarcoma (33%), and fibrosarcoma (48%). These figures reflect the significant degree of difficulty in the diagnosis of these tumor types. The treatment response rate of soft tissue sarcomas in the randomized study of Adriamycin (Adria Laboratories, Columbus, OH) regimens was slightly higher for those with lower grade sarcomas, i.e., 25% (four of 16) response rate for Grade 1 lesions; 22% (17/77) for Grade 2, and 21% (35/170) for Grade 3. When adjusted for type of sarcoma, there was no noticeable difference between Grade 1-2 versus 3 in response rate. A statistically significant difference in the percentage of complete responders was noted between Group A tumors (synovial sarcoma, hemangiopericytoma, sarcoma NOS, and Ewing's; 12.2%) versus Group B tumors (all other types--mostly spindle cell sarcomas; 3.5%) (P = 0.02).

Adolescent↗
PubMed1992

VLA-4 integrin on sarcoma cell lines recognizes endothelial VCAM-1. Differential regulation of the VLA-4 avidity on various sarcoma cell lines.

Osteosarcomas and rhabdomyosarcomas are vigorously invading tumors. Before they can extravasate to the parenchymal organs and form metastases, they have to adhere to the endothelial cells lining the blood vessels and then penetrate through the endothelium. We show that several human sarcoma cell lines, osteosarcomas HOS, MG-63, U2-OS, and a rhabdomyosarcoma RD, express VLA-4 molecule on their surface and bind to the VCAM-I-expressing activated endothelial cell line Ea.hy 926. The increased sarcoma-cell adhesion could be abolished by treating the sarcoma cells with monoclonal antibodies (MAbs) VLA4 (both alpha- and beta-chain, HP2/1 and 4B4 respectively) or treating endothelial cells with VCAM-I antibody (4B9). Furthermore, we show that sarcoma cells adhere to recombinant soluble VCAM-I protein. On the other hand, these sarcoma cell lines do not express marked amounts of other ligands (such as CDII/18 or sialyl-Lex) for other endothelial adhesion molecules (ICAM-I, ICAM-2, E- and P-selectin) indicating that the VLA-4-VCAM-I dependent pathway might be of major importance in sarcoma extravasation. VLA-4 is not always in an avid form and therefore the expression of VLA-4 does not directly predict adherence to VCAM-I. The avidity of VLA-4 (measured by adherence to soluble VCAM-I) of MG-63 and U2-OS cells could be increased by a 30-min PMA treatment, whereas the avidity of VLA-4 on HOS cells increased only after 48 hr of PMA induction. Our results show that sarcoma cell lines (HOS, MG-63, U2-OS and RD) adhere to stimulated endothelium via VLA-4-VCAM-I adhesion molecules and that VLA-4 avidity on sarcoma cells can be differentially modulated by PMA.

Base Sequence↗
PubMed1981

Properties of a sarcoma-growth-factor-like peptide from cells transformed by a temperature-sensitive sarcoma virus.

Serum-free conditioned media was collected from three sarcoma virus-transformed cell lines and an untransformed cell line. All three virally transformed lines produced and released growth factors into their serum-free media. The major activity in all cases, whether the cells were transformed by Moloney sarcoma virus (MSV) or Kirsten sarcoma virus (KiSV), or whether they were mouse or rat, was a sarcoma-growth-factor (SGF)-like activity with an apparent molecular weight of 10,000. The SGF-like pools from a Moloney sarcoma virus-transformed mouse 3T3 cell and a Kirsten sarcoma virus-transformed NRK cell were further purified by carboxymethyl cellulose chromatography. The elution profiles of these peptides were very similar. The serum-free conditioned media from the untransformed cells showed no detectable growth stimulating activity. The temperature sensitivity of an SGF-like growth factor from the supernate of a NRK cell transformed by a wild-type Kirsten sarcoma virus (KiSV) was compared with that of the SGF-like activity from the supernates of a NRK cell transformed by a ts-mutant of KiSV that is temperature sensitive with respect to transformation (ts-371 Cl 5). Neither the cells transformed by the wild-type sarcoma virus nor those transformed by the temperature sensitive virus released a SGF-like activity that was temperature sensitive under the conditions of the assays.

Animals↗
PubMed2000

Beta-catenin in soft tissue sarcomas: expression is related to proliferative activity in high-grade sarcomas.

Besides its role in cell adhesion, beta-catenin exerts a function as an oncoprotein. The aim of this study was the characterization of its expression, possible mutation, and the assessment of beta-catenin as a prognostic indicator for soft tissue sarcomas. A total of 115 soft tissue sarcomas were analyzed using immunohistochemistry, immunogold-electron microscopy, and DNA analysis. Information from 56 patients was available for follow-up. A statistically significant correlation was found between intracellular distribution of beta-catenin and the proliferative activity (MIB-1 expression) in high-grade sarcomas (P = .0008). Beta-catenin was identified with intracytoplasmic and nuclear accumulation, showing additional membranous staining in sarcomas with epithelioid pattern. Ultrastructurally, a colocalization between beta-catenin and nuclear heterochromatin was demonstrated. In 22 analyzed tumors, only one (yet undescribed) mutation of the beta-catenin gene (C-A transversion) could be detected. Prognostic validity of the cellular expression of beta-catenin, however, was not proven. Apart from its membranous function as an effective molecule for cell-adhesion in sarcomas with epithelioid pattern, beta-catenin may act as an oncoprotein in sarcomas with intracytoplasmic and nuclear localization with binding to nuclear DNA. A previously discussed stimulation of cell proliferation caused by an increased beta-catenin level can also be postulated for high-grade soft tissue sarcomas in correlation with the rate of proliferation. Mutations of the beta-catenin gene are probably of lesser importance for the accumulation of beta-catenin in soft tissue sarcomas.

Adult↗
PubMed1975

Separation of sarcoma virus-specific and leukemia virus-specific genetic sequences of Moloney sarcoma virus.

We have studied the nucleic acid sequences in nonproducer cells transformed by Moloney sarcoma virus or Abelson leukemia virus (two types of replication-defective, RNA-containing, viruses isolated by passage of Moloney leukemia virus in BALB/c mice). DNA probes from the Moloney leukemia in virus detect RNA in both Abelson virus-transformed nonproducer cells and Moloney sarcoma virus-transformed nonproducer cells. A sarcoma-specific cDNA, prepared from the Moloney sarcoma virus, has extensive homology to RNA found in heterologous nonproducer cells transformed by Moloney sarcoma virus, has little homology to RNA in cells producing Moloney leukemia virus, and no detectable homology to RNA in nonproducer cells transformed by the Abelson virus. By analogy to earlier data on avian and mammalian sarcoma viruses, these results suggest that the Moloney sarcoma virus arose by recombination between a portion of the Moloney leukemia virus genome and additional sarcoma-specific information, and indicate that the expression of this information in not essential for Abelson virus-mediated fibroblast transformation.

Cell Line↗
PubMed1998

Identification of HHV8 in early Kaposi's sarcoma: implications for Kaposi's sarcoma pathogenesis.

AIMS: Kaposi's sarcoma is a vascular tumour of uncertain pathogenesis possibly caused by an infectious agent, identified in high risk groups. Accumulating solution phase polymerase chain reaction (PCR) and seroepidemiological data suggest that a previously undescribed herpes DNA virus (human herpesvirus 8 (HHV8)) is the causative agent. Using a unique cohort of early Kaposi's sarcoma, the precise cell type infected with HHV8 in such lesions was identified to elucidate further the role of HHV8 in the pathobiology of Kaposi's sarcoma. METHODS: Sixteen cases of early Kaposi's sarcoma (derived from skin and lymph node) were assessed for the presence of HHV8 using both standard solution phase PCR and TaqMan PCR to the KS330 Bam region of HHV8. In situ amplification was also performed on a selected group in an attempt to identify the candidate infected cells. RESULTS: Using both conventional solution phase and TaqMan PCR, 87% of cases were positive. In addition, HHV8 amplicons were localised in situ to endothelial and spindle cell proliferations in early Kaposi's sarcoma. The HHV8 viral load varied from lesion to lesion. CONCLUSIONS: The presence of HHV8 in early lesions supports a role for HHV8 in the pathogenesis of Kaposi's sarcoma. Coupled with recent seroepidemiological studies, these results suggest that HHV8 is the aetiological agent of Kaposi's sarcoma. Its precise interaction with other factors known to be involved in the development of Kaposi's sarcoma, including cytokines and anti-apoptosis genes, requires elucidation.

Adolescent↗
PubMed2006

The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor as a therapeutic target for the treatment of Kaposi's sarcoma.

The Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a G protein-coupled receptor (vGPCR) that has been implicated in the initiation of Kaposi's sarcoma, identifying vGPCR as an attractive target for preventing Kaposi's sarcoma. However, as only a fraction of cells in advanced Kaposi's sarcoma lesions express vGPCR, it is unclear whether this unique viral oncogene contributes to Kaposi's sarcoma progression. We therefore set out to determine whether the few cells that express vGPCR in established tumors represent an appropriate therapeutic target for the treatment of patients with preexisting Kaposi's sarcoma. To this end, we generated endothelial cell lines stably expressing vGPCR or key KSHV latently expressed proteins (vCyclin, vFlip, and LANA1). The endothelial cell line expressing vGPCR was rendered sensitive to treatment with the nucleoside analogue ganciclovir by using a bicistronic construct coexpressing the herpes simplex virus 1 thymidine kinase. S.c. injection into nude mice with mixed-cell populations formed tumors that approximate the ratio of vGPCR-expressing and KSHV latent gene-expressing cells. These mice were then treated with ganciclovir to specifically target only the vGPCR-expressing cells. Surprisingly, despite the expression of KSHV latent genes in the vast majority of tumor cells, specifically targeting only the few vGPCR-expressing cells in established tumors resulted in tumor regression. Moreover, we observed an increase in apoptosis of latent gene-expressing cells after the pharmacologic deletion of the vGPCR-expressing cells. These findings indicate that vGPCR may play a key role in Kaposi's sarcoma progression and provide experimental justification for developing molecular-based therapies specifically targeting vGPCR and its effectors for the treatment of Kaposi's sarcoma patients.

Animals↗