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PubMed2003

Central pain in cancer patients.

The prevalence of pain caused by injury to the central nervous system (CNS), or central pain (CP), in cancer patients is unknown. In order to define prevalence and characteristics of central pain in hospitalized patients with cancer, we performed a retrospective review of medical records of patients evaluated by 2 different services: the Pain Service and the Neurology Service, at Memorial Sloan-Kettering Cancer Center. The prevalence of CP in these patients was 4% and 2%, respectively. Primary and metastatic tumors and their therapy, including surgery, radiation and chemotherapy, were all potential causes of CP. The occurrence of CP in patients with primary CNS tumors was higher in patients with spinal cord tumors compared to patients with brain tumors (P <.0001).

Adult↗

PubMed2025

A comprehensive analysis of supermere, exomere, and extracellular vesicle isolation and cargo in colorectal cancer.

Biofluids contain a heterogeneous mixture of extracellular vesicles and non-vesicular nanoparticles (including exomeres and supermeres) that transport a diverse array of proteins, RNA, and lipids. Our previous efforts to characterize the contents of these carriers in colorectal cancer relied on 2D culture systems requiring large-scale setups and time-consuming ultracentrifugation-based isolation. To streamline this process, we have combined 3D hollow-fiber bioreactor production and fast-protein liquid chromatography-based size-exclusion chromatography. Here, we compare the impact of culture methods and purification strategies on small extracellular vesicle, exomere, and supermere cargo. Proteomic analyses show consistently distinct profiles for extracellular vesicles, exomeres, and supermeres regardless of culture conditions or isolation method. In contrast, these two variables influence small RNAs, their base modifications, and lipidomic profiles. We present an online tool to query these and future secretome datasets (https://superomics.shinyapps.io/browse).

Humans↗

PubMed2024

SUMOylation controls Hu antigen R posttranscriptional activity in liver cancer.

The posttranslational modification of proteins critically influences many biological processes and is a key mechanism that regulates the function of the RNA-binding protein Hu antigen R (HuR), a hub in liver cancer. Here, we show that HuR is SUMOylated in the tumor sections of patients with hepatocellular carcinoma in contrast to the surrounding tissue, as well as in human cell line and mouse models of the disease. SUMOylation of HuR promotes major cancer hallmarks, namely proliferation and invasion, whereas the absence of HuR SUMOylation results in a senescent phenotype with dysfunctional mitochondria and endoplasmic reticulum. Mechanistically, SUMOylation induces a structural rearrangement of the RNA recognition motifs that modulates HuR binding affinity to its target RNAs, further modifying the transcriptomic profile toward hepatic tumor progression. Overall, SUMOylation constitutes a mechanism of HuR regulation that could be potentially exploited as a therapeutic strategy for liver cancer.

Animals↗

PubMed2026

FANCM is required for the PAX3::FOXO1-driven oncogenic program in rhabdomyosarcoma.

Many cancers are driven by mutationally altered transcription factors (TFs) that rewire cells to an oncogenic state. Cells must activate specific mechanisms to tolerate the burden of oncogenic TF activity. To define such mechanisms, we focused on a canonical oncogenic fusion protein-driven cancer, alveolar rhabdomyosarcoma (ARMS), where the PAX3::FOXO1 fusion protein hyperactivates and mislocalizes PAX3 and FOXO1 TF functions. Employing sequential functional genomic CRISPR-Cas9 screens, we identified FANCM, a DNA translocase in the Fanconi anemia pathway, as a selective dependency in PAX3::FOXO1+ ARMS. FANCM loss reduces fusion protein levels, induces myogenic differentiation, and disrupts the PAX3::FOXO1 transcriptional program, thereby halting oncogenic proliferation. Mechanistically, FANCM depletion exacerbates replication stress (RS) and DNA damage signaling, with chromatin-associated RS enriched at PAX3::FOXO1 target gene loci, resulting in selective downregulation of the oncogenic program. CRISPR exon-tiling screens prioritized FANCM's helicase and DNA-binding domains as essential for this dependency, linking FANCM-mediated replication fork binding to sustained oncogenesis.

ARMS↗

PubMed1999

Activation of blood coagulation and the activity of cancer procoagulant (EC 3.4.22.26) in breast cancer patients.

The activity of cancer procoagulant (CP), prothrombin time (PT), activated partial thromboplastin time (APTT), the concentration of thrombin-antithrombin complexes (TAT) and the concentration of fibrinogen were analysed in blood of breast cancer patients scheduled for surgery. The serum level of CP activity was dependent on the stage of the disease. The CP activity was increased in 72% of patients with an early stage of cancer and in only 20% of patients with an advanced stage of the disease when compared to the baseline level for non-cancer controls. In all patients PT remained at normal levels (80-120%). There was no significant change in APTT (27-39 s) in early stage cancer patients. Only one patient with advanced cancer had APTT shortened to 23 s. Also one advanced stage patient had significantly elevated level of TAT (14.96 microg/l); in all other patients the concentration of TAT remained at normal levels (1-4.1 microg/l). Forty-four percent of early stage cancer patients and 22% of advanced cancer patients had an elevated level of fibrinogen (Fg) ( > 350 mg%). However, there was no correlation between the level of Fg and the CP activity (P > 0.05). The data suggest that: (1) serum CP activity increases at the early stage of breast cancer and decreases down to the normal level in the advanced stage of the disease; (2) there is no evidence of blood clotting activation in the early stage breast cancer patients; and (3) CP does not facilitate the activation of coagulation in the breast cancer patients or the level of such activation is below the sensitivity of assays used in the experiment.

Antithrombin III↗

PubMed2005

Clinical features of chronic pancreatitis in Korea: a multicenter nationwide study.

BACKGROUND/AIMS: No reliable nationwide clinical data about chronic pancreatitis (CP) was available in Korea. The etiology and clinical features of CP were investigated using a multicenter nationwide study. METHODS: 814 cases of CP were enrolled retrospectively over the past 4 years at 13 hospitals. The following data were obtained from all patients: etiology, symptoms, complications, and surgery. RESULT: Alcohol (64.3%) was the major cause of CP and idiopathic CP (20.8%) was the second most common form. Mean patient age was 50.6 years and the male:female ratio was 6:1 (24:1 for alcoholic CP vs. 2:1 in idiopathic CP, p < 0.001). Diabetes (31.6%), pseudocysts (28.4%), biliary stricture (13.9%), and pancreatic ascites (6.6%) were the main complications. Of these, diabetes (35 vs. 26%) and pseudocyst (33.7 vs. 21.9%) were more frequent in alcoholic than in idiopathic CP. Pancreatic cancer developed in 25 patients (3.1%) during follow-up and their mean age was 59.1 years. CONCLUSIONS: In Korea, alcohol is the most common etiology of CP. Moreover, diabetes and pseudocysts are frequent complications, especially in alcoholic CP, and pancreatic cancer development is not infrequent.

Age Distribution↗

PubMed1999

Micronucleated lymphocyte rates from head-and-neck cancer patients.

We investigated whether head-and-neck cancers are associated with an increased micronucleated cell rates (MN cell rates) and whether risk factors for these cancers are associated with alterations in micronucleated lymphocytes. MN cell rates were assessed in cytokinesis-blocked lymphocytes of 57 head-and-neck cancer patients (CP) before any anticancer treatment and of 198 male and female healthy subjects (HS). In the HS group, only smoking status significantly affect MN cell rates. In CP group age, sex, tobacco status, alcohol status, tumor stage, family history of cancer had no significant effect. For the non-smokers, the comparison between MN cell rates in HS and CP adjusted for age and sex showed a significant difference. The increase of MN cell rates in non-smokers patients may be attributable to cancer status. For the smokers, the comparison of MN cell rates in HS and CP matched for age and sex showed no significant difference. Pathological status could mask the smoking effect on peripheral blood lymphocytes in patients. Moreover, it probably could partly explain why MN cell rates in matched-CP smokers and HS smokers were similar. The authors do not recommend the CBMN assay in this present form to study smoking DNA-damage effects in peripheral blood lymphocytes of cancer patients, especially for patients with upper aero-digestive tract cancers or lung cancers for which tobacco is the major risk factor.

Adult↗

PubMed2005

The activity of cancer procoagulant in cases of uterine leiomyomas.

PURPOSE: It is currently believed that cancer procoagulant (CP), an enzymatic protein, is a product of malignant neoplastic cells. The present study was designed to test whether it is also synthesized by benign neoplastic cells, namely uterine leiomyomas. MATERIALS AND METHODS: We determined the activity of CP in the blood serum of women with uterine leiomyomas (N = 24), normal women (N = 15), and genital cancer patients (N = 6) by the coagulative method according to Gordon and Benson. Also, the CP activity in 10% tissue homogenates of uterine leiomyomas, normal uterine muscle and tissues of cervical and endometrial carcinoma was determined by the chromogenic method according to Colucci et al. RESULTS: The mean CP activity in the sera of women with uterine leiomyomas was 181.1 seconds (s) +/- 19.9 s, in healthy women--293.2 s +/- 33.8 s, and in genital cancer patients--78.8 +/- 18.5 s (all differences: p < 0.001). Similarly, in homogenates of uterine leiomyomas the CP activity was 19.6 +/- 3.8 nmoles pNa/ml, in normal uterine muscle it was 13.2 +/- 2.2 nmoles pNa/ml, and in cancerous tissue--28.0 +/- 6.6 nmol pNa/ml (all values being significantly different from each other). There was a strong correlation (r = -0.8122; p < 0.001) between the CP activity in uterine leiomyomas and serum activity, suggesting that the source of the serum CP activity was from the leiomyoma. The coagulation time of 120 to 240 s by the Gordon and Benson method supported the diagnosis of uterine leiomyoma, and a value below 120 s--the suspicion of genital cancer. CONCLUSIONS: Uterine leiomyomas, representing benign genital neoplasia, synthesize CP and are the likely origin of CP activity in blood, as has been described for malignant tumors, but to a lesser degree. There may be a role for CP as a tumor marker of genital neoplasia.

Adult↗

PubMed2007

Mental health literacy in Japanese cancer patients: ability to recognize depression and preferences of treatments-comparison with Japanese lay public.

BACKGROUND: Insufficient knowledge about mental illness and its treatment has been shown to constitute a major barrier to its adequate care for mental illness in the lay public (LP). We therefore examined Japanese cancer patients' (CP) ability to recognize depression and their preferences of its treatments. PARTICIPANTS AND METHOD: One hundred lung CP and 300 LP were selected at random to participate in the study. Structured interviews using a vignette of a person with both cancer and depression were conducted with CP, and those using a vignette of a person with depression were carried out with LP, respectively. RESULTS: Only 11% of CP recognized the presence of depression in the vignette, while 25% of LP did (p<0.001). There were few significant differences in the preference for standard psychiatric treatments between CP and LP: standard treatments such as antidepressants (CP: 39%, LP: 36%) were less often rated as helpful, whereas non-standard treatments such as physical activity (CP: 85%, LP: 66%) were most often rated as helpful. CONCLUSIONS: The results indicated that cancer patients' knowledge about mental illness and its treatment were insufficient. Psychological education may reduce patient-related barriers to seek and to utilize optimal mental health care in cancer patients.

Adult↗

PubMedDate not supplied

The mutant p53-conformation modifying drug, CP-31398, can induce apoptosis of human cancer cells and can stabilize wild-type p53 protein.

CP-31398, a styrylquinazoline, emerged from a screen for therapeutic agents that restore a wild-type DNA-binding conformation of mutant p53 to suppress tumors in-vivo (Science 286, 2507, 1999). We investigated the growth inhibitory mechanism of CP-31398 using nine human cancer cell lines containing wild-type, mutant or no p53 expression. Six of nine cell lines underwent apoptosis after exposure to CP-31398, while two cell lines, DLD1 colon cancer and H460 lung cancer, underwent exclusively cell cycle arrest. Cell cycle arrest preceded the apoptosis in some cases. CP-31398 did not inhibit growth of the p53 non-expressing ovarian cancer cell line SKOV3. Interestingly, we found that wild-type p53 protein is stabilized upon CP-31398 exposure. p53 target genes such as p21WAF1/Cip1, and KILLER/DR5 were upregulated by CP-31398, but their expression did not correlate with arrest or apoptosis induction. Combination of CP-31398 and TRAIL or chemotherapeutic agents enhanced cancer cell killing effect possibly through upregulation of p53-regulated genes such as KILLER/DR5. Bax-/-, wild-type p53-expressing cells displayed reduced susceptibility to killing by CP-31398. An Affymetrix GeneChip Array screen revealed that CP-31398 alters expression of non-p53 target genes in addition to p53-responsive genes. Although our preliminary data suggest that CP-31398 does not alter wild-type p53:MDM2 interaction, further efforts are required to elucidate the mechanism of wild-type p53 stabilization by CP-31398. The results increase our understanding of CP-31398 action, and suggest strategies for improving its specificity, possibly through use of microarrays to screen related compounds with higher mutant p53-specificity.

Antineoplastic Agents↗

PubMed1997

Cancer procoagulant: a factor X activator, tumor marker and growth factor from malignant tissue.

Hemostatic abnormalities associated with malignant disease led to the search for and discovery of a proteolytic enzyme that activated factor X in the blood coagulation cascade. It was named cancer procoagulant (CP). CP is a cysteine proteinase that is found in malignant and fetal (human amnion-chorion) tissue; it has not been found in normally differentiated tissue. It is a calcium-dependent, Mn2+ stimulated enzyme that has enhanced activity and inhibition in a reduced environment. This review presents a complete compilation and discussion of the known chemical and enzymatic characteristics of CP as well as many purification and assay procedures. Several unique properties of these procedures are described. Some problems and controversies are highlighted in each of the sections. An immunoassay for CP as a tumor marker and some of its potential applications in the diagnosis and monitoring of cancer are reviewed. Some therapeutic implications of CP are noted in light of the observation that antibodies to CP block the metastatic seeding of lung colonies in vivo and diminish the viability of tumor cells in vitro. Finally, comments about the relationship between tissue factor and CP in the malignant cells are provided.

Animals↗

PubMed1998

Activation of coagulation and angiogenesis in cancer: immunohistochemical localization in situ of clotting proteins and vascular endothelial growth factor in human cancer.

Thrombin-catalyzed, cross-linked fibrin (XLF) formation is a characteristic histopathological finding in many human and experimental tumors and is thought to be of importance in the local host defense response. Although the pathogenesis of tumor-associated fibrin deposition is not entirely clear, several tumor procoagulants have been described as likely primary stimuli for the generation of thrombin (and XLF) in the tumor microenvironment (TME). In a previous study of a variety of human tumors we have shown that tissue factor (TF) is the major procoagulant. However, the relative contribution to fibrin deposition in the TME of tumor cell TF and host cell TF (eg, macrophage-derived) was not established. In addition, recent evidence has implicated TF in the regulation of the synthesis of the pro-angiogenic factor vascular endothelial growth factor (VEGF) by tumor cells. In the current study we used in situ techniques to determine the cellular localization of XLF, TF, VEGF, and an alternative tumor procoagulant, so-called cancer procoagulant (CP), a cysteine protease that activates clotting factor X. In lung cancer we have found XLF localized predominantly to the surface of tumor-associated macrophages, as well as to some endothelial cells and perivascular fibroblasts in the stromal area of the tumors co-distributed with TF at the interface of the tumor and host cells. Cancer pro-coagulant was localized to tumor cells in several cases but not in conjunction with the deposition of XLF. TF and VEGF were co-localized in both lung cancer and breast cancer cells by in situ hybridization and immunohistochemical staining. Furthermore, a strong relationship was found between the synthesis of TF and VEGF levels in human breast cancer cell lines (r2 = 0.84; P < 0.0001). Taken together, these data are consistent with a highly complex interaction between tumor cells, macrophages, and endothelial cells in the TME leading to fibrin formation and tumor angiogenesis.

Blood Coagulation↗

PubMed2005

[Cancer procoagulant and cathepsin D activity in blood serum in patients with bladder cancer].

The increasing morbidity and mortality rates of bladder cancer forced the scientists to search for new unfailing diagnostic and therapeutic methods that will improve treatment effects. There are biochemical cancer markers as cancer procoagulant (CP) and cathepsin D which may be used to this end. The aim of the study was to evaluate the activity of the cancer procoagulant and cathepsin D in the blood serum in patients with superficial bladder cancer. The venous blood samples were from 15 patients with microscopically proved superficial bladder carcinoma (i.e. study group) and 15 normal volunteers as a control group. The serum blood CP activity was determined by the Gordon-Benson's coagulation method and expressed by the clotting time in seconds (s) while the cathepsin D activity was determined by the Folin-Ciocalteau's method and expressed by a quantity of released tyrosine in nmol/ml per 4 hours. The CP activity in serum of patients with superficial bladder cancer was increased in statistically way as compared to the non-cancer controls (p<0.0001). The cathepsin D activity in blood serum of the study group was also enhanced as compared to the control group and the said values differed statistically (p<0.0351). It appears to be justifiable to apply the determination of the CP and cathepsin D activity in blood serum for the diagnostics of superficial bladder cancer.

Aged↗

PubMed1979

Electron spin resonance studies on properties of ceruloplasmin and transferrin in blood from normal human subjects and cancer patients.

The methodology of blood sample preparation and analysis has been examined to further evaluate the technique of electron spin resonance (ESR) for possible use in detecting cancer and in monitoring the progress of cancer therapy. Frozen whole blood and serum samples from 278 normal donors and 97 cancer patients were studied by ESR for signal intensity from Cu+2 bound to ceruloplasmin (g factor = 2.05). The signal from this species (Cu+2-CP) in serum rose sharply during the first two hours of storage at room temperature after being drawn from the subject, and then reached a plateau. The average Cu+2-CP ESR signal intensity was significantly different for control groups of males, females not taking estrogen medication, and females taking estrogens. The mean ESR signal intensities of Cu+2-CP from cancer patients separated into the same groups as the control data were approximately twice as great as the mean control levels. Total serum copper levels were correlated with ESR intensities of Cu+2-CP and indicated that the ratio of Cu+2/Cu+1 in CP is higher in serum from cancer patients than from controls.

Age Factors↗

PubMed1989

Analysis of serum cancer procoagulant activity and its possible use as a tumor marker.

The two objectives of the study were to determine whether a procedure could be developed for measuring cancer procoagulant (CP) activity in human serum and if this procedure provided a method for distinguishing people with cancer from those without cancer. A procedure was developed for processing human serum such that the activity of other coagulation enzymes would be minimized and the activity of cancer procoagulant could be measured. In a blinded study, we collected serum from 61 individuals in serum separator tubes, removed the clot by centrifugation, extracted the serum with a simple, single step procedure and analyzed the extract for CP activity. The results indicate that this test could correctly identify about 92% of the cancer patient serum samples and about 75% of the non-cancer patients serum samples, for an overall accuracy of about 85%.

Biomarkers, Tumor↗

PubMed2026

highSpaClone enables copy number alteration inference and tumor subclone analysis for high-resolution spatial transcriptomics.

High-resolution spatially resolved transcriptomics (SRT) offers unprecedented opportunities to investigate tumor heterogeneity but poses substantial computational and analytical challenges. Here, we present highSpaClone, a computational framework for copy number alteration (CNA) inference and tumor subclone identification from high-resolution SRT data across multiple spatial scales. By integrating spatial constraints into CNA estimation and clonal clustering, highSpaClone enables neighboring spatial locations to share information, thereby improving the robustness of genomic signals and the accuracy of subclone delineation. Across multiple Xenium and Visium HD datasets, highSpaClone revealed unique transcriptional programs, clonal evolutionary trajectories, and distinct tumor-microenvironment interactions. Furthermore, in human colorectal cancer samples, highSpaClone detected CNA events in histologically normal epithelial regions, highlighting early genomic alterations associated with field cancerization. These findings establish highSpaClone as a scalable framework for studying clonal architecture and tumor evolution.

CP: cancer biology↗

PubMed1998

Generation of a monoclonal antibody that inhibits the procoagulant activity of various cancer cell lines.

BACKGROUND: Tumor procoagulant is one of the factors responsible for disseminated intravascular coagulation and metastasis. The authors found procoagulant activity in LK52 human squamous cell carcinoma cells, which they designated cancer cell-derived blood coagulating activity 1 (CCA-1). A monoclonal antibody (MoAb) was generated to characterize this CCA-1 procoagulant activity. To date, antibodies that show an inhibitory effect on procoagulant activity as well as high reactivity in cancer cells are well known for their tissue factor specificity. METHODS: Characterization of the procoagulant activity of CCA-1 was performed and an anti-CCA-1 MoAb, FS01, was generated. CCA-1 expression on the cancer cell surface was examined by flow cytometry. Procoagulant activity of various cancer cell lines and the inhibitory effect of the FS01 MoAb on this procoagulant activity was monitored by a clot timer. RESULTS: The enzymologic character differed from that of cancer procoagulant (CP). The FS01 MoAb inhibited the procoagulant activity of CCA-1, but did not inhibit that of tissue factor. A positive correlation was observed between the expression intensity of CCA-1 and the inhibitory effect of the FS01 MoAb on the procoagulant activity of cancer cell lines. Expression of CCA-1 was observed more frequently than that of tissue factor in human cancer cell lines. CONCLUSIONS: The FS01 MoAb generated in the current study is a new antibody that reacts with various cancer cell lines, but not with normal cells. FS01 inhibits cancer cell-derived procoagulant activity and does not react with tissue factor and CP. CCA-1, which is recognized by the FS01 MoAb, appears to play a major role in cancer cell-derived procoagulant activity.

Adult↗

PubMed1980

Effect of tumor removal on the presence of lymphocytic cortisol metabolism-enhancing factor in plasma of cancer patients.

Because lymphocytic cortisol metabolism-enhancing factor (LCMEF) is absent in the plasma of cancer patients (CP), this study was undertaken to determine the influence of tumor removal on this phenomenon. Known concentrations of human lymphocytes were incubated with cortisol in media containing 50% phosphate-buffered saline (PBS) and 50% of one of the following: a) homologic normal plasma (HP),b) plasma from patients with noncancerous diseases (NCD) before surgery, c) plasma from patients with NCD after surgery, d) plasma from CP before tumor removal, e) plasma from CP after tumor removal, f) plasma from long-surviving CP (LSCP), and g) PBS. With the exception of plasma from the LSCP group, all the plasma had the capacity to enhance the lymphocytic cortisol metabolism (LCM) when compared with that of PBS. There was no significant difference between the metabolism obtained with HP and that obtained with plasma from patients with NCD either before or after surgery. The plasma from CP led to a significant reduction in activity, with no significant difference in conversion rates before and after tumor removal. The plasma from LSCP failed to enhance LCM, had a conversion rate similar to that of PBS and significantly lower than that of the plasma from CP, and appeared to contain no LCMEF. These findings, which showed that the lack of LCMEF in CP is not influenced by tumor removal, may indicate 1) that the lack of LCMEF preceded the appearance of cancer or 2) irreversibility of a possible anti-LCMEF synthesis effect was induced by the tumor.

Biological Products↗