Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ascitic fluid samples from 19 patients with ovarian carcinoma, 3 with a benign ovarian tumor, and 5 with cirrhosis of the liver were examined for their content of coagulation factors and components of the fibrinolytic system. The concentration of trypsin inhibitors in the ascitic fluid was significantly higher in the presence of carcinoma. Large amounts of FDP were found in the ascitic fluid in all patients with malignant tumors, but not in the other two groups. Determination of FDP may therefore make it possible to differentiate between malignant and nonmalignant ascitic fluid.
Cancer 1975 May
PMID:Coagulative and fibrinolytic properties of ascitic fluid associated with ovarian tumors. 4 63

In order to assess the potency of antigenic fragments of carcinoembryonic antigen (CEA) in the radioimmune assay; it is necessary to know whether the high affinity of goat anti-CEA antibody (which makes possible the detection of as little as 10--11M CEA) is due to bivalent binding of the CEA molecule. Immunoglobulin G and the F(ab')2 and Fab fragments derived from it were prepared from an anti-CEA serum and tested for their abioity to bind CEA. Equivalent concentrations of binding sites of the bivalent F(ab)2 and univalent Fab fragments of anti-CEA were identical to the immunoglobulin G fraction in the standard inhibition curve. Fragments of CEA obtained by trypsin digestion produced equivalent inhigition curves when tested with either immunoglobulin G, F(ab')2, or Fab". This, increased avidity due to bivalent binding to a single antigen molecule cannot be invoked to explain the sensitivity observed in the CEA assay. This high sensitivity implicates the protein rather than the carbohydrate as an important part of the antigenic determinant(s) of CEA.
Cancer Res 1975 Jul
PMID:The binding of carcinoembryonic antigen by antibody and its fragments. 4 22

An antigen was detected in pooled human nephroblastomas using antiserum prepared in rabbits against an ethylemediaminetetra acetic acid (EDTA) extract of the tumors. This antigen was not found in normal human plasma or kidney extracts, and was not related to the ABO or Forssman blood groups. The antigen was detected in extracts of cultured nephroblastoma cells, but was not present in extracts of normal human fetal kidney cell cultures. The antigen is believed to be present at the cell surface, as cell viability was not significantly lowered during the extraction procedure. A reaction of complete identity was demonstrated by Ouchterlony double diffusion experiments with this antigen and purified bovine fetuin. The antigen was not found in extracts of human fetal spleen, thymus or kidney, nor in human fetal serum. Furthermore, the antigen does not possess determinants in common with the human alpha-fetoprotein of hepatomas, nor was it detected in human renal clear cell carcinoma. Initial characterization of the antigen showed it to be nondialysable, not sedimentable at 100,000 times g for 2 h, stable to repeated freeze-thawing and to incubation at 56 degrees C for 1 h, and water soluble over a wide pH range. The antigen was susceptible to digestion with pronase and trypsin and possibly hyaluronidase, but not to ribonuclease or neuraminidase. The protein portion is therefore of major importance to the structural integrity of this antigen. The relationship between this antigen and other abnormal materials reported previously in nephroblastoma patients is being studied.
Int J Cancer 1975 Aug 15
PMID:A fetuin-like antigen from human nephroblastoma. 5 Feb 93

Specific cell-mediated immunity to SV40 tumor-specific transplantation antigen (TSTA) in BALB/c mice undergoing progressive tumorigenesis by syngeneic SV40-transformed cells (VLM) was investigated in vivo using a tumor-cell neutralization test. Specific cellular reactivity to SV40 TSTA was not detected in BALB/c mice bearing large tumors (10-15 mm mean diameter) but was demonstrable after tumor excision. Specific cytotoxic reactivity against syngeneic SV40-transformed cells in vivo could be restored to lymphoid cells from VLM tumor-bearing mice either by culturing the lymphoid cells in vitro or by treating them with papain or trypsin. Enzyme-treated lymphoid cells from MCA tumor-bearing BALB/c mice had no cytotoxic reactivity against VLM cells. These studies suggest that tumor-bearing hosts possess lymphocytes which are sensitized to the TSTA of the tumor but that the reactivity of these lymphocytes is blocked.
Int J Cancer 1975 Aug 15
PMID:Restoration of specific immunity against SV40 tumor-specific transplantation antigen to lymphoid cells from tumor-bearing mice. 5 Oct 12

Cells from several mouse lymphomas formed rosettes with nonsensitized foreign erythrocytes through C-type virus particles clustered on the cell surface in serum-free medium held at 4 degrees C. This type of rosetting was found most typically in a lymphoma induced by Rauscher leukemia virus in tissue culture (RD-12), but it also occurred in 23 of 61 spontaneous thymic lymphomas in AKR mice. Chemically or X-ray-induced leukemias and spontaneous reticulum cell sarcomas did not form rosettes. The nature of the rosette formation may be interpreted as viral hemadsorption, with a possible relationship to hemagglutination by murine leukemia viruses. The receptor on virus particles was trypsin sensitive and showed high affinity to serum inhibitors (RIF). Serum rosette-inhibiting activity was assessed by a quantitative rosette inhibition test; rosette inhibition proved widely distributed among species. Physicochemical properties of serum RIF and their function both in vivo and in vitro were described. Rosette formation with similar temperature requirements, previously reported in a mouse lymphoma carrying membrane-bound heterophile cold hemagglutinin, was readily distinguished from viral hemadsorption by its insensitivity to mouse serum RIF.
J Natl Cancer Inst 1975 Oct
PMID:Temperature-dependent rosette formation by mouse lymphoma cells as a result of viral hemadsorption. 5 22

An ether-sensitive antigen (es-Ag) associated with bovine leukemia virus infection was detected by immunodiffusion tests. This antigen was sensitive to ether, sodium periodate, and trypsin treatment. Based on column chromatography, es-Ag was a larger molecule than that of ether-resistant antigen (gs-Ag). With infection, precipitating antibody against es-Ag developed earlier than the precipitating antibody against the gs-Ag.
J Natl Cancer Inst 1975 Nov
PMID:An ether-sensitive antigen associated with bovine leukemia virus infection. 5 35

Four cell lines, SK-N-SH, SK-N-MC, SK-N-BE(2), and IMR-32, established in vitro from tumor tissue of patients with neuroblastoma were analyzed by trypsin-Giemsa banding methods. In two of the lines a large, abnormally staining chromosome region was observed. This "homogeneously staining region" (HSR) was considerably longer than any of the bands present in normal human cells and, as revealed by both G- and Q-banding, stained with an intermediate intensity. It was located on chromosomes No 6, 10, 17, or 19 of the SK-N-BE(2) cell line and on chromosome No 1 of the IMR-32 line. In concurrent studies, long HSR's were also observed in Chinese hamster sublines that had been exposed to and had developed high levels of resistance to methotrexate or methasquin and high levels of activity of target enzyme dihydrofolate reductase. For several sublines with the highest levels of enzyme activity, approximately 2% of the total cell protein was dihydrofolate reductase. Of 13 independently derived sublines with acquired resistance to antifolate, only those 7 with greater than 100-fold increases in enzyme activity consistently exhibited HSR's. These regions comprised 2-5% of the total length of the chromosome complement and were specifically localized, as demonstrated by G-banding. Analysis of chromosome replication patterns of the HSR in human neuroblastoma and in drug-resistant Chinese hamster cells by tritiated thymidine radioautography indicated that the long, abnormally staining region replicated relatively rapidly and synchronously and terminated replication before the midpoint of the S phase. The HSR thus appeared to represent a novel chromosome abnormality that may be present in cells with specialized functions. Drug-resistant Chinese hamster cells were characterized by overproduction of target enzyme, whereas human neuroblastoma cells had phenotypes of normal neuronal cells. Whether the HSR is transcriptionally active was not elucidated.
J Natl Cancer Inst 1976 Sep
PMID:A novel chromosome abnormality in human neuroblastoma and antifolate-resistant Chinese hamster cell lives in culture. 6 55

The purpose of this study was to explore a method by which an improved immunofluorescent staining can be applied to formalin-fixed paraffin sections to demonstrate cellular or tissue deposits of immunoglobulins, complement and fibrin, and to demonstrate alpha-1-antitrypsin storage and hepatitis B antigens in liver, toxoplasma in heart, and carcinoembryonic antigens in colonic cancer. It was shown that immunohistochemical demonstration for the above mentioned antigens, but not for complement, was feasible. The paraffin sections were first treated with trypsin and the indirect staining method was used. The trypsin treatment was found to decrease the nonspecific background fluorescence through digestion of the tissue. It probably also unmasked the immunoreactive sites of viral antigens and alpha-1-antitrypsin. In general, a 2-hour digestion was satisfactory for the types of tissues examined in this study, and an optimal period of digestion could be sought to obtain the best result for a specific antigen. This method may be a useful adjuvant to histopathologic study, in which a retrospective immunohistochemical examination may be desirable.
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PMID:Application of immunofluorescent staining on paraffin sections improved by trypsin digestion. 6 99

Ovarian carcinoma contains an antigen (TA) which is stable at 100 degrees. Rabbit antisera to glycoprotein-rich extracts of tumors detect TA in 70 per cent of ovarian malignancies, in some benign ovarian cysts, certain normal lung preparations, normal cervix, and squamous-cell carcinoma of the cervix. Highest levels may be associated with mucin secretion. No detectible antigen was present in normal ovary, plasma, A, B, and O erythrocytes, leukocytes, placenta, brain, heart, liver, corpus uteri, spleen, skeletal muscle, or kidney. Prolonged digestion of boiled tumor extracts with papain, trypsin, chymotrypsin, on Sephadex G-150 corresponding to a globular protein of 27,000 to 36,000 molecular weight. A beta-globulin mobility is seen in immunoelectrophoresis. It appears that TA differs in tissue specificity and molecular size from other known ovarian cancer associated antigens.
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PMID:A thermostable antigen associated with ovarian cancer. 6 15

In untreated patients with inoperable lung cancer, serum levels of alpha1-antitrypsin were found significantly increased in comparison to patients with non malignant diseases of the lung, alpha2-macroglobulin levels were unchanged in both groups of patients. There was also no difference in alpha2-macroglobulins in cancer patients reacting with DNCB and in non-reactors. Thus alpha2-macroglobulin levels do not seem to correlate with the immunestatus of cancer patients. Proteinase inhibitors are involved in a variety of biological processes including blood, clotting, digestion, and sperm capacitation. alpha1-antitrypsin, a alpha-globulin with a molecular weight of about 60,000 has been found to be decreased in patients' serum under several pathological conditions. A clear correlation exists between alpha1-antitrypsin deficiency and hereditary pulmonary emphysema (1, 2), respiratory distress syndrome (3), and juvenile cirrhoses of the liver (4). Elevated serum levels of alpha1-antitrypsin have also been found in some cancer cases. Thirty years ago a cancer test was developed on the basis of differences in the antiproteolytic activity in cancer patients' sera and in patients with other non-neoplastic diseases (5, 6). Several authors have tried to confirm these early data regarding specifity and sensitivity with respect to a screening test for cancer (7, 8). Methods of these authors were based mainly on enzyme substrate inhibition assays by addition of the patients' sera. Recently a commercially available test, based on immune-precipitation according to Mancini (9), has been developed (Behring-Werke, Partigen). By using this standardized method for determinating alpha1-antitrypsin, Harris et al. have recently demonstrated that patients with inoperable lung cancer have significantly elevated levels of this antiprotease in their sera (10), in comparison to patients with non malignant diseases of the lung. alpha2-macroglobulin is a serum protein with a molecular weight of 800,000 and with known antiprotease activity and can therefore bind trypsin, plasmin, elastase, and collagenase and it is known that alpha2-macroglobulin decreases with increasing of age. Changes of alpha-macroglobulin have also been observed in several pathological conditions (11). James et al. 4ave found decreases in serum of myeloma patients (12). An association between the development and function of lymphocytes and alpha2-macroglobulin has been suggested by several authors (13, 14). This alpha2-globulin has also been demonstrated on the surface of peripheral blood lymphocytes (15) and there is evidence that it is synthesized by lymphocytes (16). The purpose of the present study was to determine serum alpha1-antitrypsin levels in patients with inoperable lung cancer and to determine whether there is also an inverse correlation to alpha2-macroglobulin. It was further attempted to correlate alpha2-macroglobulin with general immunological parameters, as it is known that patients with lung cancer show a decreased general immune-reactivity (17).
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PMID:Serum levels of alpha1-antitrypsin and alpha2-macroglobulin in lung cancer. 6 86


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