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

Highly purified vesicular stomatitis virus (VSV) was obtained from VSV-infected SV40-transformed hamster cell lines. Immunization with this virus protected hamsters against challenge with SV40-transformed cells (TSV5-cl2). This protection was obtained regardless of the source of the SV40-transformed cells (e.g. cat, rat, hamster) used to produce VSV, and was therefore associated with the SV40 tumor-specific transplantation antigen (SV40-TSTA). Furthermore, when grown on spontaneously transformed cell lines or on cells transformed by a different oncogenic DNA virus, such as polyoma virus, the VSV failed to protect against the SV40-induced tumor. It was concluded that the SV40-TSTA activity of purified VSV is due to the incorporation of SV40-TSTA within the viral envelope. When VSV was treated with proteolytic enzymes (bromelain, trypsin) no loss of TSTA-induced tumor rejection was observed, although VSV had lost its ability to induce virus-neutralizing antibody. This clearly demonstrates that the TSTA activity is not related to the viral spikes. Phospholipase C suppressed the TSTA activity but neutralizing activity was still detectable in the anti-VSV sera. The results presented here demonstrate that the protection afforded by VSV is highly specific. It is particularly interesting that SV40-TSTA activity may be conveyed by the lipid core of the viral envelope.
Int J Cancer 1977 Jul 15
PMID:SV40 tumor rejection induced by vesicular stomatitis virus bearing SV40 tumor-specific transplantation antigen (SV40-TSTA). I. Specificity of immunoprotection and effect of enzyme treatment on TSTA activity. 7 Dec 74

Cytosol from human benign hyperplastic and carcinomatous prostatic tissue has been shown to contain a progestin receptor with a dissociation constant of approximately 10(-9) M. The receptor was measured using 3H-labeled R 5020 (17 alpha, 21-dimethyl-19-nor-4,9-pregnadiene-3,20-dione) as ligand. Progesterone, cyproterone acetate, and R 1881 (methyltrienolone) were efficient competitors to R 5020 for binding sites on the receptor whereas testosterone, 5 alpha--dihydrotestosterone, estradiol, cortisol, and several hydroxylated and saturated derivatives of progesterone did not compete. The [3H]R 2020-receptor-complex had a sedimentation coefficient of approximately 4 S, an isoelectric point of approximately 5, was heat-labile, and was destroyed by treatment with trypsin but not with deoxyribonuclease or ribonuclease. Seventeen of 21 patients with benign prostatic hyperplasia and three patients with prostatic carcinoma had 1 to 40 fmoles of specific R 5020-binding sites per mg of cytosol protein. One sample of normal prostatic tissue did not contain significant amounts of progesting receptor. Tissue specimens removed by transvesical adenoma enucleation displayed a larger number of specific R 5020-binding sites than electroresected specimens. The progestin receptor in hyperplastic prostate may be involved in the mechanism of the action of progestins used in the medical treatment of benign prostatic hyperplasia. Quantitation of progestin receptor in cancer of the prostate may form part of the basis of a predictive test program for endocrine therapy of prostatic malignancy.
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PMID:Demonstration of a progestin receptor in human benign prostatic hyperplasia and prostatic carcinoma. 7 18

The ratio of renal clearance of immunoreactive trypsin relative to renal clearance of creatinine was measured in 71 subjects including 27 controls and patients with cancer of pancreas, chronic pancreatitis, and acute pancreatitis. The upper limit of the control range was 4.1 x 10(-5) (mean + 2SD). 6 of 9 patients (67%) with acute pancreatitis had raised values. All 18 patients with chronic pancreatitis had values within the control range. In contrast, all 17 patients with carcinoma of pancreas had raised clearance ratios. The test may therefore prove valuable in distinguishing between chronic pancreatitis and cancer of pancreas.
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PMID:Urinary immunoreactive trypsin excretion: a non-invasive screening test for pancreatic cancer. 9 Sep 69

Biochemical characterization of serologically detected human melanoma antigens was undertaken for the development of immunodiagnostic assays in melanoma. An antiserum from a human melanoma patient, which detected melanoma antigens expressed on a large proportion of different melanoma cells, was used in leucocyte-dependent cytotoxic antibody (LDA) 51Cr-release assays to monitor the purification of melanoma antigens in urea/acetate extracts of lactoperoxidase 125I-labelled melanoma cell membranes. The separation procedures included affinity chromatography on Concanavalin A, gel filtration on porous polyacrylamide beads and preparative isoelectric focusing. The fractions were also monitored by polyacrylamide electrophoresis in sodium dodecyl sulphate and by measurement of beta 2 microglobulin and carcinoembryonic antigen content. The antigens detected by this antiserum appeared to be acidic (pI 3.5) low-mol.-wt glycoproteins of approximately 15,000 daltons which were resistant to heating at 56 degrees C and digestion with neuraminidase, but susceptible to repeated freeze-thawing and trypsin digestion. They did not appear to be related to HLA antigens, beta 2 microglobulin or known foetal antigens. The nature of the antigens detected in these studies is as yet unknown, but they appear similar to those described in the sera and urine of melanoma patients in previous reports. Thes combined results and the frequent expression of these antigens on melanoma cells from different patients suggest that assays to detect this antigen may provide a valuable immunodiagnostic aid in the management of melanoma.
Br J Cancer 1979 Oct
PMID:Detection of a low-molecular-weight antigen on melanoma cells by a human antiserum in leukocyte-dependent antibody assays. 9 79

Acid hydrolases (lysosomal enzymes) were analyzed and compared with trypsin in duodenal juice obtained after a test meal (Lundh test). The possible diagnostic role of acid hydrolases in pancreatic disease was investigated. In all patients with chronic pancreatitis normal values of acid hydrolases but subnormal trypsin activities were found. In pancreatic cancer normal values of acid hydrolases and normal trypsin values were seen in three patients with small tumors, whereas five patients with more advanced cancer of the pancreas had decreased trypsin activity and three of them high activities of acid hydrolases in duodenal juice. In five patients operated on with a gastroenteroanastomosis acid hydrolases were markedly increased. Five patients had no activity of acid hydrolases in the aspirate, probably reflecting technical failure with dislodgement of the catheter from the duodenum to the stomach. In conclusion the assay of acid hydrolases does not seem to increase the diagnostic value of the conventional Lundh test (trypsin).
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PMID:Intestinal lysosomal enzymes in the diagnosis of pancreatic disease. 11 5

The molecular weight fractions of 10,000-50,000 daltons prepared from "used" medium obtained during cultivation of human colon carcinoma cells (SW-48) in vitro inhibited the proliferation and DNA synthesis of these cells. Fractions exceeding 50,000 daltons were not inhibitory; those less than 10,000 daltons were cytotoxic. The inhibitory fraction did not affect either proliferation of human fibroblasts or transformation of human lymphocytes in vitro. Similar fractions from the colon mucosa of other species inhibited the proliferation of SW-48 cells, whereas extracts of dog jejunum or lung did not. This mitotic inhibition was completely reversible and could be destroyed by preincubation with trypsin. Therefore, colon cells appear to contain a cell- (but not species) specific, endogenous mitotic inhibitor or chalone.
J Natl Cancer Inst 1976 May
PMID:Evidence for a colon chalone. 13 20

Cancer-related urinary glycoprotein EDC1 inhibits the action of trypsin and chymotrypsin on casein and synthetic substrates. The amino acid and carbohydrate compositions of EDC1 are different from those reported for pregnancy-related urinary trypsin inhibitors.
Cancer Res 1978 Feb
PMID:Antitryptic property of cancer-related glycoprotein EDC1. 14 94

Several types of cultured cells release glycolytic enzymes into their suspending medium. This effect is most obvious with tumor cells, especially with their ascites forms. Erythrocytes do not release glycolytic enzymes. The total extracellular phosphoglucose isomerase activity consists of two components. One part is dissolved in the medium, the other one is sedimentable at 150 X g together with the cells. The latter seems to be localized at the cell surface. At densities of about 10(6) cells/ml maximum activity in the medium is reached within 5--10 min. After that no further release of enzyme activity can be observed. Serum reduces the rate of enzyme release considerably. This effect can be reversed by washing with protein free media. Treatment with trypsin leads to high extracellular phosphoglucose isomerase activities of the cells which originally show low external enzyme activity. Erythrocytes do not show any effect with trypsin, ascites tumor cells do not alter their high extracellular enzyme activity. At a density of 10(5) cells/ml, Yoshida acites tumor cells, cultured in vitro, release about 12% of originally intracellular phosphoglucose isomerase activity by 5 elutions with fresh medium. The process of enzyme release shows a certain selectivity in respect to different glycolytic enzymes. Aldolase exhibits the highest activity in the medium in relation to its homogenate activity.
Z Krebsforsch Klin Onkol Cancer Res Clin Oncol 1978 Oct 30
PMID:Release of glycolytic enzymes from cultivated tumor cells. 15 69

KCl extract from rat kidney, rat liver, and Morris hepatomas inhibited [3H]thymidine incorporation into cultured cells. Tissues came from male inbred BUF rats. The most pronounced inhibition was achieved with the kidney extract. Protein synthesis was not inhibited during a 24-hour exposure of the cells to the inhibitor. Incorporation of [3H]deoxycytidine was inhibited, as was cell growth, when the kidney KCl extract was present for several days. [3H]thymidine incorporation was inhibited almost immediately after the addition of the extract. The inhibition was reversible. Regular [3H]thymidine incorporation was restored 24 hours after removal of the inhibitor, which was neither arginase nor a thymidine-degrading enzyme. The inhibitor was stable to heat (80 degrees C for 10 min) and resistant to trypsin, pronase, DNase, and RNase. Exposure of the extract to proteolytic enzymes, hyaluronidase, and neuraminidase resulted in a loss of inhibitory activity only after extensive dialysis of the treated extract. The inhibitor appeared to be a mucoprotein in which the carbohydrate moiety may be responsible for the inhibition. The KCl extract also inhibited RNA synthesis and DNA synthesis by the de novo pathway. The inhibition of phosphorylation of thymidine, however, appeared to be the primary action of the inhibitor.
J Natl Cancer Inst 1979 Jun
PMID:Inhibition of tritiated thymidine incorporation in cultured cells by rat kidney extract. 15 53

BALB/c mouse 3T3 cells transformed by simian virus 40 (SV3T3), baby hamster kidney cells transformed by polyoma virus or Rous sarcoma virus, and a range of neoplastic human cell lines release material that inhibits the migration of macrophages and lymphocytes. Similar migration-inhibitory factor (MIF) activity was not detected in supernatants from cultures of untransformed 3T3 or baby hamster kidney cells and a variety of human diploid cell strains. Physico-chemical characterization of the MIF produced by SV3T3 and HeLa cells revealed substantial similarities with the MIF produced by mitogen-activated human peripheral lymphocytes. MIF released by tumor cells is inhibited by pancreatic and soybean trypsin inhibitors and by diisopropylfluorophosphate, indicating that it is a serine-protease. Comparison of MIF produced by SV3T3 cells with a serine-protease plasminogen activator released by the same cells indicated that the latter is more heat labile and has a more heterogenous elution profile after chromatography on Sephadex G-75. The possible role of MIF in causing proteolytic modification of the surface properties of tumor cells and in altering cell-mediated immune responses to neoplastic cells is discussed.
Cancer Res 1975 Sep
PMID:Production of a serine-protease with macrophage migration-inhibitory factor activity by virus-transformed cells and human tumor cell lines. 16 63


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