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)

Regional (popliteal) lymph node cells (RLNC) from A/Jax mice, inoculated in each hind foot with isogeneic Sarcoma 1 tumor cells, demonstrated cytotoxicity in vitro at Day 14 of tumor growth but lost this ability by Day 21. These noncytotoxic RLNC were capable of suppressing activity of other cytotoxic lymphoid cells, but after incubation for 24 hr in vitro their cytotoxicity was restored and their suppressive activity was abrogated. RLNC responsible for cytotoxicity were removed by treatment with anti-theta serum plus complement. The suppressive effect of RLNC was found to be mediated by a soluble "blocking" factor which was released into the culture medium after 24 hr incubation. The factor was not detected in culture media from RLNC pretreated with anti-theta serum plus complement prior to incubation. Absorption of RLNC culture supernatants with tumor-bearer spleen cells, but not with normal spleen cells, completely removed the blocking factor, while absorption by Sarcoma 1 cells significantly reduced blocking activity. The factor was trypsin sensitive, was retained on an Amicon XM100 filter, and did not demonstrate the presence of antibody to Sarcoma 1 in a radioimmunoassay. Although the exact nature of the factor has not been established, it appears to be a receptor antigen complex from T-cells of tumor-bearing animals.
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PMID:Immunological activity of regional lymph nodes in tumor-bearing mice. 31 91

Sarcoma-180 tumor cells in culture or grown as an ascites form in the CD-1 mouse have been subjected to mild trypsinization procedures in order to study morphological and molecular changes resulting from proteolysis. The cells attached to a substratum become rounded within 20 min. and most undergo cell division, but they do not detach from the substratum. Removal of trypsin permits the cells to go back to their original spindle shape over an 8-20 h period. Surface membranes were isolated from trypsinized ascites and cultured cells and subjected to dodecyl sulfate-acrylamide gel electrophoresis. Both cell types showed the same two kinds of changes in electrophoretic patterns. First, there was a loss of glycoproteins from both cell types even though they show different complements of cell surface glycoproteins. Second, there is a loss of high molecular weight polypeptides, which have previously been suggested to play a role in membrane stabilization and cell shape. These results further implicate these polypeptides in the control of cell morphology and offer circumstanital evidence for transmembrane interactions of surface glycoproteins with the high molecular weight polypeptides as a factor in controlling cell morphology.
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PMID:Molecular changes in cell surface membranes resulting from trypsinization of sarcoma 180 tumor cells. 125 87

Antineoplastic effects of carnosine (CAR) and beta-alanine (ALA), were examined in vivo using ddY mice implanted with the solid tumor Sarcoma-180. The sarcoma was treated with trypsin, 10(5) cells were implanted subcutaneously in the back of the animals, and CAR and ALA were administered subcutaneously 2 cm from the implantation site starting on the next day. The animals treated with ALA alone showed prolongation of survival to a T/C value of 132%; the growth of the tumor was inhibited and mortality reduced in those treated with CAR alone. Regression of the tumor was observed in the animals treated with either drug. The effects of these agents were enhanced when administered in combination with the non-specific active immuno-enhancing agent OK-432. More than half the animals treated with CAR and OK-432 survived the observation period (T/C greater than 218%), and survival was prolonged in those treated with ALA and OK-432 to a T/C value of 132%. The agents also showed potent antineoplastic effects on Sarcoma-180 when the tumor had been attenuated in vivo with mitomycin C (MMC).
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PMID:[Antineoplastic effects of carnosine and beta-alanine--physiological considerations of its antineoplastic effects]. 310 21

Sarcoma virus transformed rat kidney cells, NRK[MSV-MLV] cells, and their non-transformed counterparts, NRK cells, were repeatedly subcultured in medium supplemented with 1 mM 2-deoxy-D-glucose (dGlc). These dGlc-grown cells exhibited alterations in glycosylation of surface proteins. Gel filtration analyses of pronase-treated, trypsin-sensitive, surface fucopeptides indicated a reduction in the average size of the fucopeptides from both dGlc-grown NRK and NRK[MSV-MLV] cells. When the cells were grown in control medium the fucopeptides from the NRK[MSV-MLV] cells were larger than those from NRK cells, i.e. the fucopeptide difference observed in a wide range of transformed versus normal cells. The changes in the fucopeptides of dGlc-grown cells were greater for the NRK cells so that after growth in dGlc-supplemented medium there was an enhancement in the typical fucopeptide differences between normal and transformed cells, namely a larger difference in both size distribution and degree of sialylation. These dGlc-related alterations were readily reversed when the cells were transferred to control medium. The changes in glycosylation were compatible with continued cell replication although there was an increase in doubling time of the dGlc-grown cells, 6-7 h increase for NRK cells, 1-2 h increase for NRK[MSV-MLV] cells.
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PMID:Differential effects of 2-deoxy-D-glucose on surface glycoproteins of normal and transformed cells. 630 66

The multifunctional Ewing Sarcoma (EWS) protein, a member of a large family of RNA-binding proteins, is extensively asymmetrically dimethylated at arginine residues within RGG consensus sequences. Using recombinant proteins we examined whether type I protein arginine methyltransferase (PRMT)1 or 3 is responsible for asymmetric dimethylations of the EWS protein. After in vitro methylation of the EWS protein by GST-PRMT1, we identified 27 dimethylated arginine residues out of 30 potential methylation sites by mass spectrometry-based techniques (MALDI-TOF MS and MS/MS). Thus, PRMT1 recognizes most if not all methylation sites of the EWS protein. With GST-PRMT3, however, only nine dimethylated arginines, located mainly in the C-terminal region of EWS protein, could be assigned, indicating that structural determinants prevent complete methylation. In contrary to previous reports this study also revealed that trypsin is able to cleave after methylated arginines. Pull-down experiments showed that endogenous EWS protein binds efficiently to GST-PRMT1 but less to GST-PRMT3, which is in accordance to the in vitro methylation results. Furthermore, methylation of a peptide containing different methylation sites revealed differences in the site selectivity as well as in the kinetic properties of GST-PRMT1 and GST-PRMT3. Kinetic differences due to an inhibition effect of the methylation inhibitor S-adenosyl-L-homocysteine could be excluded by determining the corresponding K(i) values of the two enzymes and the K(d) values for the methyl donor S-adenosyl-L-methionine. The study demonstrates the strength of MS-based methods for a qualitative and quantitative analysis of enzymic arginine methylation, a posttranslational modification that becomes more and more the object of investigations.
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PMID:Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide. 1604 63