Regulation of the immune response to tumor antigens. II. The nature of immunosuppressor cells in tumor-bearing hosts.

Immunosuppressor (IS) cells were found to be generated in tumor-bearing animals (TBA) within 24 hr after inoculation of tumor cells of the methylcholanthrene-induced Sarcoma 1509a and appeared to persist in the hosts as long as the tumor was progressing. However, IS cells disappeared with 5 days after extirpation of the tumor. Increasing doses of thymus cells of TBA increased the degree of suppression of tumor rejection in immune syngeneic animals. Ten million thymus cells of TBA were capable of suppressing significantly the tumor rejection. The IS cells were detected in the thymus, spleens, and draining lymph nodes, as well as in bone marrow of TBA, but could not be detected in the peripheral circulating blood. Since immunosuppressive activity of bone marrow cells from TBA was entirely abolished by the in vitro treatment of the cells with anti-theta serum and complement, the observed immunosuppression appears to be mediated by the T cell population.     

Serotonin-sensitive aryl acylamidase in rat brain

Aryl acylamidase (E.C.3.5.1.13) was extracted from rat brain. The enzyme activity was inhibited by low concentrations of serotonin. The inhibition was non-competitive type and K_i value was about 3 × 10^?5M. Tryptamine inhibited the enzyme to a lesser extent. Other amines such as noradrenaline, tyramine and histamine did not affect the enzyme reaction. In contrast, aryl acylamidase from rat liver was insensitive to serotonin.     

Molecular cloning and characterization of a cDNA for a novel ethylene receptor, NT-ERS1, of tobacco (Nicotiana tabacum L.)

The cDNA encoding a novel member (NT-ERS1) of ethylene receptor family of tobacco (Nicotiana tabacum L.) was obtained by a combination of RT-PCR and 5'-/3'-RACE cloning. The cDNA was 2,092 nucleotides long and had an open reading frame of 1,911 bp encoding 637 amino acids. The deduced polypeptide lacked a response regulator domain, indicating that the ethylene receptor belongs to an ERS-group. The amino acid sequence was similar to respective members of the tobacco ethylene receptor family: 67.8% to NT-ETR1, 39.1% to NTHK1 and 31.1% to NTHK2. Comparison of amino acid sequence suggested that NT-ERS1 is the counterpart of Nr in the ethylene receptor family of tomato, which belongs to Solanaceae as does tobacco. Northern blot analysis showed that mRNA of NT-ERS1 was present in leaf, shoot and root tissues, and accumulated in leaves treated with exogenous ethylene. A mutated NT-ERS1 cDNA transgene, obtained by introducing one nucleotide substitution into NT-ETR1 cDNA, conferred ethylene insensitivity in tobacco plants, indicating that the translation product of the cDNA actually functioned in the plants.     

Rotation angle of stem cell division plane controls spiral phyllotaxis in mosses

Journal of Plant Research - The spiral arrangement (phyllotaxis) of leaves is a shared morphology in land plants, and exhibits diversity constrained to the Fibonacci sequence. Phyllotaxis in...     

Common and Distinct Clinical Features in Adult Patients with Anti-Aminoacyl-tRNA Synthetase Antibodies: Heterogeneity within the Syndrome

Objective

To identify similarities and differences in the clinical features of adult Japanese patients with individual anti-aminoacyl-tRNA synthetase antibodies (anti-ARS Abs).

Methods

This was a retrospective analysis of 166 adult Japanese patients with anti-ARS Abs detected by immunoprecipitation assays. These patients had visited Kanazawa University Hospital or collaborating medical centers from 2003 to 2009.

Results

Anti-ARS Ab specificity included anti-Jo-1 (36%), anti-EJ (23%), anti-PL-7 (18%), anti-PL-12 (11%), anti-KS (8%), and anti-OJ (5%). These anti-ARS Abs were mutually exclusive, except for one serum Ab that had both anti-PL-7 and PL-12 reactivity. Myositis was closely associated with anti-Jo-1, anti-EJ, and anti-PL-7, while interstitial lung disease (ILD) was correlated with all 6 anti-ARS Abs. Dermatomyositis (DM)-specific skin manifestations (heliotrope rash and Gottron’s sign) were frequently observed in patients with anti-Jo-1, anti-EJ, anti-PL-7, and anti-PL-12. Therefore, most clinical diagnoses were polymyositis or DM for anti-Jo-1, anti-EJ, and anti-PL-7; clinically amyopathic DM or ILD for anti-PL-12; and ILD for anti-KS and anti-OJ. Patients with anti-Jo-1, anti-EJ, and anti-PL-7 developed myositis later if they had ILD alone at the time of disease onset, and most patients with anti-ARS Abs eventually developed ILD if they did not have ILD at disease onset.

Conclusion

Patients with anti-ARS Abs are relatively homogeneous. However, the distribution and timing of myositis, ILD, and rashes differ among patients with individual anti-ARS Abs. Thus, identification of individual anti-ARS Abs is beneficial to define this rather homogeneous subset and to predict clinical outcomes within the “anti-synthetase syndrome.”     

Capsaicin Modifies Responses of Rat Chorda Tympani Nerve Fibers to NaCl

Single-fiber preparations of the rat chorda tympani (CT) nervewere used to study the mechanism of action of capsaicin on salt-tastetransduction. Capsaicin selectively suppressed the responsesto NaCl of the CT nerve fibers (N-fibers) that are sodium-specific(insensitive or poorly sensitive to potassium). Among the morebroadly responsive, cation-sensitive fibers (E-fibers) thereare two subtypes, both of which responded to capsaicin but indifferent ways (‘enhanced’ type and ‘suppressed’type). In both N- and E-fibers, 5% ethanol (the vehicle forcapsaicin) slightly reduced the response to 100 mM NaCl. Thesuppressive effect of capsaicin on the response of the N-typefibers to 100 mM NaCl was significantly stronger than the effectof 5% ethanol. The suppression lasted for at least 20 s afterthe simultaneous application of 100 p.p.m. capsaicin-100 mMNaCl. These results indicate that 100 p.p.m. capsaicin can modifythe response of CT fibers to NaCl. The observed effect of capsaicinon gustatory fibers could be the net result of opposite suppressiveand enhancing processes in the taste buds cells and excitedintra- or extragemmal trigeminal nerve endings. Chem. Senses22: 249–255, 1997. ^*These authors contributed equally to this study     

Mixed cell agglutination reaction of ABO substances in the saliva and determination of human-type ABO blood groups in the cynomolgus monkey.

For detection of ABO substances in the saliva of the cynomolgus monkey, the mixed cell agglutination reaction (MCAR) gave specific and clear results with a very small amount of saliva. Anti-A and anti-B antibodies in the sera of the same species showed the clearest hemagglutination by the saline agglutination method. The combined use of both methods was demonstrated to be easily and accurately applicable to the determination of human-type ABO blood groups of the cynomolgus monkey.     

Regulation by thyrotropin-releasing hormone (TRH) of TRH receptor mRNA degradation in rat pituitary GH3 cells.

In rat pituitary GH3 cells, thyrotropin-releasing hormone (TRH) down-regulates TRH receptor (TRH-R) mRNA (Fujimoto, J., Straub, R.E., and Gershengorn, M.C. (1991) Mol. Endocrinol. 5, 1527-1532), at least in part, by stimulating its degradation (Fujimoto, J., Narayanan, C.S., Benjamin, J.E., Heinflink, M., and Gershengorn, M.C. (1992) Endocrinology 130, 1879-1884). Here we show that TRH regulates RNase activity in GH3 cells and that specific mRNA sequences are needed for in vivo regulation of TRH-R mRNA by TRH. TRH affected RNase activity in a biphasic manner with rapid stimulation (by 10 min) followed by a decrease to a rate slower than in control lysates within 6 h. This time course paralleled the effects of TRH on degradation of TRH-R mRNA in vivo. The regulated RNase activity was in a polysome-free fraction of the lysates and was not specific for TRH-R RNA. A truncated form of TRH-R RNA that was missing the entire 3'-untranslated region (TRHR-R5) was more stable than full-length TRH-R RNA (TRHR-WT). In contrast to TRHR-WT mRNA, TRHR-R5 mRNA and TRHR-D9 mRNA, which was missing the 143 nucleotides 5' of the poly(A) tail, were not down-regulated by TRH in stably transfected GH3 cells as their rates of degradation were not increased. These data show that TRH regulates RNase activity in GH3 cells, that the 3'-untranslated region bestows decreased stability on TRH-R mRNA and that the 3' end of the mRNA is necessary for regulation by TRH of TRH-R mRNA degradation. We present an hypothesis that explains specific regulation of TRH-R mRNA degradation by TRH in GH3 pituitary cells.