Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.22.54 (calpain 3)
 430 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have characterized a cytolytic T-cell clone, isolated from a A.TH anti-A.TL mixed lymphocyte culture, which recognized a private determinant of the I-Ak molecule. This specificity has been confirmed by inhibition of effector-target cell interaction by anti-I-Ak monoclonal antibody (mAb). Comparison of the inhibitory capacity of various mAb and the spatial arrangement of their epitopes (defined in previous studies by antibody-binding competition) indicated that the antigenic site recognized by this cytolytic T-cell clone was topologically related to one of the major polymorphic domains of the Ak molecule. This clone expressed the Thy-1.2+, Lyt-1.+, Lyt-1.2+low and I-As- cell surface phenotype. Testing of several rat mAb, screened for their ability to inhibit H-2K/D-specific cytolysis at the level of the effector cells, revealed that two anti-p94, 180 mAb but not various anti-Lyt-2 mAb inhibited the lytic function of this anti-I-Ak T-cell clone.
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PMID:Characterization of an Lyt-1+ cytolytic T-cell clone specific for a polymorphic domain of the I-Ak molecule. 618 58

The allospecific T cell recognition of the I-Ek molecule was assessed by using eight A. TH anti-A. TL proliferative T cell clones, all of which expressed the Thy-1-2+, Lyt-1+, Lyt-2-, Ia-, and p94,180+ cell surface phenotype. The use of panels of stimulating cells from homozygous of F1 hybrid strains indicated each T cell clone exhibited specificity for distinct alloactivating determinants including: i) a private E beta k-controlled determinant expressed in cis- or trans-complementing E beta kE alpha strains; ii) an apparently nonpolymorphic E alpha determinant resembling the serologic specificity Ia.7, i.e., present in all strains carrying E alpha and E beta expressor alleles; and iii) a series of conformational I-E determinants, the expression of which required a precisely defined combinatorial association of E beta plus E alpha chains. Two clones were found to be reactivated by cis- but not trans-complementing E beta k E alpha k strains, and another recognized an allodeterminant shared by the I-Ab molecule. Various I-Ek-reactive monoclonal antibodies (mAb) directed to epitopes presumably expressed on either E alpha (epitope clusters I and II) or E beta (epitope cluster III) chains inhibited the proliferative responses of seven clones recognizing private E beta k or unique E beta E alpha conformational activating determinants. By contrast, the restimulation of the clone directed to a nonpolymorphic E alpha determinant was selectively blocked by anti-Ia.7 mAb defining epitopes on the E alpha chains but not by those directed to the E beta chain. On the basis of these data, it was concluded that the recognition sites of most anti-I-Ek proliferative T cells were expressed on the E beta chain or the E beta plus E alpha interaction products, and that a minority of such alloreactive T cells could be activated through recognition of the E alpha chain per se.
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PMID:Clonal analysis of B and T cell responses to Ia antigens. IV. Proliferative T cell clones recognizing E beta and/or E alpha allodeterminants. 618 75

Avian infectious bronchitis virus (IBV) was grown and radiolabelled with 35S-methionine, 3H-leucine and 3H-glucosamine in de-embryonated chicken eggs. Approximately 12 different polypeptides were clearly detected by SDS-polyacrylamide gel electrophoresis of virus preparations. Growth of IBV in chorioallantoic membrane cells labelled with 35S-methionine indicated that most of these polypeptides, and additional ones, some of which were glycosylated, were host components. Five polypeptides appeared to be virus-coded, with apparent mol. wt. of 94 x 10(3), 84 x 10(3), 54 x 10(3), 30 x 10(3) and 28 x 10(3). Four of these, p94, p84, p30 and p28, were glycosylated. The virion spikes appeared to be composed of p94 and p84, while p30 and p28 were partially embedded in the virion membrane. By analogy with other reports, p54 is the nucleocapsid polypeptide.
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PMID:Structural polypeptides of coronavirus IBV. 626 43

Sera from (i) gnotobiotic BALB/c, CD-1, and CFW mice and (ii) conventional BALB/c mice were evaluated by radioimmunoassay, radioimmunoprecipitation, and plaque reduction neutralization, using the Wa, SA-11, and WC-3 (bovine) strains of rotavirus as the detecting antigens. The gnotobiotic mice had no antirotavirus antibody detectable by radioimmunoprecipitation and no neutralizing antibody at a dilution of 1:50 by plaque reduction neutralization. All sera from the conventional mice had rotavirus-specific antibodies detected by radioimmunoassay and by radioimmunoprecipitation at serum dilutions of 1:50 and 1:10,000, respectively. The antibodies were directed against viral proteins p116, p94, p88, and p84 of all three viruses, but had no neutralizing activity against heterologous rotaviruses at a dilution of 1:50. Conventional seropositive mice were parenterally immunized with the Wa, SA-11, or WC-3 strain of rotavirus. An approximate 100-fold increase in rotavirus-specific antibodies was detected by radioimmunoassay, and greater than 20-fold selective neutralization of the immunizing strain of virus was observed. Sera from the mice immunized with Wa virus had antibodies directed against inner and outer capsid proteins of all three rotaviruses. The mouse can be a useful model for studying the immune response to heterologous rotavirus infection; preexisting antibodies presumably directed towards murine rotavirus do not prevent the development of a type-specific immune response to a nonmurine rotavirus.
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PMID:Response of mice to rotaviruses of bovine or primate origin assessed by radioimmunoassay, radioimmunoprecipitation, and plaque reduction neutralization. 631 47

Changes in the expression of the genes encoding alpha-tubulin and a 94,000-dalton protein (p94) specified by a cDNA clone, p4-30, were examined in a differentiated teratocarcinoma-derived parietal endoderm cell line, PYS-2, and an undifferentiated teratocarcinoma stem cell line, F9. Relative to other proteins or mRNA species, the synthesis rate of the alpha-tubulins and of p94, as well as the levels of their corresponding cytoplasmic mRNAs, were lower in PYS-2 than in F9 cells. The decrease was greater for the relative abundance of cytoplasmic alpha-tubulin mRNA than for p94 mRNA. Similarly, induction of differentiation of F9 cells by simultaneous exposure to retinoic acid (RA) and dibutyryl cyclic AMP resulted in reduced relative levels of the cytoplasmic mRNAs for these proteins. The reduction in abundance of the two RNA species was not due to a decrease in growth rate since the differentiated cells, PYS-2, RA-treated F9, and RA plus dibutyryl cyclic AMP-treated F9 cells, grew at a rate similar to that of undifferentiated F9 cells. However, induction of differentiation of F9 cells by treatment with RA alone did not cause down-regulation of the two RNA species. The relative levels of total cellular RNA encoding alpha-tubulin and p94 in PYS-2 cells were also lower than those in F9 cells to an extent comparable to the decrease in the cytoplasmic RNAs. Since the apparent relative rates of RNA transcription were similar in both cell types, we conclude that the reduction in relative levels of the alpha-tubulin and p94 RNAs in the cell depends largely on the relative stability of the two RNAs and not on the relative rates of transcription. The faster disappearance of the two RNA species relative to other cellular RNAs from actinomycin D-treated PYS-2 compared with F9 cells is consistent with this interpretation.
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PMID:Post-transcriptional regulation of the abundance of mRNAs encoding alpha-tubulin and a 94,000-dalton protein in teratocarcinoma-derived stem cells versus differentiated cells. 651 23

One of the most important cytokines involved in immune response regulation is interleukin 2 (IL-2), a potent activator of the proliferation and function of T lymphocytes and natural killer cells. The mechanisms by which the effects of IL-2 are propagated within cells are not understood. While the binding of IL-2 to its receptor was recently shown to lead to the activation of two kinases, Jak-1 and Jak-3, subsequent steps in the signaling pathway to the nucleus that lead to the activation of specific genes had not been characterized. Since many cytokines that activate Jak kinases also lead to the tyrosine phosphorylation and activation of members of the Stat family of transcription factors, the ability of IL-2 to trigger Stat phosphorylation was examined. Exposure of activated human T lymphocytes or of a natural killer cell line (NKL) to IL-2 leads to the phosphorylation of Stat1 alpha, Stat1 beta, and Stat3, as well as of two Stat-related proteins, p94 and p95. p94 and p95 share homology with Stat1 at the phosphorylation site and in the Src homology 2 (SH2) domain, but otherwise are immunologically distinct from Stat1. These Stat proteins were found to translocate to the nucleus and to bind to a specific DNA sequence. These findings suggest a mechanism by which IL-2 binding to its receptor may activate specific genes involved in immune cell function.
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PMID:Interleukin 2 signaling involves the phosphorylation of Stat proteins. 754 1

Ovine progressive pneumonia virus (OPPV) was proliferated utilizing sheep foetal lung cells, and the cytopathic effect (CPE) of the virus was investigated. OPPV was purified with a 10%-sucrose cushion and then with 20%-55% discontinuous sucrose density gradient centrifugation. The structural proteins and antigen compositions of OPPV were analysed by SDS-PAGE and Western blotting. Besides, the OPP proviral cDNAs of the virus-infected cell cultures and the peripheral blood monocytes from sheep infected by the virus were detected using polymerase chain reaction (PCR). The results show that the CPE of sheep foetal lung cells infected by OPPV is typical of the disease. The purified virions are intact and of high purity when observed with an electron microscope. OPPV proteins consist of 18 polypeptide bands and the molecular weights range from 18 to 120 kd. Among these, 3 were glycoproteins (designated by gp120, gp50 and gp47). The appearance and peak time of the p28 antibody from sheep inoculated with OPPV are earlier than those of the p94 antibody to OPPV. Besides, the strength of immune reaction of p28 antibody is greater than that of p94 antibody. With PCR, it is demonstrated that the initial time for OPP proviral cDNAs to be integrated into the sheep foetal lung cells and the peripheral blood monocytes in sheep were 24 h and 9 d after inoculation, respectively.
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PMID:Analysis and PCR detection of antigen compositions of ovine progressive pneumonia virus. 762 98

Previous studies have led to the hypothesis of a possible role for m-calpain (EC 3.4.22.17) in myoblast fusion in culture in vitro. To support this hypothesis, an antisense strategy has been used with cultured primary rat myoblasts. Using an appropriate antisense oligodeoxyribonucleotide to m-calpain mRNA, an inhibition of myoblast fusion has been observed, the maximum being obtained when the cell culture was treated with 30 microM of oligomer. Synthesis of m-calpain was decreased by 48% while high concentrations of antisense oligonucleotide do not significantly affect myoblast proliferation. The specificity of m-calpain intervention during fusion has also been confirmed using antisense oligonucleotides to mu-calpain and p94 mRNAs, respectively.
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PMID:An antisense oligodeoxyribonucleotide to m-calpain mRNA inhibits myoblast fusion. 765 25

Our previous studies have demonstrated that, in addition to the conventional mu- and m-calpains ubiquitously expressed in tissues, a muscle-specific calpain comprising a novel member of the large subunit family (p94 or nCL-1, which stands for novel Calpain Large subunit) exists in muscle cells. To clarify the physiological function of nCL-1, we screened cDNA libraries of various rat tissues for other tissue-specific calpains and, as a result, discovered a novel member of the calpain large subunit family. RNA blot analysis showed that the mRNA is expressed predominantly in the stomach. Isolated cDNA clones could be structurally divided into two groups, whose 5'-halves of about 1.1 kilobase pairs were identical, but whose 3'-halves bore no similarity at all. This suggests generation by an alternative splicing mechanism, which was proved by genomic DNA cloning. Open reading frames were found encoding 703 and 381 amino acid residues with calculated molecular masses of 79,554 and 42,591 for nCL-2 and -2', respectively. The deduced amino acid sequence of nCL-2 is very similar to those of other calpain large subunits and can be aligned without significant insertions or deletions, suggesting that nCL-2 should possess cysteine protease activity and calcium binding ability. nCL-2' is identical to the N-terminal half of nCL-2 and, thus, contains only the cysteine protease domain but not the calcium binding domain. Possible roles of the calpain family are discussed based on these findings.
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PMID:A novel tissue-specific calpain species expressed predominantly in the stomach comprises two alternative splicing products with and without Ca(2+)-binding domain. 769 35

In the mammalian calpain system, two isozymes, mu- and m-types, have been well-characterized, and are considered to be conserved in the avian system as well. Thus, chicken calpain, whose large subunit was cloned in 1984, has long been regarded as 'm-type', since chicken also possesses 'mu-type' activity, although its structure has not yet been elucidated. In this study, we identified three kinds of cDNAs encoding distinct chicken calpain large subunits. Two of the three were highly similar to the mammalian mu-type and p94, respectively. The third shows a much higher similarity to mammalian m-type than the first identified chicken calpain, indicating that this molecule, which has been considered as 'm-type', should be renamed. We, therefore, designated it 'mu/m-calpain', because its sequence and Ca(2+)-sensitivity lie between mu- and m-types. Northern blot analyses revealed that chicken mCL and muCL, as well as mu/mCL, show ubiquitous expression, while p94 was detected predominantly in skeletal muscle, as previously reported. Chicken skeletal muscle, therefore, expresses at least four types of calpain, three ubiquitous and one tissue-specific.
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PMID:Identification of a third ubiquitous calpain species--chicken muscle expresses four distinct calpains. 774 67


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