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

Cloned human CD4+ T cell lines specific for the house dust mite Dermatophagoides pteronyssinus were used to map minimal T cell activation-inducing epitopes on the Group I allergen in D. pteronyssinus extracts (Der p I) molecule. Most of these Der p I-specific T cell clones expressed different TCR V alpha and V beta gene products. Using recombinant deletion proteins, three T cell epitopes were identified on the Der p I molecule; p45-67 and p117-143 were recognized by HLA-DR7-restricted T cells, whereas p94-104 was recognized in the context of HLA-DR2, DRw11 (DR5), and -DR8 molecules. This degenerate class II MHC restriction appears to be due to shared Phe and Asp residues at positions 67 and 70, respectively, in the third variable domain of the HLA-DR beta chain. All three T cell epitopes induced Th2-like cytokine production profiles by the Der p I-specific T cell clones, which were characterized by the production of very high levels of IL-4 and IL-5, as compared with those secreted by tetanus toxin-specific T cell clones derived from the same patients, but no or low amounts of IL-2 and IFN-gamma. This Th2-like production profile was, however, not an intrinsic property of the Der p I-specific T cells, but was dependent upon their mode of activation. Stimulation with Con A also induced very low or no measurable levels of IL-2 and IFN-gamma, whereas activation with TPA and the calcium ionophore A23187 resulted in the production of high levels of IL-4, IL-5, IL-2, and IFN-gamma. These results indicate that Der p I-specific T cell clones are not defective in their capacity to produce high levels of Th1 cytokines.
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PMID:T cell activation-inducing epitopes of the house dust mite allergen Der p I. Proliferation and lymphokine production patterns by Der p I-specific CD4+ T cell clones. 137 May 14

While conventional calpains, m- and mu-calpains named according to their calcium-dependence, are expressed in almost every tissues, mRNA of newly identified p94, which has a significant sequence similarity to the conventional calpain large subunits, is abundantly expressed only in skeletal muscle. In addition to this specific expression, p94 is distinct from conventional calpains in that it contains three unique regions showing no similarity to conventional calpain subunits. When rat and human p94 are compared, overall sequence similarity is 94.0%, which is close to those for m- and mu-calpain large subunits; 93.1% and 95.4% between human and rabbit, respectively, suggesting the evolutionary importance of p94. These calpain large subunit proteins, p94, m- and mu-types, can be considered to constitute a super family, whose p94, m- and mu-types represent the three major types. Sequences of the calpain large-subunit family members, including the recently reported Schistosoma calpain, are compared. Their evolutionary correlation and function are discussed on the basis of the results thus far obtained.
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PMID:Sequence comparison among muscle-specific calpain, p94, and calpain subunits. 142 Mar 33

Recently there have been reports on high-molecular mass components of Borrelia burgdorferi, namely the p100, p94 and p83, which claimed these proteins to be specific marker antigens for the serodiagnosis of late Lyme borreliosis. The nucleotide sequences of the p100 and p83 have been published. The alignment of the deduced N-terminal amino acid sequences with the N-terminal sequence of the p94 now provides evidence that all three proteins are identical.
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PMID:Evidence that Borrelia burgdorferi immunodominant proteins p100, p94 and p83 are identical. 142 83

Fractionation of a cytosolic extract of HeLa cells revealed the existence of a highly active protein tyrosine kinase. Chromatographic fractionation of the extract resulted in partial purification of a single enzymatic activity that coeluted with a 94-kDa polypeptide. In vitro phosphorylation of the isolated enzyme showed that p94 was the only polypeptide phosphorylated and only the tyrosine residue(s) was (were) modified. The fractionated enzyme (p94 kinase) also phosphorylated a number of other nonspecific substrates exclusively on tyrosine residues. Unlike other protein tyrosine kinases that have been characterized, p94 kinase is relatively insensitive to inhibition by the isoflavone genistein. Using two different antisera, we provided evidence that the HeLa p94 kinase is most likely the FER gene product, which was previously shown to be expressed in a wide variety of cell types. These results represent the first biochemical characterization of the cellular FER gene product and also provide a basis for studying the biochemistry of tyrosine kinase function in HeLa cells.
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PMID:Identification and characterization of a cytosolic protein tyrosine kinase of HeLa cells. 155 92

The RNA of densonucleosis virus type 1 (GmDNV), isolated from GmDNV-infected Galleria mellonella larvae, was shown by Northern blotting to contain five polyadenylated, viral-specific RNA species with sizes of 1.8, 2.4, 3.5, 4.0, and 5.0 kb. Poly(A)-containing RNA from whole larvae and hybrid-selected viral RNA were translated in a rabbit reticulocyte lysate system and the translation products were coelectrophoresed with proteins extracted from CsCl-purified virus. All four virion-associated proteins, namely p49, p55, p65, and p94, were present in the in vitro-translated products. However, in the majority of the experiments the most abundant translation product was a 30K polypeptide which is absent from virion extracts. The most abundant viral protein is p49, and the 49K polypeptide was also the most abundant translation product in about 30% of the preparations. The 1.8 kb transcript, which constitutes about half of the total viral RNA, is only slightly larger than the template required for a 30K polypeptide, suggesting that the latter may be a primary translation product of the smallest RNA transcript. The similarities in gene expression between densoviruses and mam malian parvoviruses are discussed.
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PMID:Expression of densonucleosis virus GmDNV in Galleria mellonella larvae: size analysis and in vitro translation of viral transcription products. 227 84

In the course of cDNA cloning of the large subunits of human mu- and mCANPs, a novel cDNA clone encoding a putative calcium-dependent cysteine protease homologous to but distinct from both mu- and m-types was found. The encoded protein, designated tentatively as p94, is composed of four domains similar to those found in other CANP large subunits, but includes three unique regions that have no homology to other CANPs. These unique sequences might be involved in regulating the activation and/or determining the intracellular localization of p94. Since the mRNA for p94 is five times more abundant than that for the CANP small subunit in skeletal muscle, it is possible that p94 does not associate with the small subunit in vivo. In contrast to the ubiquitous expression of mu- and m-types, the mRNA for p94 is expressed only in skeletal muscle. Besides acting as a protease, p94 may act as a skeletal muscle specific regulatory protein like troponin C.
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PMID:A novel member of the calcium-dependent cysteine protease family. 240 May 79

Hepatitis B surface antigen (HBsAg) particles are composed of a major polypeptide, p25, and additional polypeptides of higher m.w., namely p33 and p39, are variably present. All three polypeptides share the 226 amino acid residues of the S region: p33 consists of the p25 sequence plus an NH2-terminal 55 residues (pre-S(2], and p39 consists of the p33 sequence plus an NH2-terminal 108-119 residues (pre-S(1). In previous studies we demonstrated the influence of two Ir genes on the humoral and cellular immune responses to the S region and identified nonresponder phenotypes (H-2f,s). Subsequent studies showed that the immune response to the pre-S(2) region was regulated by H-2-linked genes independently of the S region response, such that immunization of S region nonresponder, pre-(S2) region responder mice (H-2s) with HBsAg/p33 circumvented nonresponse to the S region. In the present study, we have extended this analysis to the pre-S(1) region of HBsAg, with the following results: 1) and pre-S(1) region is immunogenic at the T and B cell levels; 2) anti-pre-S(1) specific antibody production is regulated by H-2-linked genes and can be independent of anti-S and anti-pre-S(2) antibody production; 3) immunization of H-2f strains with HBsAg/p39 particles containing the pre-S(1) region can bypass nonresponsiveness to the S and pre-S(2) regions in terms of antibody production; 4) two synthetic peptides, p32-53 and p94-117, define murine and human antibody binding sites on the pre-S(1) region, and p1-21 and p12-32 define additional human antibody binding sites; 5) pre-S(1)-specific T cells can be elicited in S and pre-S(2) region nonresponder mice (H-2f) and provide functional T cell help for S-pre-S(2)-, and pre-S(1)-specific antibody production; and 6) a T cell recognition site in the pre-S(1) region, p12-32 was identified. These results are relevant to HBV vaccine development, and possibly to viral clearance mechanisms, since the higher m.w. polypeptides are preferentially expressed on intact virions.
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PMID:Immune response to the pre-S(1) region of the hepatitis B surface antigen (HBsAg): a pre-S(1)-specific T cell response can bypass nonresponsiveness to the pre-S(2) and S regions of HBsAg. 242 7

The purpose of this study was to identify and characterize T cell and B cell recognition sites within the pre-S(1) region of HBsAg/p43, and to then analyze functional T cell-B cell interactions at the level of in vivo antibody production. The results indicate: three peptide sequences within the pre-S(1) region of HBsAg were identified which can induce and elicit HBsAg/p43-specific T cell proliferation; a 10-amino acid peptide, p12-21, defines one pre-S(1)-specific T cell recognition site, and residues 18 and 19 are critical to the recognition process; the p12-21 sequence can function as a T cell carrier for a synthetic B cell epitope within the pre-S(2) region; the p94-117 sequence contains at least two T cell recognition sites; five distinct, pre-S(1)-specific antibody binding sites were identified; synthetic pre-S(1) region T cell determinants can prime in vivo antibody production to multiple B cell epitopes within the pre-S(2) and S regions, as well as within the pre-S(1) region; the specificity of the primed T cell population can influence the specificity of the B cell response; and T cell recognition of pre-S(1) region peptides is regulated by H-2-linked genes.
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PMID:A single 10-residue pre-S(1) peptide can prime T cell help for antibody production to multiple epitopes within the pre-S(1), pre-S(2), and S regions of HBsAg. 243 44

Two types of calcium-dependent protease with distinct calcium requirements (termed muCANP and mCANP) are known in mammalian tissues. These two isozymes consist of different large (80-kDa) subunits (mu- or m-types) and identical small (30-kDa) subunits. By screening human and rat muscle cDNA libraries with a cDNA probe for the chicken CANP large subunit, which has a structure similar to both the mammalian mu- and m-types, a cDNA clone encoding a novel member of the CANP large subunit family was obtained. The encoded protein (designated "p94") consists of 821 amino acid residues (Mr 94,084) and shows significant sequence homology with both human mu-type (54%) and m-type (51%) large subunits. p94 can be divided into four domains (I-IV) as reported for the CANP large subunit family. Domains II and IV are potential cysteine protease and calcium-binding domains, respectively, and have sequences homologous to the corresponding domains of other CANP large subunits. However, domain I of p94 is significantly different from others. Moreover, p94 contains two unique sequences of 62 and 77 residues in domains II and III, respectively. In contrast to the ubiquitous expression of mu- and m-types, Northern blot analysis revealed that the mRNA for p94 exists only in skeletal muscle with none detected in other tissues including heart muscle and smooth muscles such as intestine.
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PMID:Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. 255 41

The immunohistochemical localization of melanoma-associated antigen p94 kd200 was investigated in frozen sections of 3 congenital nevi, 4 benign intradermal nevi, 1 regressing nevus, 1 blue nevus, 1 dysplastic nevus, 1 lentigo maligna, 1 superficial spreading melanoma and 2 metastatic melanomas. The original avidin-biotin complex lectin method (Hsu SM, Raine L, Fanger H: Am. J. Clin. Pathol., 75: 734-738, 1981) was modified to detect the antigen. The sections were exposed to the monoclonal antibody to p94 kd200 (Hybritech Inc.), the linking biotin-labelled anti-mouse IgG, the avidin-biotin peroxidase complex and the 3-amino-9-ethylcarbazole solution in an incubator at 37 degrees C and 100% humidity. We found that the percentage of cells expressing p94 kd200 varied between 0 and 100% in congenital nevi, between 80 and 100% in benign intradermal nevi, between 0 and 20% in the regressing, blue and dysplastic nevi, and in the lentigo maligna, 80 to 100% in the superficial spreading melanoma, and between 0 and 40% in the metastatic melanomas. Positive cells were found to be hypomelanotic (did not have heavy melanin content). The intensity of labelling or the degree of antigen expression on benign and malignant hypomelanotic cells was also found to vary. These findings 1) reinforce the concept of quantitative rather than qualitative antigenic differences in benign and malignant cells 2) suggest that kd200 is lost with increasing pigment production 3) offer a potentially significant tool to investigate the antigenic changes during cell differentiation.
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PMID:Immunohistochemical localization of melanoma-associated antigen p94 kd200 with the use of a modified avidin-biotin-complex lectin method. 331 50


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