Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibody (MAb) MUSE11 detects an adenocarcinoma-associated antigen and is useful for the serodiagnosis of pancreas cancer. We established a sandwich enzyme immunoassay using MAb MUSE11 and MAb DF3 against a breast cancer-associated mucin core protein as a catcher and a tracer, respectively. With this assay system, the binding of the tracer MAb DF3 to an antigen in the human kidney tissue lysate was clearly inhibited by MAb MUSE11. In addition, MAb MUSE11 showed a significant binding activity to the synthetic peptide corresponding to the tandem repeat of a human epithelial mucin core protein. These data suggest that MAb MUSE11 could detect the polypeptide core of a mucin, and may be of use for studying mucin as a gene product.
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PMID:Recognition of the polypeptide core of mucin by monoclonal antibody MUSE11 against an adenocarcinoma-associated antigen. 212 88

The human T lymphocyte Ag CD28 (Tp44) is a homodimeric glycoprotein expressed on the surface of a majority of human peripheral T cells and thymocytes. Although exposure of T cells to anti-CD28 mAb does not activate T cells, stimulation of CD28 can synergize with signals transmitted through the TCR or other stimuli to augment proliferation and lymphokine production. We have used a portion of the human CD28 cDNA to isolate a homologous murine cDNA from an EL4 T lymphoma library. The murine clone has 61% nucleotide identity with the human cDNA. Both human and murine sequences exhibit homology with members of the Ig supergene family and CTLA-4, a T cell specific murine gene. Many characteristics of the human CD28 molecule are conserved within the putative murine CD28 polypeptide. The murine cDNA sequence encodes a polypeptide of 218 amino acids that has 68% identity with the human sequence. Both the murine and human molecules are integral membrane glycoproteins with hydrophobic signal peptide sequences and transmembrane region. All five potential N-linked glycosylation sites are conserved and six of the seven cysteine residues of the mouse protein are found in the human CD28 polypeptide. The murine cDNA is encoded by a single copy nonrearranging gene whose expression at the mRNA level is restricted to T cells. A rabbit antiserum was raised against a synthetic peptide corresponding to a hydrophilic portion of the translated murine cDNA sequence. This antiserum identifies an 80-kDa homodimer consisting of disulfide-bonded subunits of 40 kDa that is expressed on splenic T cells, thymocytes, and several T cell tumors, but not on B cells. deglycosylation studies indicate that four of the five N-linked glycosylation sites are used and that the mature core protein has a molecular mass of 25 kDa, close to that predicted by the cDNA sequence. Transfection of the murine cDNA into Chinese hamster ovary cells resulted in the expression of an 80-kDa dimeric molecule that was immunoprecipitated by the antipeptide antiserum. Taken together, these data provide strong support that we have identified the murine homologue of CD28.
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PMID:The murine homologue of the T lymphocyte antigen CD28. Molecular cloning and cell surface expression. 215 64

Core protein II of mitochondrial cytochrome bc1 complex is the second largest nuclear-encoded subunit. We have isolated two overlapping cDNA clones encoding the precursor to this protein by screening a rat liver cDNA library, and determined the nucleotide sequence of the cDNAs. Based on the deduced amino acid sequence of the corresponding human precursor, the mature polypeptide of rat core protein II appears to consist of 438 amino acid residues with a molecular weight of 46,751, and to be formed as a precursor with an amino-terminal presequence. The mature form of the rat protein shows 83% and at most 24% homology with its human and yeast counterparts, respectively. Northern blot analysis showed that rat liver poly(A)+ RNA contains a single mRNA of approximately 2000 nucleotides for the core protein II.
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PMID:The primary structure of the precursor to core protein II, a putative member of mitochondrial processing protease family, of rat mitochondrial cytochrome bc1 complex deduced from cDNA sequence analysis. 216 68

The mouse lymph node specific homing receptor gp90MEL-14 is a 95-kDa molecular mass ubiquitinated cell surface molecule involved in the binding of lymphocytes to high endothelial venules in peripheral lymph nodes. The molecule is thought to consist of a core protein to which ubiquitin side chains are covalently bound. Recently we cloned the cDNA encoding the core protein; this cDNA clone encodes for a polypeptide with an estimated molecular mass of 37 kDa. We have studied the biosynthesis of gp90MEL-14 in an effort to explain the difference in molecular mass between the core protein and the 95-kDa mature molecule. Pulse labeling experiments show a rapid synthesis of a 70-kDa precursor form that contains high-mannose N-linked oligosaccharides. On processing of the high-mannose oligosaccharides into complex N-linked oligosaccharides, the precursor matures in a single step into the 95-kDa form. Experiments using deglycosylating enzymes and inhibitors of N-linked glycosylation demonstrate that the molecular mass of deglycosylated gp90MEL-14 is 45 kDa; extensive N-linked glycosylation is responsible for the difference in molecular mass with the mature 95-kDa form. The core protein molecular weight of in vitro transcribed and translated gp90MEL-14 cDNA is consistent with the estimated molecular mass of 37 kDa, calculated from the cDNA sequence of the core protein, and 8 to 10 kDa less than the protein molecular mass of gp90MEL-14 translated in vivo in the presence of tunicamycin (45 kDa). Inasmuch as we have ruled out glycosylation as accounting for this discrepancy, this is consistent with the addition of one ubiquitin moiety to the core protein during biosynthesis. Limited proteolysis confirms the similarity between in vitro transcribed gp90MEL-14 cDNA and the tunicamycin form of gp90MEL-14.
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PMID:Biosynthesis pathway of gp90MEL-14, the mouse lymph node-specific homing receptor. 216 61

The Ad2 proteinase, which is thought to be encoded by a 23-kDa open reading frame located at the end of the L3 family of late mRNAs, is expressed poorly even late after infection. To obtain sufficient proteinase for biochemical characterization, a DNA fragment containing the 23-kDa open reading frame was cloned into plasmids that permit efficient expression in Escherichia coli. Polyclonal antiserum specific for the Ad2 proteinase was produced by immunizing rabbits with a fusion protein that included the entire proteinase open reading frame, and this antiserum was used to show that the product of the 23-kDa reading frame is assembled into virions. Bacterial products corresponding to the complete 204 amino acid proteinase reading frame, to a 9 amino acid proteinase deletion, and to a proteinase fusion protein of 227 amino acids were used to determine the size of the proteinase polypeptide in Ad2 virions and in infected HeLa cell extracts. A single proteinase polypeptide that migrated during SDS-polyacrylamide gel electrophoresis with the 204 amino acid recombinant proteinase was detected in wild-type and H2ts1 virions, and in infected cell extracts. Immunoblot titrations showed that a wild-type Ad2 virus particle contains about 10 proteinase polypeptides; an H2ts1 virion has approximately fivefold less proteinase. In virions, the proteinase was associated primarily with the virus core. The 204 amino acid proteinase produced in E. coli permitted cleavage of the major core protein precursor, P-VII, to mature, authentic VII, but the proteinase deletion lacking 9 amino acids from near the amino-terminus was inactive. These results are inconsistent with autocatalytic processing of the Ad2 proteinase as was reported by Chatterjee and Flint (1987, Proc. Natl. Acad. Sci. USA 84, 714-718).
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PMID:The proteinase polypeptide of adenovirus serotype 2 virions. 219 98

A lambda gt11 cDNA library prepared from bovine submaxillary gland mRNA was screened with polyclonal anti-apo-bovine submaxillary mucin antibodies with the aim of obtaining the deduced amino acid sequence of the mucin core protein. One of the positive clones had a 1.8 kilobase (kb) cDNA insert and coded for an incomplete protein. A 2.0-kb cDNA clone was isolated by rescreening the library with the 1.8-kb cDNA. Nucleotide sequencing of the full-length 2.0-kb cDNA revealed an open reading frame that coded for a 563-amino acid protein. A striking feature of the cloned protein is the skewed distribution of the amino acids, most notably that of the hydroxy amino acids and cysteine. The amino-terminal domain of 339 residues is very rich in threonine, serine, and glycine and poor in cysteine, aspartic acid, tyrosine, phenylalanine, and tryptophan. In contrast, the carboxyl-terminal domain of 224 residues is rich in cysteine, aspartic acid, tyrosine, lysine, and asparagine and relatively poor in threonine, serine, and glycine. A search of the protein data bank for homologies to the deduced amino acid sequence revealed statistically significant matches to several proteins, including the porcine submaxillary apomucin fragment. The cysteine-rich domain by itself was not statistically homologous with any of the registered polypeptide sequences. RNA blot analysis using DNA probes corresponding to the mucin-like and cysteine-rich regions detected a nearly identical pattern of transcripts, demonstrating that the characterized clones are not artifacts of cDNA library construction. The blots also showed the presence of polydisperse transcripts in bovine submaxillary gland but no detectable hybridization signals in liver or brain RNA.
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PMID:Cloning and cDNA sequence of a bovine submaxillary gland mucin-like protein containing two distinct domains. 220 65

The primary structure of rice dwarf phytoreovirus (RDV) genome segment S3 was determined. RDV S3 consists of 3195 nucleotides. A 14-bp segment-specific inverted repeat is located immediately adjacent to the conserved terminal sequence (5'GGCAAA---UGAU3'). A single long open reading frame encoding for 1019 amino acids with an Mr of 114,289 is also identified. In order to investigate the localization of the predicted polypeptide, we determined the amino acid sequence of the 26-kDa peptide fragment obtained from the structural core protein digested by Staphylococcus aureus V8 protease. The sequence of the fragment was found in the translational product presumed from the nucleotide sequence of RDV S3, indicating that RDV S3 encodes the major structural core protein of 114 kDa.
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PMID:Sequence analysis of the rice dwarf phytoreovirus segment S3 transcript encoding for the major structural core protein of 114 kDa. 221 33

Chondrocytes, derived from a tissue that remains as permanent hyaline cartilage in vivo (embryonic chicken caudal sterna) were treated with 10(-8) to 10(-8) M 1,25-dihydroxyvitamin D3 [1,25(OH)2D3]. These nonadherent rounded chondrocytes acquired an adherent, polygonal morphology in a dose-dependent fashion with 1,25(OH)2D3 treatment. During the first 4 days of 1,25(OH)2D3 treatment cell flattening was associated with a 10-fold increase in beta-actin and fibronectin and their corresponding messenger RNAs (mRNAs). After adherence over the 12 days of continuous hormone treatment, a 2- to 4-fold increase in DNA synthesis and DNA accumulation were observed for the highest hormone dose (10(-8) M). Over the same time course total collagen synthesis decreased 35-50% primarily due to decreased type II collagen synthesis, which accompanied comparable decreases in its mRNA. In contrast, both alpha 1(I) and alpha 2(I) showed a continuous 5- to 10-fold increase; however, type I collagen protein synthesis remained undetectable, indicating translational control of the type I collagen synthesis. alpha 1(X) mRNAs showed a 2- 3-fold increase after 12 days of hormone treatment, and its polypeptide was clearly detected by sodium dodecyl sulfate polyacrylamide gel analysis. Type IX collagen synthesis showed a 2-fold increase in synthesis and its mRNA levels during the first 4 days of 1,25(OH)2D3 treatment but thereafter had levels comparable to control cultures. Analysis of proteoglycan synthesis and core protein mRNA levels showed there was a 2-fold increase in core protein mRNAs while proteoglycan synthesis, as assessed by 35S incorporation, showed only a 10-20% increase. Direct hormone effects vs. those secondary to altered cellular morphology were determined by blocking cell adherence by growth of the 1,25(OH)2D3-treated cultures on bacteriological petri dishes. All of the observed effects on cytoskeletal and collagen mRNAs were blocked except the elevations observed in proteoglycan core protein and alpha 1(IX) mRNAs. DNA contents in hormone-treated cultures also remained elevated. These results suggest that 1,25(OH)2D3 both activates and suppresses specific genes, promoting chondrocyte maturation toward a more hypertrophic phenotype. However, prevention of the initial morphological alterations that are induced by 1,25(OH)2D3 blocks many of the subsequent changes in connective tissue expression.
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PMID:Effect of 1,25-dihydroxyvitamin D3 on induction of chondrocyte maturation in culture: extracellular matrix gene expression and morphology. 230 21

The complete nucleotide sequence of segment 7 of the rice dwarf virus (RDV) genome was determined. The segment was 1696 bp long and its plus-strand terminal sequence, 5'GGCAAA---UGAU3', was in agreement with the consensus sequence previously found in other segments of RDV. A 10 bp inverted repeat was found adjacent to the termini. A single long open reading frame extended for 1518 bp from the first AUG triplet (positions 26 to 28), and encoded a polypeptide of 506 amino acids (Mr 55,339). This protein had 32% identity in the amino acid sequence to the 57K protein encoded by segment 7 of the wound tumour virus genome. The translation product of transcript RNA made from 'tailored' cDNA of RDV segment 7 comigrated with the 60K core protein of RDV in 10% polyacrylamide gel and reacted with antiserum against the 60K core protein of RDV. Segment 7 of the RDV genome therefore codes for the 60K core protein.
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PMID:Sequence analysis and product assignment of segment 7 of the rice dwarf virus genome. 231 70

Entomopoxviruses are a class of insect viruses whose virions are embedded in cytoplasmic occlusion bodies. The major component of these protective complexes is a protein called spheroidin. An open reading frame encoding the spheroidin gene of Choristoneura biennis entomopoxvirus has been identified and sequenced in our laboratory. This protein coding region is 1023 nucleotides long and specifies a polypeptide of 38,500 Da. Spheroidin was purified by SDS polyacrylamide gel electrophoresis, electroeluted, and its amino terminus sequence was determined on a gas phase sequencer. We observed that the first 20 N-terminal amino acids were absent in the mature processed form of the spheroidin molecule. Examination of these 20 residues revealed their hydrophobic nature and close resemblance to the consensus signal peptide sequence which is commonly found on membrane proteins. The DNA sequence of the spheroidin gene predicted a processed polypeptide with a molecular weight of 36 kDa. However, spheroidin was observed to aggregate in complexes composed of 50-kDa monomers. Intermolecular disulfide bonds were shown to play major roles in the formation and structure of these viral occlusion bodies. The difference in molecular weight between the predicted protein and its counterpart in infected cells is likely due to post-translational modifications. Indeed, two potential asparagine-linked glycosylation sites are present on the spheroidin molecule. The 5' flanking regions of the spheroidin gene and the vaccinia major core protein precursor gene P4b were shown to share substantial homology.
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PMID:Identification and sequencing of the spheroidin gene of Choristoneura biennis entomopoxvirus. 232 73


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