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)

A cDNA encoding the human homolog of mouse T-cell and mast cell growth factor P40 was derived from peripheral blood mononuclear cells (PBMC) stimulated with phytohemagglutinin and phorbol myristate acetate. Sequence analysis of the cDNA predicted a precursor protein of 144 amino acids including a signal peptide of 18 residues, a structure identical with that of mouse P40. The homology between the mouse and human proteins is 55% with a perfect conservation of the 10 cysteine residues present in the mature polypeptide. Expression of the cDNA for human P40 in a baculovirus vector yielded a protein capable of enhancing in vitro survival of human T cell lines.
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PMID:Cloning and expression of a cDNA for the human homolog of mouse T cell and mast cell growth factor P40. 212 1

We have previously reconstituted the soluble phase of precursor protein translocation in vitro using purified proteins (the precursor proOmpA, the chaperone SecB, and the ATPase SecA) in addition to isolated inner membrane vesicles. We now report the isolation of the SecY/E protein, the integral membrane protein component of the E. coli preprotein translocase. The SecY/E protein, reconstituted into proteoliposomes, acts together with SecA protein to support translocation of proOmpA, the precursor form of outer membrane protein A. This translocation requires ATP and is strongly stimulated by the protonmotive force. The initial rates and the extents of translocation into either native membrane vesicles or proteoliposomes with pure SecY/E are comparable. The SecY/E protein consists of SecY, SecE, and an additional polypeptide. Antiserum against SecY immunoprecipitates all three components of the SecY/E protein.
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PMID:The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. 216 76

Arginine decarboxylase is the first enzyme in one of the two pathways of putrescine synthesis in plants. We purified arginine decarboxylase from oat leaves, obtained N-terminal amino acid sequence, and then used this information to isolate a cDNA encoding oat arginine decarboxylase. Comparison of the derived amino acid sequence with that of the arginine decarboxylase gene from Escherichia coli reveals several regions of sequence similarity which may play a role in enzyme function. The open reading frame (ORF) in the oat cDNA encodes a 66 kDa protein, but the arginine decarboxylase polypeptide that we purified has an apparent molecular weight of 24 kDa and is encoded in the carboxyl-terminal region of the ORF. A portion of the cDNA encoding this region was expressed in E. coli, and a polyclonal antibody was developed against the expressed polypeptide. The antibody detects 34 kDa and 24 kDa polypeptides on Western blots of oat leaf samples. Maturation of arginine decarboxylase in oats appears to include processing of a precursor protein.
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PMID:Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing. 226 46

The cDNA sequence of the large dsRNA segment (segment A) of the N1 strain of infectious pancreatic necrosis virus (IPNV) has been determined. The nucleotide and deduced amino acid sequences were compared to the sequences of segment A of the Jasper strain of IPNV and to the sequences of segments A and B (5' and 3' flanking regions) of the 002-73 strain of infectious bursal disease virus (IBDV). The comparison demonstrated that the precursor protein of the major structural polypeptide, pVP2, is highly conserved at the N and C termini, whereas the amino acid sequence of an internal segment shows greater diversity between the strains. This internal segment probably carries the serotype-specific epitopes of birnaviruses. An alternative open reading frame (ORF) (444 bp) partly overlapping with the large ORF (2916 bp) of segment A was found to be conserved among the IPNV strains and is probably also present in the 002-73 strain of IBDV. This small ORF may encode a novel birnavirus polypeptide with an Mr of 17K. SDS-PAGE of radiolabelled purified IPNV particles revealed a band corresponding to the possible novel 17K polypeptide. Short terminal inverted repeats are found in segment A of the N1 and Jasper strains of IPNV and in segment B of the 002-73 strain of IBDV. Segment A of IPNV and segment B of IBDV also contain adjacent inverted repeats at their 5'-terminal flanking regions.
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PMID:Sequence of the large double-stranded RNA segment of the N1 strain of infectious pancreatic necrosis virus: a comparison with other Birnaviridae. 230 63

The precursor protein of von Willebrand factor (pro-vWF) consist of four repeated domains, denoted D1-D2-D'-D3-A1-A2-A3-D4-B1-B2-B3-C1-C2. The domains D1 and D2 constitute the amino-terminal pro-polypeptide and the remaining domains mature vWF, generated upon proteolytic processing. We have shown previously that the pro-polypeptide of pro-vWF is obligatory for assembly of pro-vWF dimers into multimers, a process vital for efficient adhesion of platelets to an injured vessel wall. Here, we have employed full length vWF cDNA to construct a series of deletion mutants, based on the homology between the various domains. Specifically, the domains D', D3 or both were deleted and the multimeric pattern of the mutant vWF proteins was analysed after transient expression in COS-1 cells. It is demonstrated that in addition to the pro-polypeptide, both the D' and the D3 domain are required for multimer assembly. Furthermore, by analysing a construct containing only the domains D' and D3 next to the pro-polypeptide it is shown that this is the only part of the vWF protein involved in multimer assembly. Since, the formation of pro-vWF dimers relies on the carboxy-terminal area of mature vWF, it is concluded that multimer assembly is a process independent of dimerization.
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PMID:Domains involved in multimer assembly of von willebrand factor (vWF): multimerization is independent of dimerization. 231 82

By means of a cloning strategy employing the polymerase chain reaction, we have isolated and characterized cDNAs for Xenopus laevis insulin-like growth factor I (IGF-I). These cDNAs encode a primary IGF-I translation product of 153 residues that demonstrates considerable amino acid sequence similarity with IGF-IA peptides from other species. Fifty-seven of 70 residues of the mature protein are identical among human, rat, chicken, and Xenopus IGF-I, while less amino acid conservation is found at the COOH-terminus (25/35 identities) or at the NH2-terminus (24/48 identities) of the precursor protein. Despite the lower degree of structural similarity at the NH2-terminus, in vitro studies of IGF-I biosynthesis and proteolytic processing support a conserved function for the atypically long 48 residue NH2-terminal signal sequence in directing the nascent IGF-I peptide through the secretory pathway. The 5'-untranslated region of Xenopus IGF-I mRNA matches the human, rat, and chicken sequences in greater than 90% of 279 nucleotides. IGF-I mRNAs from all four species encode a conserved upstream open reading frame of 14 amino acids starting 240-250 nucleotides 5' to the translation start site, suggesting a possible role for this region in modulating IGF-I gene expression. The X. laevis IGF-I gene is transcribed and processed into three mRNAs of 1.6, 2.1, and 3.0 kilobases in liver, and IGF-I mRNAs can be detected in liver, lung, heart, kidney, and peritoneal fat of adult animals. These studies demonstrate that both the IGF-I protein precursor and potential regulatory regions of IGF-I mRNA have been conserved during vertebrate evolution, and indicate that like several other polypeptide growth factors, IGF-I may be of fundamental importance in regulating specific aspects of growth and development in all vertebrates.
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PMID:Evolution of insulin-like growth factor I (IGF-I): structure and expression of an IGF-I precursor from Xenopus laevis. 233 2

A full-length cDNA clone for rat placental lactogen I (rPL-I) has been isolated from a phage lambda gt11 library containing cDNA synthesized from day 11 rat placental mRNA. By Northern blot analysis the rPL-I cDNA clone hybridizes to a 1.0-kilobase placental mRNA and appears as early as day 10 of gestation. Maximal expression of this mRNA was observed in day 11 and 12 placenta, and faint hybridization of the rPL-I cDNA was also detected in day 18 to term placenta. In contrast, the mouse clone hybridized to mRNA for mouse PL-I (mPL-I) only in day 10 mouse placenta (9). In vitro translation of rPL-I mRNA produced by transcription of the cDNA template yielded a 27-kDa polypeptide the size of the expected precursor protein which was immunoprecipitated by a monoclonal antibody to rPL-I. The rPL-I cDNA nucleotide sequence has been determined. The sequence is very similar to that for mPL-I and contains an open reading frame encoding a polypeptide of 230 amino acids compared to 224 for mPL-I. Comparison of the predicted primary translation product of rPL-I mRNA with that of mPL-I mRNA revealed that rPL-I shares 73% identity to mPL-I at the amino acid level. The predicted rPL-I protein shares 41% amino acid identity with rPL-II precursor, 24% with rat prolactin-like protein A, 26% with rat prolactin-like protein B, and 31% with rat PRL. In situ hybridization studies indicated that mRNA for rPL-I was present in a few rapidly dividing cells as early as day 8 of gestation, and by day 9 could be localized to giant cells which surround the conceptus.
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PMID:Molecular cloning and expression of rat placental lactogen-I complementary deoxyribonucleic acid. 237 51

Most cell surface proteins are anchored to the cell bilayer by hydrophobic membrane-spanning domains. Recently it has been shown that a small class of molecules are attached to cell surfaces via a phosphatidylinositol moiety covalently linked to the C-terminus of the mature processed polypeptide. The molecular signals that identify a polypeptide for phosphatidylinositol (PI) attachment have not been well defined in any system, but are thought to reside in the C-terminus of the primary translation product. We report that all the signals responsible for PI anchoring of Qa-2 Ag are confined to the 36 C-terminal residues of the precursor proteins. To investigate further the features that signal cleavage and PI addition, we have studied mutants of two closely related murine class I MHC molecules: the PI-linked Ag, Q9b, from the Qa-2 Ag family, and the integral membrane transplantation antigen, H-2Ld. The addition of 15 amino acids to the three residue long cytoplasmic domain of Q9b or the mutation of Asp295 found in its C-terminal hydrophobic domain to Val converts this molecule into an integral membrane protein. However, the introduction of a short three residue cytoplasmic tail and Asp295 into the transmembrane domain of H-2Ld does not convert this molecule to a PI-linked one. The results of these analyses suggest that the PI-processing signals may depend on overall conformation, hydrophobicity, and length of the C-terminal domain of the precursor protein. In addition these data indicate that PI anchoring of class I Ag requires more than two mutational steps and may have been selected during the evolution.
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PMID:Molecular signals for phosphatidylinositol modification of the Qa-2 antigen. 239 78

Inter-alpha-trypsin inhibitor is a 240-kDa plasma-protein complex of three different types of glycoproteins. Their stoichiometric relation in the complex is not yet known. One subunit results from proteolytic processing of a precursor protein composed of alpha 1-microglobulin and a double-headed Kunitz-type proteinase inhibitor protein. From this, only the inhibitor protein becomes part of the inter-alpha-trypsin inhibitor complex. Another subunit whose function is not yet understood is structurally unrelated to the first one as well as to other proteins of various data collections. Now we have obtained a cDNA clone coding for 837 amino acid residues of a precursor protein of the third subunit. Its primary structure is 40% identical to that of the completely known second-subunit precursor. Peptide sequences obtained from isolated inter-alpha-trypsin inhibitor represent a distinct part of only about two thirds of the predicted polypeptide precursor, suggesting that its maturation is very similar to that of the second subunit. Therefore, we conclude that the deduced primary structure covers about 98% of the mature third subunit.
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PMID:Two out of the three kinds of subunits of inter-alpha-trypsin inhibitor are structurally related. 247 37

Amyloid deposition in senile plaques and the cerebral vasculature is a marker of Alzheimer's disease. Whether amyloid itself contributes to the neurodegenerative process or is simply a by-product of that process is unknown. Pheochromocytoma (PC12) and fibroblast (NIH 3T3) cell lines were transfected with portions of the gene for the human amyloid precursor protein. Stable PC12 cell transfectants expressing a specific amyloid-containing fragment of the precursor protein gradually degenerated when induced to differentiate into neuronal cells with nerve growth factor. Conditioned medium from these cells was toxic to neurons in primary hippocampal cultures, and the toxic agent could be removed by immunoabsorption with an antibody directed against the amyloid polypeptide. Thus, a peptide derived from the amyloid precursor may be neurotoxic.
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PMID:Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease. 247 1


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