The Experts below are selected from a list of 177 Experts worldwide ranked by ideXlab platform
Hiroko Mine - One of the best experts on this subject based on the ideXlab platform.
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Isolation and amino acid sequence of a cystatin-type cysteine Proteinase Inhibitor from bovine hoof
Archives of Dermatological Research, 1996Co-Authors: Hirofumi Tsushima, Kayo Higashiyama, Hiroko MineAbstract:A low molecular mass cysteine Proteinase Inhibitor was found and isolated from bovine hoof. Purification of the Inhibitor to homogeneity was performed by carboxymethyl-papain-sepharose affinity and DE-52 ion exchange chromatographies. From 15 g of bovine hoof, 0.25 mg of cysteine Proteinase Inhibitor was isolated. It had 100 amino acid residues and molecular mass of 11406 Da, and its N-terminus was blocked. The amino acid sequence of the Inhibitor demonstrated high similarity with that of the family 1 group, especially bovine thymus-derived cystatin. Thus, in summary, bovine hoof contains a cystatin-type cysteine Proteinase Inhibitor, presumably a family 1 cystatin.
Jack Gauldie - One of the best experts on this subject based on the ideXlab platform.
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regulation of secretory leukocyte Proteinase Inhibitor slpi and elastase specific Inhibitor esi elafin in human airway epithelial cells by cytokines and neutrophilic enzymes
American Journal of Respiratory Cell and Molecular Biology, 1994Co-Authors: Jeanmichel Sallenave, Jerry Shulmann, John Crossley, Manel Jordana, Jack GauldieAbstract:The regulation of the activity of potentially harmful Proteinases secreted by neutrophils during inflammation is important for the prevention of excessive tissue injury. Secretory leukocyte Proteinase Inhibitor (SLPI), also called antileukoprotease (ALP) or mucus Proteinase Inhibitor (MPI), is a serine Proteinase Inhibitor that has been found in a variety of mucous secretions and that is secreted by bronchial epithelial cells. We recently reported the presence of SLPI and of an elastase-specific Inhibitor (ESI), also called elafin, in the supernatants of two cell lines, NCI-H322 and A549, which have features of Clara cells and type II alveolar cells, respectively. We showed in addition that epithelial cell lines produce the elastase-specific Inhibitor as a 12 to 16 kD precursor of the elafin molecule (6 kD) called pre-elafin. In the present study, we show that NCI-H322 cells produced higher amounts of both Inhibitors than A549 cells and that basal production of SLPI in both cell lines is higher than the p...
Clarence A Ryan - One of the best experts on this subject based on the ideXlab platform.
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overexpression of the prosystemin gene in transgenic tomato plants generates a systemic signal that constitutively induces Proteinase Inhibitor synthesis
Proceedings of the National Academy of Sciences of the United States of America, 1994Co-Authors: Barry Mcgurl, Gregory Pearce, Martha L Orozcocardenas, Clarence A RyanAbstract:Abstract Tomato plants (Lycopersicon esculentum, var. Better Boy) were stably transformed with a gene consisting of the open reading frame of a prosystemin cDNA under the regulation of the cauliflower mosaic virus 35S promoter. The leaves of the transgenic plants constitutively produced Proteinase Inhibitor I and II proteins, which accumulated over time to levels exceeding 1 mg/g of dry leaf weight. This phenotype contrasts with that of untransformed plants, which produce Proteinase Inhibitor proteins in leaves only in response to wounding or chemical inducers. The transgenic plants were also stunted, although they appeared normal in all other respects. Grafting the upper half (scion) of an untransformed tomato plant onto the lower half (root stock) of a tomato plant expressing the prosystemin transgene resulted in the constitutive expression of Proteinase Inhibitor proteins in the leaves of both the transformed root stock and the untransformed scion, demonstrating that expression of the prosystemin transgene generates a mobile wound signal. These results show that systemic signal propagation in the transgenic plants does not require wounding, and they support the proposed role of systemin as the mobile wound signal.
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Systemin, a Polypeptide Signal for Proteinase Inhibitor Gene Expression in Plants
Developments in Plant Pathology, 1993Co-Authors: Clarence A Ryan, Barry Mcgurl, Martha L. Orozco-cárdenas, S Johnson, Gregory Pearce, Edward E. FarmerAbstract:Although signalling pathways that regulate plant defensive genes are poorly understood at the biochemical level, several types of signalling molecules have been identified that are associated with the expression of genes activated in response to plant-herbivore or plant-pathogen interactions. These molecules include plant hormones and growth regulators as well as oligosaccharides and a polypeptide (1–4). Recent evidence indicates that the polypeptide, called systemin (4), is a systemic signal that activates Proteinase Inhibitor genes in response to wounding via an octadecanoid-based intracellular signalling cascade (5). In this chapter we briefly summarize the properties of systemin and its precursor, prosystemin (6), and their possible roles in regulating the expression of Proteinase Inhibitor genes in response to wounding.
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a polypeptide from tomato leaves induces wound inducible Proteinase Inhibitor proteins
Science, 1991Co-Authors: Gregory Pearce, Daniel Strydom, Scott Johnson, Clarence A RyanAbstract:Defensive genes in plants can be activated by several different types of nonpeptide signaling molecules. An endogenous polypeptide, consisting of 18 amino acids, was isolated from tomato leaves and was able at very low concentrations to induce the synthesis of two wound-inducible Proteinase Inhibitor proteins when supplied to young tomato plants. The sequence of the polypeptide was determined, and an identical polypeptide was synthesized that possessed full inducing activity. These data establish that a polypeptide factor can initiate signal transduction to regulate the synthesis of defensive proteins in plant tissues.
V. K. Hopsu-havu - One of the best experts on this subject based on the ideXlab platform.
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Purification and characterization of a cystatin-type cysteine Proteinase Inhibitor in the human hair shaft
Archives of Dermatological Research, 1992Co-Authors: H. Tsushima, A. Ueki, H. Mine, N. Nakajima, H. Sumi, V. K. Hopsu-havuAbstract:We found a cysteine Proteinase Inhibitor in human hair shaft extract treated with 0.01 M Tris HCl buffer, pH 8.0. A yield of 0.2 mg of purified cysteine Proteinase Inhibitor was obtained from 86 g of hair shaft. The cysteine Proteinase Inhibitor had a molecular mass of 13 kDa as determined by high-performance liquid chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. It was more stable to heat and pH than most proteins and had a pI of 4.7. Immunologically, its antigenicity was the same as that of cystatin A, but differed from that of cystatin B and C, and kininogen. The amino-acid sequence of the first 30 residues from the NH terminus of the Inhibitor was identical to that of cystatin A from human epidermis. Hair shaft cysteine Proteinase Inhibitor is thus considered to be identical to epidermal cystatin A.
Harald Burkhardt - One of the best experts on this subject based on the ideXlab platform.
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purification of a serine Proteinase Inhibitor from human articular cartilage identity with the acid stable Proteinase Inhibitor of mucous secretions
Biochemical Journal, 1991Co-Authors: B Bohm, Rainer Deutzmann, Harald BurkhardtAbstract:An Inhibitor of the serine Proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-Proteinase Inhibitor of human mucous secretions. Identity of both Inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-Proteinase Inhibitor. In all 24 residues the cartilage Inhibitor was shown to be identical with the human secretory leucocyte Proteinase Inhibitor (‘SLPI’). The Inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.
