Proteinase neutral

Inflammatory injury is tied to both neutrophil release of neutral proteinases and a respiratory burst with production of superoxide anion and hydrogen peroxide... 

This enzyme [EC 3.4.24.27], also known as Bacillus ther-moproteolyticus neutral proteinase, is a thermostable extracellular metalloendopeptidase containing zinc and four calcium ions. A member of the peptidase family M4, this enzyme catalyzes the hydrolysis of peptide bonds with a preference for Xaa—Leu > Xaa—Phe. 

Okita, J. R., Erojmovic, M. M., Kristopeit, S., et al., Montreal platelet syndrome A defect in calcium-activated neutral proteinase (Calpain). Blood 74, 715-721 (1989). 

Saito, K., Elce, J.S., Hamos, J.E., and Nixon, R.A., 1993, Widespread Activation of Calcium-Activated Neutral Proteinase (Calpain) in the Brain in Alzheimer Disease A Potential Molecular Basis for Neuronal Degeneration, Proc. Natl. Acad. Sci. U. S. A., 90, 2628-2632 Kawai, H., Akaike, M., Kunishige, M., Inui, T., Adachi, K., Kimura, C., Kawajiri, M., Nishida, Y., Endo, I., and Kashiwagi, S. et al., 1998, Clinical, pathological, and genetic features of limb-girdle muscular dystrophy type 2A with new calpain 3 gene mutations in seven patients from three Japanese families, Muscle Nerve, 21, 1493-1501... 

Saito, K., Elce, J. S., Hamos, J. E., and Nixon, R. A. (1993). Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 90, 2628-2632. 

Other name Aspergillus sojae neutral proteinase II Microbial neutral proteinase II Preferential cleavage of bonds with hydrophobic residues in Pi also Asn3- -Gln and Glys-J.-Ser bonds in insulin B chain. For calf thymus histone H4, high activity towards... 

Sekine, H. (1973). Neutral proteinases II of Aspergilus sojae an enzyme specifically active on protamine and histone. Agric. Biol. Chem., 37, 1765-1767. 

Tatsumi, H., Ikegaya, K., Murakami, S., Kawabe, H., Nakano, E., and Motai, H. (1994). Elucidation of the thermal stability of the neutral proteinase II from Aspergillus oryzae. Biochim. Biophys. Acta, 1208, 179-185. 

The neutral proteinase, enterokinase, which cleaves trypsinogen to trypsin... 

Zapelena, M. J., Zalacain, I., Pena, P. D., Astiasaran, I., and Bello, J. 1997. Effect of the addition of a neutral proteinase from Bacillus subtilis (Neutrase) on nitrogen fractions and texture of Spanish fermented sausage. J. Agric. Food Chem., 45, 2798-2801. 

The ratio of microfibrillar protein to elastin, however, appears to decrease upon maturation (2). Other proteins are also secreted with microfibrillar protein and elastin. It is now clear that bound to elastin in its non-crosslink form(s) is a trypsin-like neutral proteinase (26). This proteinase effects... 

Japanese Society of Miso Science and Technology Figure 18. Schematic representation of effect of heat treatment on soybean protein and its hydrolysis patterns by various enzymes. Pattern A, pepsin and other acid proteinoses pattern B, the proteinoses having an optimum near neutrality, such as papain, bacteria neutral proteinase, Aspergillus alkaline proteinase, Aspergillus neutral proteinase and pattern C, trypsin and in vivo nutritional... 

Backstrom JR, Miller CA, Tokes ZA (1992) Characterization of neutral proteinases from Alzheimer-affected and control brain specimens identification of calcium-dependent metal-loproteinases from the hippocampus. J Neurochem 58 983-992 Basun H, Forssell LG, Wetterberg L, Winblad B (1991) Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer s disease. J Neural Transm Park Dis Dement Sect 3 231-258... 

Thermolysins (Thermostable neutral proteinase ) Bacillus caldolyticus, sp., stearother-mophilus, thermoproteolyti- Extracellular, thermostable, digestive bacterial proteases. Hydrolyze the N-terminal side of hydrophobic residues. Xaa Eeu > Xaa Phe 53-56... 

Senior, RM. and Campbell, E.J. (1983). Neutral proteinases from human lung inflammatory cells. Clin. Lab. Med. 3, 645-666. 

Papain Neutral Proteinase Carica papaya Meat and Plant Protein Hydrolysis Yields Amino... 

Bromelain Neutral Proteinase Anana sativa Acids and Peptides Precursors for Maillard Reactions... 

Pancreatin Peptidase Neutral Proteinase Exopeptidase Animal Pancreas Aspergillus ssp. Bitter-free Protein Hydrolysates... 

PMN Products - Neutral proteinases of PMN lysosomes degrade a wide variety of collective tissue substrates including elastin, proteoglycan, and collagen. Cathepsin G has been found only in PMN, and elastase from these cells has a substrate gpecificity different from that of pancreatic and macrophage elastase. In addition to their effects on connective tissue components, the neutral proteinases of PMN lysosomes also stimulate the activity of other cells involved in the inflammatory response. Both elastase and cathepsin G from human PMN stimulate the incor- poration of thymidine by human peripheral blood and splenic lymphocytes. The stimulated lymphocytes are of the B lineage, with no effect seen on T lymphocytes. 

Rabbit synovial fibroblasts in culture have been shown to secrete a metal dependent neutral proteinase that degrades the protein core of cartilage proteoglycans. The enzyme is found in a latent form in the culture medium and is activated by limited proteolysis.23... 

Mouse and chick bone explants have been shown to produce a latent collagenase.33,34 jn addition, the mouse bone explants produce a latent neutral proteinase. Limited proteolysis of these molecules gives rise to proteoglycan and collagen degrading action. Latency may be due to the presence of an enzyme inhibitor complex. The chick latent collagenase has an apparent MW of 54,000, while the active form has an MW of 43,000. 3 Trypsin activation of both latent mouse enzymes decreases their MW s from 60-70,000 to about 40,000. The mouse neutral protease is inhibited by EDTA, cysteine, and serum.34... 

In a model of acute inflammatory disease, the reverse passive Arthus reaction, protease Inhibitors such as trasylol and SBTI have been shown to diminish the inflammatory response, particularly accumulation of leukocytes and vascular permeability.95 This provides support for the rational to search for specific neutral proteinase inhibitors as new modalities of therapy in R.A. See also chapter 23. 

Neutral Proteinases in Rheumatoid Arthritis Arnold L. Gronsky, Christine Winslow Buermann 14, 219 ... 

In rheumatoid arthritis, collagenous tissues of the joint (including articular cartilage) are eroded by collagenases and neutral proteinases derived from proliferating cells of the synovial membrane and leukocytes. Therapeutic approaches may depend on regulation of collagen synthesis, breakdown, or both. 

Neutral proteinases, elastase (EC 3.4.21.11), cathepsin G, and a third serine proteinase seem to be the most important mediators of these effects. In addition to their degradative properties, it was found that PMN elastase and cathepsin G can stimulate lymphocyte B antibody formation in vitro (VI). The granules have been intensively studied for their role in the oxidative burst of the PMN this aspect is discussed in Section 4.4. 

VI. Vischer, T. L., Bretz, U., and Baggiolini, M., In vitro stimulation of lymphocytes by neutral proteinases from human polymorphonuclear leukocyte granule. /. Exp. Med. 144, 863-870 (1976). 

Bacillus thermoproteolyticus neutral proteinase. Preferential cleavage Xaa-I-Leu > Xaa-I-Phe. 

Andresen, K., Tom, T. D. and Strand, M. (1991) Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni. J. Biol. Chem. 266 15085-15090. 

The practical utilization of pH during the sorption of neutral proteinase from Bacillus subtilis on Sepharose with attached glycyl-D-phenylalanine (through a spacer 23 atoms long) is shown in Fig. 4.7.5. Walsh et al. [62] demonstrated that between pH 5 and 6.5 neutral proteinase was effectively adsorbed and thus separated both from subtilisin and other proteins present in the culture filtrate. At higher pH values, an effective separation of neutral proteinase from subtilisin does not take place. 

Neutral proteinase is set free from the complex with the immobilized affinant by increasing the pH to values at which the binding of the substrate is already weak, but at which the enzyme is still not denatured. The optimum pH for the elution of neutral proteinase depends not only on its affinity towards the affinant and on the pH dependence of this affinity, but also on the concentration of the immobilized inhibitor. Neutral proteinase is a metalloenzyme and is therefore inhibited by... 

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