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Alpha -macroglobulin

Tsuji, A., Akamatsu, T., Nagamune, H., Matsuda, Y. (1994). Identification of targeting proteinase for rat alpha 1-macro-globulin in vivo. Mast-cell tryptase is a major component of the alpha 1-macroglobulin-proteinase complex endoc dosed into rat liver lysosomes. Biochem. J. 298 79-85. [Pg.90]

Fryer, S.E., Bender, R.C. and Bayne, C.J. (1996) Inhibition of cysteine proteinase from Schistosoma mansoni larvae by alpha-macroglobulin from the plasma of Biomphalaria glabrata. Journal of Parasitology 82, 343-347. [Pg.240]

Sottrup-Jensen L, Sand O, Kristensen L, Fey GH. The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins. J Biol Chem 1989 264 15781-15789. [Pg.70]

Sottrup-Jensen, L. (1989). Alpha-macroglobulins structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 264 11539-42. [Pg.90]

Toxic and carcinogenic effects of nickel compounds are associated with nickel-mediated oxidative damage to DNA and proteins and to inhibition of cellular antioxidant defenses. Most authorities agree that albumin is the main transport protein for nickel in humans and animals and that nickel is also found in nickeloplasmin - a nickel-containing alpha-macroglobulin - and in an ultrafilterable semm fraction similar to a nickel-histidine complex. Normal routes of nickel intake for humans and animals are ingestion, inhalation, and... [Pg.537]

Ashie, I.N.A. Simpson, B.K. Effects of hydrostatic pressure on alpha-Macroglobulin and selected proteases. J. Food Biochem. 1995,18, 377-391. [Pg.79]

B30. De Boer, J. R, Creasey, A. A., Chang, A., Abbink, J. J., Roem, D., Eerenberg, A. J., Hack, C. E., and Taylor, F. B., Alpha-2 macroglobulin functions as an inhibitor of fibrinolytic, clotting and neutrophilic proteinases in sepsis Studies using a baboon model. Infect. Immun. 61,5035-5043 (1993). [Pg.109]

Blacker, D., Wilcox, M. A., Laird, N. M. et al. Alpha-2 macroglobulin is genetically associated with Alzheimer disease. Nat. Genet. 19 357-360,1998. [Pg.665]

A. M. Tiggelman, C. Linthorst, W. Boers, H. S. Brand, and R. A. Chamuleau, Transforming growth factor-beta-induced collagen synthesis by human liver myofibroblasts is inhibited by alpha 2-macroglobulin. J. Hepatol. 26 1220-1228 (1997). [Pg.234]

C. A. Kawser, J. P. Iredale, P. J. Winwood, and M. J. P. Arthur, Rat hepatic stellate cell expression of alpha 2-macroglobulin is a feature of cellular activation implications for matrix remodelling in hepatic fibrosis, Clin. Sci. 95 179-186 (1998). [Pg.234]

Bu, G., S. Williams, D.K. Strickland, and A.L. Schwartz. 1992. Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor is an hepatic receptor for tissue-type plasminogen activator. Proc. Natl. Acad. Sci. USA... [Pg.42]

G7. Gross, V., Scholmerich, J., Leser, H. G., Salm, R., Lausen, M., and Ruckauer, K., Granulocyte elastase in assessment of severity of acute pancreatitis. Comparison with acute-phase proteins C-reactive protein, alpha 1-antitrypsin, and protease inhibitor alpha 2-macroglobulin. Dig. Dis. Sci. 35, 97-105 (1990). [Pg.73]

Borth W. Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics. FASEB J 1992 6(15)3345-3353. [Pg.26]

LaMarre J, Wollenberg GK, Gonias SL, Hayes MA. Cytokine binding and clearance properties of proteinase-activated alpha 2-macroglobulins. Lab Invest 1991 65(1)3-14. [Pg.26]

Delacroix DL, Marchandise FX, Francis C, Sibille Y. Alpha-2-macroglobulin, monomeric and polymeric immunoglobulin A, and immunoglobulin M in bron-choalveolar lavage. Am Rev Respir Dis 1985 132(4) 829-35. [Pg.274]

G22. Gravagna, P., Gianazza, E., Arnaud, P., Neels, M., and Ades, E. W., Modulation of the immune response by plasma protease inhibitors. II. Alpha 2-macroglobulin subunits inhibit natural killer cell cytotoxicity and antibody-dependent cell-mediated cytotoxicity. Scand. J. Immunol. 15, 115-118 (1982). [Pg.237]

Alpha 2-antiplasmin and alpha 2-macroglobulin. These inactivate plasmin. Plasmin activity is also reduced by thrombin-activatable fibrinolysis inhibitor, which modifies fibrin to make a less potent co-factor for the t-PA-mediated plasminogen. [Pg.177]

Beauchamp CO, Gonias SL, Menapace DP, Pizzo SV. A new procedure for the synthesis of polyethylene glycol-protein adducts—effects on function, receptor recognition, and clearance of superoxide-dismutase, lactoferrin, and alpha-2-macroglobulin. Analyt. Biochem. 1983 131 25-33. [Pg.546]

Kolodziej SJ, et al. The three-dimensional structure of die human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes. J. Biol. Chem. 2002 277 28031-28037. [Pg.1599]

Alpha-amylase Albumin Myeloperoxidase Alpha2-macroglobulin... [Pg.2058]

James K. Interactions between cytokines and alpha-2 macroglobulin. Immunol Today 1990 11 163-6. [Pg.498]

Dickinson AM, Shenton BK, Alomran AH, Donnelly PK, Proctor SJ. Inhibition of natural killing and antibody-dependent cell-mediated cytotoxicity by the plasma protease inhibitor alpha 2-macroglobulin (alpha 2M) and alpha 2M protease complexes. Clin Immunol Immunopathol 1985 36 259-5. [Pg.498]

Huang JS, Huang SS, Deuel TF. Specific covalent binding of platelet-derived growth factor to human plasma alpha 2-macroglobulin. Proc Natl Acad Sci USA 1984 81 342-6. [Pg.498]

Legres LG, Pochon F, Barray M, Gay F, Chouaib S, Delain E. Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin. J Biol Chem 1995 8381h1. [Pg.498]


See other pages where Alpha -macroglobulin is mentioned: [Pg.582]    [Pg.81]    [Pg.81]    [Pg.448]    [Pg.448]    [Pg.174]    [Pg.166]    [Pg.14]    [Pg.63]    [Pg.237]    [Pg.370]    [Pg.558]    [Pg.122]    [Pg.358]    [Pg.582]    [Pg.98]    [Pg.336]    [Pg.256]    [Pg.81]    [Pg.81]    [Pg.2057]    [Pg.498]   
See also in sourсe #XX -- [ Pg.58 , Pg.597 ]




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