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Histidine rich proteins

Sullivan, D.J., Gluzman, I.Y. and Goldberg, D.E. (1996) Plasmodium hemozoin formation mediated by histidine-rich proteins. Science 271,219-222. [Pg.337]

Iron(n) is known to decompose hydrogen and dialkyl peroxides to free radicals by reductive cleavage of the 0—0 bond and early investigations established the parasite s sensitivity to these species. When treated with radiolabelled C-artemisinin, the hemin-hemozoin fraction of the lysed malaria-infected erythrocytes was shown to contain a radiolabel, though the mechanism of incorporation is not clear. Meshnick and coworkers demonstrated that uninfected cells did not contain radiolabelled proteins whereas six radiolabelled proteins were isolated from cells infected with the Plasmodium falciparum (P. falciparum) strain of the parasite. It was suspected that one of the alkylated proteins was the Histidine Rich Protein (HRP) that was known to bind multiple heme monomers and therefore thought to be instrumental to the parasite s detoxification process. Moreover, iron chelators were found to inhibit the lethal effects of peroxides on the parasite. ... [Pg.1283]

Another possible participant in hemozoin nucleation is the histidine-rich protein (HRP). Using monoclonal antibodies to probe the proteins of the digestive food vacuole of P. falciparum, Sullivan et al. identified two histidine-rich proteins, HRP II and HRP III, and demonstrated that these proteins could mediate the formation of hemozoin [37]. HRP II (Mr 35 kD) contains 51 repeats of the sequence Ala-His-His (76% of the mature protein is histidine and alanine) [38], while HRP III (Mr 27 kD) contains 28 Ala-His-His sequences (56% of the mature protein is histidine and alanine) [39]. While a clone lacking both HRP II and III has been shown to produce hemozoin, a third protein which cross reacted with anti-HRP monoclonal antibodies has also been found in the digestive vacuole of this strain. Although this protein has not been isolated or shown to mediate hemozoin formation, a candidate is HRP IV (Mr 10 kD) which is 31% histidine [40]. [Pg.334]

Harding, C.R., and I.R. Scott. 1983. Histidine-rich proteins (filaggrins) Structural and functional heterogeneity during epidermal differentiation. J Mol Biol 170 651. [Pg.228]

Salivary histatins have a high ability to precipitate tannins [18, 40, 71]. Histatins are histidine-rich proteins that can be found in both sublingal/submandibular saliva and parotid saliva and represent about 2.6% of the total salivary proteins. It has been proposed that histatins could be important in neutralizing tannins in situations where they come not from the diet but from other situations when the saliva is not stimulated, such as when cotton workers breathe tannin-rich dust [181-... [Pg.388]

Scott, I., Harding, C., and Barrett, J., Histidine-rich protein of the keratohyalin granules source of the free amino acids, urocanic acid and pyrrolidone carboxylic acid in the stratum comeum, Biochim. Biophys. Acta, 719, 110, 1982. [Pg.93]

Horii, I. et al. Histidine-rich proteins as a possible source of free amino acids of stratum comeum, J. Dermatol. (Tokyo), 10, 25, 1983. [Pg.207]

Ziegler J, Change R, Wright D. Multiple-antigenic peptides of histidine-rich protein 11 of Plasmodium falciparum den-drimeric biomineralization template. J. Am. Chem. Soc. 1999 121 2395-2400. [Pg.2116]

Schneider EL, Marietta MA. Heme binding to the histidine-rich protein II from Plasmodium falciparum. Biochemistry 2005 44 979-986. [Pg.2116]

The sequence of appearance, relative amounts, and final relationships of cell components that survive lysis are presented diagrammatically in Figure 11. The smallest filaments that have been isolated (35 A thick) have low sulfur content (32). They thicken to 60-90 A with addition of sulfur-rich protein (demonstrated by heavy metal staining) (32, 64) and histidine-rich protein (demonstrated with radioactive labeling) (49). Five to 10 of these thickened filaments aggregate to form fibrils that average 250 A in diameter (70). Meanwhile, KH and ER protein accumulate until the cell is lysed when they are mixed and dispersed (47) to coat the 250-A fibrils (70). The coated fibrils are submerged in a matrix that includes nucleoproteins and nonfibrous proteins these incorporate about 10 times more sulfur than the fibrils (32). The insoluble fibrils and matrix constitute about 65% of the cornified cell (66) other components include 10% soluble keratin, 10% dialyzable substances (amino acids, etc.), 7-9% lipids, and about 5% membrane protein (65, 66). [Pg.55]

Keratohyalin and Tonofibrils. The investment of tonofibrils with a histidine-rich protein is followed by their aggregation into bundles of filaments 64, 84). X-ray diflFraction studies and electron microscopy indicate that tonofilaments tend to associate in bundles of 5 to 10 filaments (Figure 14), each with a collective diameter of about 250 A (70, 81). These bundles correspond in size to the tonofibrils of the light microscopist (81). [Pg.59]

A number of histidine analogues, including 2-azido-L-histidine (201), have been evaluated by the NIH as part of a programme directed towards the development of new antimalarials for the prophylaxis and treatment of drug-resistant Plasmodium falciparum malaria [261]. Asexual P. falciparum parasites have a much higher histidine content than mammalian cells, and several histidine-rich proteins are thought to be functionally important in... [Pg.196]

Keratohyalin Granules The Story of the Histidine-Rich Protein ... 348... [Pg.319]

Voorhees et al. (V6) have recently reviewed the situation in psoriasis with regard to the formation of the histidine-rich protein. As has been stated previously, keratohyalin granules are absent from the intermediary layer in psoriasis, and these authors have demonstrated a lack of synthesis of the histidine-rich protein and a return toward normal with treatment and with the return of the keratohyalin granule. How the defect in formation of this protein is related to the increased epidermal proliferation is not known, but presumably on grounds of economy they should be related to one underlying abnormality. [Pg.349]

Chiodini, P. L., Bowers, K., Jorgensen, P., Barnwell, J. W., Grady, K. K., Luchavez, J., Moody, A. H., Cenizal, A., and Bell, D. (2007). The heat stability of Plasmodium lactate dehydrogenase-based and histidine-rich protein 2-based malaria rapid diagnostic tests. Trans. R. Soc. Trop. Med. Hyg. 101, 331-337. [Pg.335]

Kilejian, A. (1978). Histidine-rich protein as a model malaria vaccine. Science 201,922-924. [Pg.355]

Kilejian, A., Chen, S., and Sloma, A. (1985). The biosynthesis of the histidine-rich protein of Plasmodium lophurae and the cloning of its gene in Escherichia coli. Mol. Biochem. Parasitol. 14, 1-10. [Pg.355]

Margossian, S. S., McPhie, P., Howard, R. J., Coligan, J. E., and Slayter, H. S. (1990). Physical characterization of histidine-rich protein from Plasmodium lophurae. Biochim. Biophys. Acta 1038,330-337. [Pg.362]


See other pages where Histidine rich proteins is mentioned: [Pg.80]    [Pg.1311]    [Pg.1283]    [Pg.1311]    [Pg.342]    [Pg.360]    [Pg.168]    [Pg.63]    [Pg.191]    [Pg.195]    [Pg.162]    [Pg.145]    [Pg.488]    [Pg.5363]    [Pg.2109]    [Pg.60]    [Pg.197]    [Pg.12]    [Pg.14]    [Pg.349]    [Pg.349]    [Pg.386]    [Pg.31]    [Pg.208]    [Pg.252]    [Pg.281]   
See also in sourсe #XX -- [ Pg.334 , Pg.342 , Pg.360 ]

See also in sourсe #XX -- [ Pg.25 , Pg.334 , Pg.342 , Pg.360 ]




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Proteins Histidine

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