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Proteins in normal humans

Izquierdo MA, Scheffer GL, Flens MJ, Giaccone G, Broxterman HJ, Meijer CJ, van der Valk P, Scheper RJ (1996) Broad distribution of the multidrug resistance-related vault lung resistance protein in normal human tissues and tumors. Am J Pathol 148(3) 877-887. [Pg.255]

Boni R, Burg G, Doguoglu A, Ilg EC, Schafer BW, Muller B, Heizmann CW. 1997. Immunohis-tochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions. Br J Dermatol 137(1) 39—43. [Pg.124]

Cross SS, Hamdy FC, Deloulme JC, Rehman I. 2005. Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers. Histopathology 46(3) 256-269. [Pg.125]

Gown AM, Vogel AM. Monoclonal antibodies to human intermediate filament proteins. II. Distribution of filament proteins in normal human tissues. Am. J. Pathol. 1984 114 309-321. [Pg.111]

Aggarwal, S., S. W. Kim, K. Cheon, et al. 2006. Nonclassical Action of Retinoic Acid on the Activation of the Camp Response Element-Binding Protein in Normal Human Bronchial Epithelial Cells. Mol Biol Cell 17, no 2 566-75. [Pg.20]

Keyse SM, Tyrrell RM (1987) Both near ultraviolet radiation and the oxidizing agent hydrogen peroxide induce a 32-kDa stress protein in normal human skin fibroblasts. J Biol Chem 262 14821-14825... [Pg.261]

Walser, M., 1961, Ion Association VI. Interactions between calcium, magnesium, inorganic phosphate, citrate and protein in normal human plasma, /. Clin. Invest. 40 723. [Pg.62]

In normal human subjects, some 25 % of total body iron (800-1000 mg) is present in the storage forms, mostly as ferritin. Whereas it is likely that all mammalian cell types contain some ferritin, haemosiderin in normal subjects is essentially restricted to cells of the reticuloendothelial system. Ferritin turns out to be almost universal in its distribution ferritin and ferritin-like proteins have been found in all organisms except for one or two archaebacteria. In contrast, haemosiderin has not been found to any extent outside of iron-loaded animals, except for a brief report of a phytosiderin in pea seeds (Laulhere et ah, 1989). [Pg.173]

B. Sjostrom et al. Correlation of gene expression of ten drug efflux proteins of the atp-binding cassette transporter family in normal human jejunum and in human intestinal epithelial caco-2 cell monolayers, /. Pharmacol. Exp. Ther. 2001, 299, 164-170... [Pg.84]

Maliepaard M, Scheffer GL, Faneyte IF, van Gastelen MA, Pijnenborg AC, Schinkel AH et al. Subcellular localization and distribution of the breast cancer resistance protein transporter in normal human tissues. Cancer Res 2001 61(8)3458-3464. [Pg.211]

Smithies, O., Zone electrophoresis in starch gels group variations in the serum proteins of normal human adults. Biochem. J. 61, 629 (1955). [Pg.186]

Fig. 3. Predicted alternative splicing in HPS (Hermansky-Pudlak Syndrome). The HPS polypeptide is a novel transmembrane protein that is likely to be a component of multiple cytoplasmic organelles and is apparently crucial for their normal development and function. We demonstrated an putative alternate transcript of the HPS gene. By RT-PCR, two transcripts were found in normal human brain, kidney, liver, lung, pancreas, and placenta. The short transcript (AA700609, length 302 bp) shows a deletion of 521 bp in the 3 UTR region of the HPS gene. Fig. 3. Predicted alternative splicing in HPS (Hermansky-Pudlak Syndrome). The HPS polypeptide is a novel transmembrane protein that is likely to be a component of multiple cytoplasmic organelles and is apparently crucial for their normal development and function. We demonstrated an putative alternate transcript of the HPS gene. By RT-PCR, two transcripts were found in normal human brain, kidney, liver, lung, pancreas, and placenta. The short transcript (AA700609, length 302 bp) shows a deletion of 521 bp in the 3 UTR region of the HPS gene.
Lung resistance protein Lung resistance protein (LRP) is expressed in normal human bronchial epithelium (NHBE) as well as in other tissues potentially exposed to toxins [104], LRP was reported to be expressed in both Calu-3 cells [105] and 16HBE14o- model [70], However, the role of LRP in different cellular locations is not clear to date. [Pg.244]

Lehmann T, Torky AR, Stehfest E, Hofmann S, Foth H (2005) Expression of lung resistance-related protein, LRP, and multidrug resistance-related protein, MRP1, in normal human lung cells in long-term cultures. Arch Toxicol 79(10) 600-609... [Pg.280]

Kobayashi D, Watanabe N, Yamauchi N, Tsuji N, Sato T, Sasaki H, Okamoto T, Niitsu Y (1997) Protein kinase C inhibitors augment tumor-necrosis-factor-induced apoptosis in normal human diploid cells. Chemotherapy 43 415-423... [Pg.78]

The role of phosphorylation and degradation of hPER protein oscillation in normal human fibroblasts... [Pg.238]

DeLa Cadena, R.A., A. Majluf-Cruz, A. Stadnicki, M. Tropea, D. Reda, IM. Agosti, R.W. Colman, and A.F. Suffredini, Recombinant tumor necrosis factor receptor p75 fusion protein (TNFR Fc) alters endotoxin-induced activation of the kinin, fibrinolytic, and coagulation systems in normal humans. Thromb Haemost, 1998. 80(1) 114-8. [Pg.287]


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See also in sourсe #XX -- [ Pg.27 , Pg.28 , Pg.29 , Pg.30 ]




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