Syrian Hamster protein

FIGURE 8.3 (a), Output of the Driftscope program for a truncated Syrian Hamster protein... 

Monte Carlo/simulated annealing (MC/SA) algorithm for sequential assignment in uniformly 13C, 15N-labeled proteins [137]. The two-dimensional (2D) NCACX and NCOCX spectra measured for the fibril samples of full-length Syrian hamster prion protein (residues 23-231) have been analyzed by the MC/SA protocol, from which it has been concluded that the fibril core is formed primarily in the region of residues 173-224 [54]. 

Sokolowski, F., Modler, A. J., Masuch, R., Zirwer, D., Baier, M., Lutsch, G., Moss, D. A., Gast, K., and Naumann, D. (2003). Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein. / Biol. Chem. 278, 40481-40492. 

Both specificity studies confirmed that bromosulphthalein (BSP) competitively inhibited taurocholate transport by NTCP and OATP. This is in conflict with reports that BSP transport was not sodium dependent, suggesting that OATP was responsible.The reason for this dilference is not clear but may reflect dilferences in the approaches, using isolated rat hepatocytes or transfection to produce cells that stably express the protein. Choice of cell line may also be important as expression of MEH also showed dilferences, with no demonstrable Na" -dependent transport of taurocholate in Syrian hamster kidney cells or oocytes but Na" -dependent transport was shown in Mardin-Darby canine... 

As expected, castration affects gland size, activity, and composition of the secretion profoundly. Eor example, castration changes the levels of porphyrins, indoles, and proteins in the Harderian gland secretion of the Syrian hamster (Buzzelletflk, 1991). 

Dichloromethane induced DNA-protein cross-links in vitro in hepatocytes of male B6C3Fi mice but not in hepatocytes of Fischer 344 rats, Syrian hamsters or in human hepatocytes with functional GSTTl genes. DNA-protein cross-links were also induced in Chinese hamster ovary CHO cells exposed to dichloromethane with or without exogenous metabolic activation. DNA damage was greater, however, in the presence of metabolic activation. 

DIA, DNA-protein cross-links, Syrian hamster hepatocytes in vitro... 

Benzoyl peroxide generally inhibits gap-junctional intercellular communication in cultured cells. In contrast, an increase in gap-junctional intercellular communication was observed in a Syrian hamster embryo cell line. Changes in the expression of gap-junctional proteins (connexins) concomitant with inhibition of gap-junctional intercellular communication have been observed. In SEN mice treated with 83 jmol benzoyl peroxide, keratinocytes expressed the gap-jimctional connexin 26 gene (not normally expressed in adult mouse skin), transiently increased the expression of connexin 43 and reduced the expression of connexin 31.1 (Budunova et al., 1995, 1996). In primary mouse kerati-nocyte cultures, benzoyl peroxide strongly decreased the amount of E-cadherin protein (Jansen etal., 1996). 

Lucas, E.A., Khalil, D.A., Daggy, B.P., and Arjmandi, B.H. 2001. Ethanol-extracted soy protein isolate does not modulate serum cholesterol in golden Syrian hamsters A model of postmenopausal hypercholesterolemia. J. Nutr. 131, 211-214. 

Afshari, C., S. Kodama, H. Bivins, T.B. Willard, H. Fujiki, and J.C. Barrett. 1993. Induction of neoplastic progression in Syrian hamster embryo cells treated with protein phosphatase inhibitors. Cancer Res. 53 1777-1782. 

Kessler, P.D., Cates, A.E., Van Dop, C., and Feldman, A.M. 1989. Decreased bioactivity of the guanine nucleotide-binding protein that stimulates adenylate cyclase in hearts from cardiomyo-pathic Syrian hamsters. J. Clin. Invest. 84 244-252. 

Mally, M. I., Grayson, D. R., and Evans, D. R. (1980). Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells. J. Biol Chem., 255, 11372-11380. 

There are 25 cysteines in apoB 16 of these are known to be involved in disulfide bonds, 7 are known to be free, and the remaining two, Cys-2906 and Cys-4326, are unknown (Yang et al., 1990). Only two of the free cysteines of apoB, Cys-3734 and Cys-4190, are labeled in LDL by the fluorescent probe 5-iodoacetamidofluorescein, possibly because they are exposed on the surface of the lipoprotein (Coleman et al., 1990). Of the 8 disulfide bonds in apoB 100, 7 are within 1000 amino acids of the N terminus of the protein (6 in the first 500 amino acids). The first two disulfides, Cys -Cys and Cys -Cys °, cross the remainder of the disulfides are between nearest neighbors. The number of amino acids separating the cysteines in each disulfide is relatively small, 5-49 amino acids the exception is Cys -Cys , wherein the cysteines are separated by 130 amino acids. This disulfide is apparently unique to the human sequence, because cysteines are not found in homologous positions in rat, mouse, Syrian hamster, pig, rabbit, or chicken apoB (Law and Scott, 1990). The disulfide pattern of apoB 100 is shown schematically in Fig. 1C. 

Kollack-Walker S, Newman SW (1997) Mating-induced expression of c-fos in the male Syrian hamster brain role of experience, pheromones, and ejaculations. J Neurobiol 32 481-501 Krieger J, Schmitt A, Lobel D, Guderman T, Schultz G, Breer H, Boekhoff I (1999) Selective activation of G protein subtypes in the vomeronasal organ upon stimulation with urine-derived compounds. J Biol Chem 274 4655 1662... 

Liu H, Larr-Jones S, Ulyanov NB et al (1999) Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 38 5362-5377... 

Parchment OG, Essex JW (2000) Molecular dynamics of mouse and Syrian hamster PrP implications for activity. Proteins Struct Funct Genet 38 327... 

Fig. 8. Cartoons of three-dimensional PrP structures. (A) Intact recombinant bovine prion protein, bPrP(23-230). (B) Intact recombinant human prion protein, hPrP(23-230). (C) Recombinant Syrian hamster prion protein, shPrP(29-231). The helices are colored green in (A), red in (B) and pink in (C) in all three structures the P strands are cyan, the segments with nonregular secondary structure within the globular domain are yellow, and the residues 23-120 in (A) and (B), and 29-124 in (C) of the flexibly disordered tail are schematically represented by yellow dots.

II. The NMR Structures oe the Recombinant Bovine, Human, Mouse, and Syrian Hamster Prion Proteins... 

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