Carbohydrate moieties of glycoproteins a re-evaluation of their function

Olden, Kenneth; Parent, J B; White, Sandra L.

doi:10.1016/0304-4157(82)90017-x

Cited by 403 publications

(156 citation statements)

References 185 publications

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“…Sialic acid is an acylated derivative of neuraminic acid and exists as a terminal component of the non-reducing end of carbohydrate chains of glycoprotein in mammals. Their implications in a variety of surface-related vital cell functions in numerous tissues are well documented (Olden et al, 1982). Fucose has hydrophobic properties (Montreuil, 1980) and its presence in the mucous gland secretion and in the epidermis interstices can represent a barrier against the animal desiccation.…”

Section: Discussionmentioning

confidence: 99%

Effect of Luteolin on the Levels of Glycoproteins During Azoxymethane-induced Colon Carcinogenesis in Mice

Pandurangan¹,

Dharmalingam²,

Sadagopan³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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Section: Discussionmentioning

confidence: 99%

Effect of Luteolin on the Levels of Glycoproteins During Azoxymethane-induced Colon Carcinogenesis in Mice

Pandurangan¹,

Dharmalingam²,

Sadagopan³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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“…Finally, such a crosstalk may involve components of the unfolded protein (UPR) and ER overload (EOR) response pathways (Pahl and Baeuerle, 1995). The transcription factor CHOP/Gadd153, a component of the UPR pathway, has been shown to mediate apoptosis triggered by tunicamycin (Brenner et al, 1997;Olden et al, 1982;Zinszner et al, 1998). CHOP-regulated genes relevant for apoptosis regulation have not yet been identi®ed but may include pro-apoptotic molecules such as the Bcl-2 family member Bax, a known trigger of cytochrome c release on mitochondria (RosseÂ et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…Scale bar in the lower left corner corresponds to 1 mm not yet know how they impinge on the apoptotic machinery. Here we apply two apoptotic stresses that produce aberrant protein in the secretory system; brefeldin A (BFA), which blocks retrograde transport of Golgi-derived vesicles, leading to a stop in secretion and the fusion of the Golgi/ER compartments (Chardin and McCormick, 1999;Fujiwara et al, 1998) and tunicamycin which inhibits the ®rst reaction in the dolichol pathway of N-glycosylations of proteins in the ER lumen (Olden et al, 1982;Tkacz and Lampen, 1975). Interestingly, both stresses provoke a release of cytochrome c before or at the time of e ector caspase-3 activation suggesting a crosstalk between the perturbed ER and mitochondria.…”

Section: Introductionmentioning

confidence: 99%

Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2

et al. 2000

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Apoptosis involves mitochondrial steps such as the release of the apoptogenic factor cytochrome c which are e ectively blocked by Bcl-2. Although Bcl-2 may have a direct action on the mitochondrial membrane, it also resides and functions on the endoplasmic reticulum (ER), and there is increasing evidence for a role of the ER in apoptosis regulation as well. Here we uncover a hitherto unrecognized, apoptotic crosstalk between the ER and mitochondria that is controlled by Bcl-2. After triggering massive ER dilation due to an inhibition of secretion, the drug brefeldin A (BFA) induces the release of cytochrome c from mitochondria in a caspase-8-and Bid-independent manner. This is followed by caspase-3 activation and DNA/nuclear fragmentation. Surprisingly, cytochrome c release by BFA is not only blocked by wild-type Bcl-2 but also by a Bcl-2 variant that is exclusively targeted to the ER (Bcl-2/cb5). Similar ®ndings were obtained with tunicamycin, an agent interfering with N-linked glycosylations in the secretory system. Thus, apoptotic agents perturbing ER functions induce a novel crosstalk between the ER and mitochondria that can be interrupted by ER-based Bcl-2.

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“…After treatment with tunicamycin (10 ~tg/ml) the 26K and 35K bands disappeared, indicating that both proteins were glycosylated. No non-glycosylated precursor of the middle S protein was detected, but it is known that the non-glycosylated form of some proteins is sensitive to protease digestion (Olden et al, 1982). Western blot analysis showed that the 35K band reacted with antipre-S2 antibody (Fig.…”

Section: Characterization Of Hbsag Released From Ms128 Cellsmentioning

confidence: 98%

Stable Expression of the Hepatitis B Virus Surface Antigen Containing Pre-S2 Protein in Mouse Cells Using a Bovine Papillomavirus Vector

Yoneyama

Akatsuka

Miyamura

1988

Journal of General Virology

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SUMMARYThe large BglII fragment (2-8 kilobases) of hepatitis B virus DNA including the transcription unit for the hepatitis B surface antigen (HBsAg) was inserted into a bovine papillomavirus vector containing the neomycin resistance gene. The recombinant DNA was transfected into mouse C127 cells. A stable transformed cell line (MS128) secreting a large amount of 22 nm HBsAg particles containing pre-S2 protein was established. The secreted HBsAg particles had the receptor for polymerized human serum albumin. Immunoprecipitation and Western blot analyses showed that HBsAg particles consisted of two major proteins of 22K and 26K encoded by the S gene and a minor protein of 35K encoded by the pre-S2 and S genes. Southern blot analysis revealed that the transfected plasmid was integrated into the host chromosomal DNA and that most of the plasmid sequences were present. These results suggest that the stable expression of the HBsAg in MS128 cells is related to the integrated state of the recombinant DNA.

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Carbohydrate moieties of glycoproteins a re-evaluation of their function

Cited by 403 publications

References 185 publications

Effect of Luteolin on the Levels of Glycoproteins During Azoxymethane-induced Colon Carcinogenesis in Mice

Effect of Luteolin on the Levels of Glycoproteins During Azoxymethane-induced Colon Carcinogenesis in Mice

Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2

Stable Expression of the Hepatitis B Virus Surface Antigen Containing Pre-S2 Protein in Mouse Cells Using a Bovine Papillomavirus Vector

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