An abundant ubiquitous glycoprotein (GP<sub>100</sub>) in nucleated mammalian cells

Koch, G.; Smith, Michael J.; Mortara, Renato Arruda

doi:10.1016/0014-5793(85)80537-8

Cited by 13 publications

(1 citation statement)

References 16 publications

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“…It is also referred to as GP100 (18), ERp99 (26), or endoplasmin (16) and was found to be substantially overexpressed in tissues or cells that are rich in ER (26). Another abundant protein in the ER is the 78-kilodalton GRP (GRP78), which has been identified as the immunoglobulin heavy-chain-binding protein (BiP; 12,31).…”

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confidence: 99%

Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.

1989

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We isolated the promoter of the human gene encoding the 94,000-dalton glucose-regulated protein (GRP94). The 5'-flanking region important for its expression was identified by deletion analysis. Comparison of the promoters of the genes for GRP78 and GRP94 derived from human, rat, and chicken cells revealed a common domain of 28 base pairs within the putative regulatory regions of both genes. This domain has been shown to interact with protein factors in the promoter of the gene for GRP78. Since the genes for GRP94 and GRP78 are transcriptionafly regulated with similar kinetics under a variety of stress conditions, we are interested in examining the possible mechanisms for their coordinated expression. Through in vitro and in vivo competition assays, we found that the protein factors which interact with the promoter of the gene for GRP94 also have affinity for the conserved domain of the promoter of the gene for GRP78. These findings suggest that the genes for GRP94 and GRP78 are coordinately regulated through common trans-acting factors which recognize a common regulatory domain of glucose-regulated protein gene promoters.

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confidence: 99%

Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.

1989

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Analysis of development and differentiation with tumour cell glycoproteins

Koch

Smith

1985

BioEssays

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The repertoire of acceptor glycoproteins for concanavalin A expressed by a cultured tumour cell reflects the normal developmental lineage from which it was derived, as well as the degree of maturation along that lineage. Antibodies to this particular set of glycoproteins show a considerable specificity towards normal differentiation antigens which are often preferentially associated with the less mature intermediates of the corresponding pathway. In addition, comparisons between ‘immature’ and ‘mature’ tumour cells can be used to identify glycoproteins associated with specific differentiated functions such as secretion. Thus tumour cell glycoproteins provide useful probes for analysis of the molecular biology of development and differentiation.

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The analysis of glycoproteins in cells and tissues by two‐dimensional polyacrylamide gel electrophoresis

Koch

Smith

1990

Electrophoresis

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Two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) was used to identify and analyse subsets of proteins in cells and tissues. The combination of 2-D PAGE and [125I] concanavalin A overlay revealed an extraordinary complexity and diversity in the glycoprotein profiles of different cell types. However, the glycoproteins are not expressed idiosyncratically. Rather, their expression is closely linked to the state of differentiation of a particular cell type. Such glycoproteins can therefore be used to generate antibodies specific for differentiated cells. 2-D PAGE analyses of cellular glycoproteins also revealed a major common glycoprotein of 100 kDa. This was localised to the lumen of the endoplasmic reticulum and is referred to as endoplasmin. The combination of 2-D PAGE with electroblotting and 45Ca overlay revealed that endoplasmin and several other luminal endoplasmic reticulum proteins (reticuloplasmins) are high capacity, low affinity calcium binding proteins which could function as calcium storage proteins in the endoplasmic reticulum. One of these called calreticulin is also found in the sarcoplasmic reticulum. 2-D PAGE and 45Ca overlay has been used to demonstrate the presence of a calcium-binding protein (CP22/sorcin) in the cytosol of rodent multidrug resistant cells. Analyses of murine serum by 2-D PAGE revealed the presence of a novel stress protein serum amyloid P component. These studies illustrate the value of 2-D PAGE when used in combination with detection methods which select specific subsets of proteins such as glycoproteins.

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An abundant ubiquitous glycoprotein (GP₁₀₀) in nucleated mammalian cells

Cited by 13 publications

References 16 publications

Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.

Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.

Analysis of development and differentiation with tumour cell glycoproteins

The analysis of glycoproteins in cells and tissues by two‐dimensional polyacrylamide gel electrophoresis

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An abundant ubiquitous glycoprotein (GP100) in nucleated mammalian cells

Cited by 13 publications

References 16 publications

Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.

Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.

Analysis of development and differentiation with tumour cell glycoproteins

The analysis of glycoproteins in cells and tissues by two‐dimensional polyacrylamide gel electrophoresis

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An abundant ubiquitous glycoprotein (GP₁₀₀) in nucleated mammalian cells