ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).

Mazzarella, Richard; Green, M

doi:10.1016/s0021-9258(18)47496-0

Cited by 274 publications

(23 citation statements)

References 60 publications

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“…In addition to possessing the same N-terminal sequence, there are other similarities between the heparanase enzyme and the mammalian hsp9o-like proteins mentioned above. The enzyme migrates in SDS/PAGE with an apparent M, of97 000 , near the midpoint of the range of sizes encompassed by grp94, gp96 and ERp99 (nominal Mr values 94000-99000), and all of these proteins are glycosylated (Mazzarella and Green, 1987;. Moreover, the pl range of 5.0-5.2 determined experimentally for the murine heparanase glycoprotein is not far removed from the pl value of 4.5 calculated for the polypeptide component of mature murine ERp99 (Mazzarella and Green, 1987;Devereux et al, 1984).…”

mentioning

confidence: 99%

“…It is worth mentioning that the 23-residue sequence of interest is not present in all members of the hsp90 family; for example, the yeast hsp9o and Escherichia coli HtpG proteins lack approx. 70 residues at the N-terminus relative to their gp96-like counterparts (Mazzarella and Green, 1987;Bardwell and Craig, 1987). Where the sequence does occur, it is preceded in the gene product by a signal sequence.…”

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confidence: 99%

“…Where the sequence does occur, it is preceded in the gene product by a signal sequence. Interestingly, analyses of the DNA-derived amino acid sequences for murine ERp99 and gp96 suggest that removal of the signal peptides should yield N-termini that commence DDEVDVDG... (Mazzarella and Green, 1987;Srivastava et al, 1987;Maki et al, 1990). Although Edman degradation shows that the N-terminus of the ERp99 protein does begin with this sequence (Mazzarella and Green, 1987), the N-termini of murine gp96 and murine melanoma heparanase lack the two N-terminal aspartyl residues (see above).…”

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confidence: 99%

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Tumour rejection antigens of the hsp90 family (gp96) closely resemble tumour-associated heparanase enzymes

Graham

1994

Biochemical Journal

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Tumour rejection antigens of the hsp90 family (gp96) closely resemble tumour-associated heparanase enzymes

Graham

1994

Biochemical Journal

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“…Membros da família Hsp90 clonados e seqüenciados mostraram ser os mais conservados entre todas as famílias de proteínas de estresse (Mazzarella and Green, 1987). Diversos estudos demonstraram que as proteínas da família Hsp90 são as mais abundantes proteínas do estresse de eucariotos (Jakob and Burchner, 1994).…”

Section: Família Hsp90unclassified

“…A proteína associada ao RE é induzida em condições de privação de glicose, devido a este fato, tem sido designado a esta proteína o nome de proteína regulada por glicose. Grp94 também é denominada endoplasmina (Koch et ai., 1986), Erp99 (Mazzarella and Green, 1987) e Gp96 (Maki et ai., 1990). Grp94 é expressa constitutivamente em condições normais de crescimento, mas pode ser induzida por inibidores de glicosilação, cálcio ionofore e drogas que utilizam de nucleotídeos análogos, mas não é significantemente induzida por estímulos térmicos (Schleisinger, 1986).…”

Section: Família Hsp90unclassified

Analise da proliferação celular e expressão de colageno e suas proteinas chaperones, citocinas e metaloproteinas de matriz e seus inibidores teciduais em fibroblastos gengivais de pacientes com fibromatose gengival herditaria

DellaColetta¹

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Distribution of transferrin binding protein immunoreactivity in the chicken central and peripheral nervous systems

et al. 1997

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Transferrin binding protein (TfBP) is a glycoprotein originally purified from chicken oviduct that exhibits transferrin binding activity. Recent work has shown that TfBP is a post-translationally modified form of the heat shock protein (HSP108), the avian homologue of a glucose regulated protein, GRP94. The function of this protein, however, has not yet been clearly defined. Antiserum to TfBP was found to selectively stain oligodendrocytes of the avian brain. In this study, we further describe these oligodendrocytes and other cell types positive to anti-TfBP in the chick nervous system. In accordance with previous studies, the most prominent cell type that labels with antiserum to TfBP is the oligodendrocyte. At the electron microscopic level, the immunoreactive product is confined to the perinuclear cytoplasm and fine processes of the oligodendrocytes, whereas myelin and axoplasm are devoid of staining. The immunoreactive product is found both in the cytoplasmic matrix and bound to the endoplasmic reticulum and plasma membrane, suggesting that TfBP may have properties of both a soluble and an integral membrane protein. There is great variability in the number of TfBP-oligodendrocytes in different areas of the central nervous system (CNS); large numbers of cells are associated with the white matter regions and are found in the myelinated tracts, whereas few cells are present in the gray matter regions. In the retina, TfBP is localized specifically in the cells, that are morphologically oligodendrocytic and is present in the optic nerve fiber layer and the ganglion cell layer. Obvious staining is also seen in the Bergmann glial cells of the cerebellum and in the Schwann cells of the sciatic nerve. Furthermore, the choroid plexus cells similarly exhibit a strong reaction. The association of TfBP in these specific cell types responsible for myelination and sequestering iron and transferrin implies that TfBP may be involved in myelination and iron metabolism of the chick nervous system, perhaps through a role in transferrin concentration in these cells. A putative role of TfBP, as HSP108, is considered.

show abstract

ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).

Cited by 274 publications

References 60 publications

Tumour rejection antigens of the hsp90 family (gp96) closely resemble tumour-associated heparanase enzymes

Tumour rejection antigens of the hsp90 family (gp96) closely resemble tumour-associated heparanase enzymes

Analise da proliferação celular e expressão de colageno e suas proteinas chaperones, citocinas e metaloproteinas de matriz e seus inibidores teciduais em fibroblastos gengivais de pacientes com fibromatose gengival herditaria

Distribution of transferrin binding protein immunoreactivity in the chicken central and peripheral nervous systems

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