Characterization of p29, an estrogen-receptor associated tumor marker

Coffer, Arnold I.; King, R. J. B.

doi:10.1016/0022-4731(88)90281-6

Cited by 17 publications

(11 citation statements)

References 11 publications

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“…Hsp27, which is also known as a cytoplasmic estrogen receptor associated protein (p29), selectively binds GTP and to a lesser extent ATP and plays a role in the estrogen response intracellular pathways [33,34]. Our study did not show any correlation between Hsp27 expression and the expression of ER and PR.…”

Section: Discussioncontrasting

confidence: 53%

Hsp-27 Expression in Invasive Ductal Breast Carcinoma

Grzegrzółka¹,

Kurnol

Piotrów

et al. 2012

Folia Histochem Cytobiol.

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Abstract:The aim of this study was to determine the intensity of Hsp27 protein expression in fibrocystic breast changes (FC) and invasive ductal breast carcinoma (IDC) and to examine its impact on patients' clinico-pathological characteristics and overall survival. Immunohistochemical reactions were conducted on archival samples of 20 cases of FC and 101 cases of IDC treated in 1999-2002. Nuclear-cytoplasmic Hsp27 expression was observed in 92 (92.1%) of the examined cases of IDC, and all the cases of FC. Significantly higher Hsp27 expression was observed in G2 (p < 0.01) and G3 cases (p < 0.0001) compared to FC. HER-2 positive cases had higher Hsp27 expression (p = 0.0153), than HER-2 negative cases. Our research showed that Hsp27 could have an impact on tumor malignancy. Moreover, a positive correlation between the expression of Hsp27 and HER-2 positive cases was demonstrated.

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Section: Discussioncontrasting

confidence: 53%

Hsp-27 Expression in Invasive Ductal Breast Carcinoma

Grzegrzółka¹,

Kurnol

Piotrów

et al. 2012

Folia Histochem Cytobiol.

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“…The differences in the molecular weights reported in previous publications could be attributed to differences in the molecular weight standards and to the individual electrophoretic conditions in each laboratory. In fact, there is an overlap in the reported molecular weight for the hsp27 and p29 proteins [1,3,4,9,12]. The lower molecular weight component of hsp27 obtained in our endometrial tumor cytosol due to proteolytic degradation also has the same characteristics as that shown in a study of p29 antigen in MCF-7 cytosol [9].…”

Section: Discussionmentioning

confidence: 54%

“…In addition, the Cll and ER-D5 antibodies revealed the presence of a = 65,000 dalton band in the immunoprecipitate. In cross-linking experiments performed on ZR-75-1 cells it has been shown that p29 protein was associated with a 62,000 dalton protein when the ER-D5 antibody was used [12].…”

Section: Identity Of Hsp27 and P29mentioning

confidence: 99%

“…This protein was first isolated from human myometrium. Under estrogen receptor activating conditions it can be associated with cytosolic estrogen receptor, and it is recognized by a monoclonal antibody termed ER-D5 [11,12]. The distribution of this protein has been studied by immunohistochemistry in several tissues, but the ER-D5 antibody gives good staining in ethanol-based fixatives while the reaction is poor in formalin-fixed material [13,14].…”

Section: Introductionmentioning

confidence: 99%

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Immunological evidence for the identity between the hsp27 estrogen-regulated heat shock protein and the p29 estrogen receptor-associated protein in breast and endometrial cancer

Ciocca

Luque

1991

Breast Cancer Res Tr

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Previous studies have shown several similarities between an estrogen-regulated heat shock protein of 24,000-28,000 daltons (hsp27), and a cytoplasmic estrogen receptor-associated protein of 27,000-29,000 daltons (p29). These proteins have been studied by monoclonal antibodies generated in different laboratories. In the present report we have performed immunocytochemical and immunoblot studies to explore if the monoclonal antibodies against hsp27 (C11) and against p29 (ER-D5) may be identifying the same protein. Breast and endometrial carcinomas and normal endometrial samples were examined by immunocytochemistry (in mirror sections and by double-immunostaining). Identical hsp27 and p29 immunostaining intensity, distribution, and percentage of stained cells was demonstrated by immunocytochemistry. The antigens examined by the two antibodies appeared in the same cells. Cytosols from tumors analyzed by the Western blot technique revealed that the C11 and the ER-D5 antibodies recognized bands with identical electrophoretic mobility. Immunoprecipitation studies with one antibody, C11, followed by Western blot showed that the precipitate was reactive with both antibodies. Identical C11 and ER-D5 reacting spots were observed after blotting proteins separated by high resolution two-dimensional gel electrophoresis. In addition, p29 protein was induced by heat shock in the estrogen receptor negative MDA-MB-231 human breast tumor cell line. These results strongly suggest that the two proteins under investigation are identical.

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“…An immunologic approach was simultaneously pursued to identify 29a-c, in which candidate antibodies for the platelet proteins were used to screen twodimensional immunoblots. D5, a murine monoclonal antibody raised by Coffer et al (16) during attempts to obtain antibody to-the purified estrogen receptor, had been shown to recognize 29-kDa phosphoprotein(s) with characteristics similar to those of the 29-kDa platelet proteins (16,30,31 Two-dimensional immunoblots from 32P-labeled platelets demonstrated precise recognition of the phosphorylated proteins 29a-c by antibody D5 (Fig. 4 Upper).…”

mentioning

confidence: 99%