Identification of Potential Tumor Differentiation Factor (TDF) Receptor from Steroid-responsive and Steroid-resistant Breast Cancer Cells

Sokolowska, Izabela; Woods, Alisa G.; Gawinowicz, Mary Ann; Roy, Urmi; Darie, Costel C.

doi:10.1074/jbc.m111.284091

Cited by 54 publications

(64 citation statements)

References 77 publications

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“…The biological activity of TDF on breast and prostate cancer cells has not been reproduced by any other growth factors or pituitary hormones. Its secretion from the pituitary into the bloodstream and its differentiation activity on breast and prostate cancer cells suggest that TDF may have an endocrine role [3].…”

Section: Introductionmentioning

confidence: 99%

“…To shed some light into TDF's function, our laboratory isolated and characterized potential TDF receptor (TDF-R) candidates from breast cancer cell lines, nonbreast cancer cell lines, and from fibroblasts [3], [4]. We concluded that TDF-R candidates are members of the 70 kDa heat shock protein family (HSP70).…”

Section: Introductionmentioning

confidence: 99%

“…The molecular mechanism through which TDF induces cell differentiation is not known [1][2][3][4]. To shed some light into TDF's function, our laboratory isolated and characterized potential TDF receptor (TDF-R) candidates from breast cancer cell lines, nonbreast cancer cell lines, and from fibroblasts [3], [4].…”

Section: Introductionmentioning

confidence: 99%

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Structural investigation of tumor differentiation factor

Roy¹,

Sokolowska²,

Woods

et al. 2012

Biotech and App Biochem

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Abstract.Tumor differentiation factor (TDF) is a 17 kDa protein produced by the pituitary and secreted into the bloodstream, with no definitive function and incomplete characterization. TDF has the following four cysteine (Cys) residues: Cys17, Cys70, Cys97, and Cys98. To understand the function of TDF, we (1) overexpressed and characterized recombinant TDF (rTDF); (2) investigated native, secreted TDF; and (3) assessed potential disulfide connectivities using molecular modeling. Our results from Western blotting (WB) experiments suggest that rTDF is mostly expressed as insoluble, monomeric, and dimeric forms. Mass spectrometry analysis of the overexpressed rTDF identified a peptide that is a part of TDF protein. WB of the native, secreted TDF detected it as a 50 kDa band. In addition, investigation of TDF by molecular modeling suggests that the Cys residues may form disulfide bridges between Cys17-Cys98 and Cys70-Cys17.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structural investigation of tumor differentiation factor

Roy¹,

Sokolowska²,

Woods

et al. 2012

Biotech and App Biochem

Self Cite

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“…MS-based proteomics methods [13,20,21,[27][28][29][30]. The first step in a proteomics experiment is sample fractionation, which can be done by non-denaturing biochemical approaches such as chromatography or centrifugation, or by denaturing methods such as acetone precipitation or electrophoresis (Figure 2).…”

Section: Introductionmentioning

confidence: 99%

“…MS is a method that can reliably and comprehensively identify proteins and putative biomarkers [4,5,[12][13][14][15][16][17][18][19][20][21][22]. MS is already in use for newborn screening for several other disorders, including phenylketonuria, congenital hypothyroidism and cystic fibrosis [23].…”

Section: Introductionmentioning

confidence: 99%

The Potential for Proteomics in Understanding Neurodevelopmental Disorders

Wormwood¹,

Sokolowska

Ryan

et al. 2015

J Proteomics Bioinform

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Disulfide proteomics for identification of extracellular or secreted proteins

et al. 2012

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The combination of SDS-PAGE and MS is one of the most powerful and perhaps most frequently used gel-based proteomics approaches in protein identification. However, one drawback of this method is that separation takes place under denaturing and reducing (R) conditions and as a consequence, all proteins with identical apparent molecular mass (Mr) will run together. Therefore, low-abundant proteins may not be easily identified. Another way of investigating proteins by proteomics is by analyzing subproteomes from a total proteome such as phosphoproteomics, glycoproteomics, or disulfide proteomics. Here, we took advantage of the property of secreted proteins to form disulfide bridges and investigated disulfide-linked proteins, using SDS-PAGE under nonreducing (NR) conditions. We separated sera from normal subjects and from patients with various diseases by SDS-PAGE (NR) and (R) conditions, followed by LC-MS/MS analysis. Although we did not see any detectable difference between the sera separated by SDS-PAGE(R), we could easily identify the disulfide-linked proteins separated by SDS-PAGE (NR). LC-MS/MS analysis of the disulfide-linked proteins correctly identified haptoglobin (Hp), a disulfide-linked protein usually found as a heterotetramer or as a disulfide-linked heteropolymer. Western blotting under NR and R conditions using anti-Hp antibodies confirmed the LC-MS/MS experiments and further confirmed that upon reduction, the disulfide-linked Hp heterotetramers and polymers were no longer disulfide-linked polymers. These data suggest that simply by separating samples on SDS-PAGEunder NR conditions, a different, new proteomics subset can be revealed and then identified.

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Identification of Potential Tumor Differentiation Factor (TDF) Receptor from Steroid-responsive and Steroid-resistant Breast Cancer Cells

Cited by 54 publications

References 77 publications

Structural investigation of tumor differentiation factor

Structural investigation of tumor differentiation factor

The Potential for Proteomics in Understanding Neurodevelopmental Disorders

Disulfide proteomics for identification of extracellular or secreted proteins

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