Stage-dependent increase of orosomucoid and zinc-alpha2-glycoprotein in urinary bladder cancer

Irmak, Ster; Tilki, Derya; Heukeshoven, Jochen; Oliveira‐Ferrer, Leticia; Friedrich, Martin; Huland, Hartwig; Ergün, Süleyman

doi:10.1002/pmic.200402005

Cited by 81 publications

(71 citation statements)

References 36 publications

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“…Although the exact mechanism by which ZAG actively participates in tumor proliferation is not known, a large body of data exists in favor of the expression of ZAG with respect to the stages of tumor (39)(40)(41)(42). ZAG is designated as a potential biomarker of different types of carcinomas (6,7,27,35,38,(43)(44)(45)(46).…”

Section: Zag As a Biomarkermentioning

confidence: 99%

Zinc α2-Glycoprotein: A Multidisciplinary Protein

Hassan

Waheed

Yadav

et al. 2008

Molecular Cancer Research

216

204

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Zinc A2-glycoprotein (ZAG) is a protein of interest because of its ability to play many important functions in the human body, including fertilization and lipid mobilization. After the discovery of this molecule, during the last 5 decades, various studies have been documented on its structure and functions, but still, it is considered as a protein with an unknown function. Its expression is regulated by glucocorticoids. Due to its high sequence homology with lipid-mobilizing factor and high expression in cancer cachexia, it is considered as a novel adipokine. On the other hand, structural organization and fold is similar to MHC class I antigen-presenting molecule; hence, ZAG may have a role in the expression of the immune response. The function of ZAG under physiologic and cancerous conditions remains mysterious but is considered as a tumor biomarker for various carcinomas. There are several unrelated functions that are attributed to ZAG, such as RNase activity, regulation of melanin production, hindering tumor proliferation, and transport of nephritic by-products. This article deals with the discussion of the major aspects of ZAG from its gene structure to function and metabolism. (Mol Cancer Res 2008;6(6):892 -906)

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Section: Zag As a Biomarkermentioning

confidence: 99%

Zinc α2-Glycoprotein: A Multidisciplinary Protein

Hassan

Waheed

Yadav

et al. 2008

Molecular Cancer Research

216

204

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“…16 ZAG is overexpressed by several types of malignant tumors, such as cancers of breast, prostate, bladder and lung. [17][18][19][20] As serum ZAG levels are elevated in patients with prostate 18,21 and cervical 22 cancers, ZAG has been proposed to serve as a potential biomarker for these carcinomas.…”

Section: Introductionmentioning

confidence: 99%

Zinc-α2-glycoprotein: an adipokine modulator of body fat mass?

et al. 2010

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The importance of white adipose tissue in the control of energy balance is now firmly recognized. In addition to fuel storage, adipocytes secrete an array of proteins factors (adipokines), which regulate multiple physiological and metabolic processes as well as influence body fat accumulation. Zinc-a2-glycoprotein (ZAG), a lipid mobilizing factor initially characterized as a tumor product associated with cachexia, has recently been identified as a novel adipokine. Although the exact role of ZAG in adipose tissue remains to be clarified, there is evidence that ZAG expression appears to be inversely related to adiposity, being upregulated in cachexia whereas reduced in obesity. Investigations on the regulation of ZAG give insights into its potential function in adipose tissue with a link to lipid mobilization and an anti-inflammatory action. Recent work shows that ZAG stimulates adiponectin secretion by human adipocytes. Data from genetic studies suggest that ZAG may be a candidate gene for body weight regulation; this is supported by the demonstration that ZAG-knockout mice are susceptible to weight gain, whereas transgenic mice overexpressing ZAG exhibit weight loss. The present review summarizes these new perspectives of ZAG and the potential mechanisms by which it might modulate adipose tissue mass and function.

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“…For example, a-1-acid glycoprotein, a-1-microglobulin, prostaglandin-H 2 -D-isomerase, inter-a trypsin inhibitor, kinninogen and zinc-a-2-glycoprotein were all identified in the sediments, and have been reported in the literature as biomarkers for various diseases [18][19][20][21][22][23]. These diseases range from liver fibrosis, bladder cancer, prostate cancer, and Hodgkin's disease to urinary tract infections and more.…”

Section: Analysis Of the Sediment Proteome Has Implications For Biomamentioning

confidence: 98%

A qualitative proteome investigation of the sediment portion of human urine: Implications in the biomarker discovery process

Mataija-Botelho¹,

Murphy²,

Pinto³

et al. 2009

Proteomics Clinical Apps

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Inherent to the biomarker discovery process is a comparative analysis of physiological states. It is therefore critical that the proteome detection protocol does not bias the analysis. With urine, the sediment portion, obtained upon thawing frozen urine, is routinely discarded prior to proteome analysis. However, our results demonstrate that such a practice inadvertently induces bias, having significant implications in the biomarker discovery process. We present the first proteome investigation of human urinary sediments, identifying 60 proteins in this phase by MS. Many sediment proteins were also detected in the urinary supernatant, indicating that several proteins partition between the two phases. This partitioning is dependant on the pH of the sample, as well as the degree of sample agitation. As a consequence of discarding the sediment portion of urine, the concentration of potential candidate biomarkers in the supernatant phase will be altered or, in other instances, may be completely removed from the sample. To minimize this, the pH of all samples should first be normalized, and the samples vigorously vortexed prior to discarding the sediments. For more comprehensive biomarker investigations, we suggest that urinary sediments be analyzed along with the supernatant proteins.

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Stage-dependent increase of orosomucoid and zinc-alpha2-glycoprotein in urinary bladder cancer

Cited by 81 publications

References 36 publications

Zinc α2-Glycoprotein: A Multidisciplinary Protein

Zinc α2-Glycoprotein: A Multidisciplinary Protein

Zinc-α2-glycoprotein: an adipokine modulator of body fat mass?

A qualitative proteome investigation of the sediment portion of human urine: Implications in the biomarker discovery process

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