Proteomic comparison of prostate cancer cell lines LNCaP-FGC and LNCaP-r reveals heatshock protein 60 as a marker for prostate malignancy

Johansson, Björn; Pourian, Mohammad R.; Chuan, Yin-Choy; Byman, Irene; Bergh, Anders; Pang, See‐Tong; Norstedt, Gunnar; Bergman, Tomas; Pousette, Åke

doi:10.1002/pros.20453

Cited by 38 publications

(19 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As such, the chaperonin has become the subject of studies aiming at determining its precise role as etiologic-pathogenic factor and also aiming at inventing new diagnostic and therapeutic ways centered on it. Adrenal gland Adrenal Cushing's tumor [168] Bladder Transitional cell carcinoma; carcinosarcoma [169][170][171] Bone marrow, blood, lymph nodes Acute myeloid leukemia; Hodgkin's lymphoma [155,[172][173][174] Brain Astroglyoma; glioblastoma; meningioma [175][176][177][178][179] Breast Breast ductal carcinoma [180,181] Esophagus Oesophageal carcinoma [182,183] Large bowel Adenocarcinoma [23,169,[184][185][186][187] Liver Hepatocellular carcinoma [188] Lung Bronchial carcinoma [25,26,189,190] Ovary Serous ovarian cancer [191] Prostate Prostate carcinoma [24,[192][193][194] Stomach Gastric maltoma [195] Uterus Exocervical carcinoma [22,196] Adapted from [2]. ATP synthase [197] Dihydrofolatereductase [37,46] Hsp10 [37,41] Human Carbonicanhydrase II [37,198,…”

Section: Expert Opinionmentioning

confidence: 99%

Hsp60 chaperonopathies and chaperonotherapy: targets and agents

Cappello

Gammazza

Piccionello

et al. 2013

Expert Opinion on Therapeutic Targets

140

133

View full text Add to dashboard Cite

Section: Expert Opinionmentioning

confidence: 99%

Hsp60 chaperonopathies and chaperonotherapy: targets and agents

Cappello

Gammazza

Piccionello

et al. 2013

Expert Opinion on Therapeutic Targets

140

133

View full text Add to dashboard Cite

“…Proteins have been separated by 2D-PAGE, and differentially expressed proteins subsequently identified. Of these, HSP60 (60 kDa heat shock protein) was more abundant in LNCaP-r than LNCaP-FGC cells, showing a correlation with the resistant phenotype (80). Immunohistochemistry studies on prostate tissues demonstrated that prostate epithelial cells showed a moderate to strong HSP60 staining, without any apparent correlation between Gleason grade and staining intensity.…”

Section: Tissue Proteomic-based Molecular Analysis Of Prostate Cancermentioning

confidence: 98%

Application of proteomic technologies for prostate cancer detection, prognosis, and tailored therapy

Fredolini

Liotta

Petricoin

2010

Critical Reviews in Clinical Laboratory Sciences

View full text Add to dashboard Cite

Prostate cancer affects 3 in 10 men over the age of 50 years, and, unfortunately, the clinical course of the disease is poorly predicted. At present, there is no means that can distinguish indolent from aggressive/metastatic tumors. Thus, a personalized clinical approach could be helpful in diagnosing clinically relevant disease and guiding appropriate patient therapy. Individualized medicine requires a deep knowledge of the molecular mechanisms underpinning prostate cancer carcinogenesis. Proteomics may be the most powerful way to uncover biomarkers of detection, prognosis, and prediction, as proteins do the work of the cell and represent the majority of the diagnostic markers and drug targets today. Proteomic technologies are rapidly advancing beyond the two-dimensional gel separation techniques of the past to new types of mass spectrometry and protein microarray analyses. Biological fluids and tissue-cell proteomes from men with prostate cancer are being explored to identify diagnostic and prognostic biomarkers and therapeutic targets using these new proteomic approaches. Traditional and novel proteomic technology and their application to prostate cancer studies in translational research will be presented and discussed in this review. Proteomics coupled with powerful nanotechnology-based biomarker discovery approaches may provide a new and exciting opportunity for body fluid-borne biomarker discovery and characterization. While innovative mass spectrometry technology and nanotrap could be applied to improve the discovery and measurement of biomarkers for the early detection of prostate cancer, the use of tissue proteomic tools such as the reverse-phase protein microarray may provide new approaches for personalization of therapies tailored to each tumor's unique pathway activation network.

show abstract

“…Comparative proteomic studies using 2-D gel electrophoresis coupled to mass spectrometric identification has been applied in studies of various cancers, including hepatomas [4] , lung cancer [5] , prostate [6] , and ovarian cancers [7] . The search for markers and vaccines at the protein level is more reliable than at the transcriptional level, as the translation process is often unpredictable and the spatiotemporal in situ localization of a given protein is not often correlated with its in situ expression pattern [8] .…”

Section: Introductionmentioning

confidence: 99%

Comparative proteomic analysis of human osteosarcoma and SV40-immortalized normal osteoblastic cell lines

Guo

Shen

Jin

et al. 2007

Acta Pharmacologica Sinica

View full text Add to dashboard Cite

Aim: Comparative proteomics provide a powerful approach in screening for alterations in protein levels and post‐translational modifications that are associated with tumors. In the present study, we aimed to identify candidate biomarkers to distinguish osteosarcoma (OS) cells from normal osteoblastic cells. Methods: We employed 3 OS cell lines (U2OS, IOR/OS9, and SaOS‐2), and used the SV40‐immortalized normal osteoblastic cell line (hFOB1.19) as the control. The differential protein levels in OS and osteoblastic cells were identified using 2‐D gel electrophoresis followed by matrix‐assisted laser desorption/ionization‐time of flight mass spectrometry analyses. Two proteins of interest, the levels of which were significantly increased in OS cells, were further characterized by Western blot analyses. Results: Twenty‐six proteins were identified, the expression level of which was either significantly increased or decreased in the OS cells as compared to the control cells. The expression level of the activator of 90 kDa shock protein ATPase homolog 1 (AHA1), was enhanced 12.4‐, 24.1‐, and 23.8‐fold in SaOS‐2, IOR/OS9, and U2OS cells, respectively, and the level of the stomatin‐like protein 2 (SLP‐2) was increased by 10.4‐ and 7.8‐fold in IOR/OS9 and U2OS cells, respectively, as compared to normal osteoblastic cells. Those observations were confirmed by Western blot analyses. Conclusion: A differential proteomic analysis was successfully used to identify AHA1 and SLP‐2 that were significantly overproduced in OS cells as compared to normal osteoblastic cells, suggesting that those proteins among others may be effective biomarker candidates for the identification of OS cells.

show abstract

Proteomic comparison of prostate cancer cell lines LNCaP-FGC and LNCaP-r reveals heatshock protein 60 as a marker for prostate malignancy

Cited by 38 publications

References 28 publications

Hsp60 chaperonopathies and chaperonotherapy: targets and agents

Hsp60 chaperonopathies and chaperonotherapy: targets and agents

Application of proteomic technologies for prostate cancer detection, prognosis, and tailored therapy

Comparative proteomic analysis of human osteosarcoma and SV40-immortalized normal osteoblastic cell lines

Contact Info

Product

Resources

About