Proteomic analysis of normal and malignant prostate tissue to identify novel proteins lost in cancer

Alterations of important protein pathways, including loss of prostate secretory granules, and disruption of the prostatic secretory pathway have been identified as early events in malignancy. In this study, proteomics was used to map the differences in protein expression between normal and malignant prostate tissues and to identify and analyze differentially expressed proteins in human prostate tissue with particular regard to the proteins lost in malignancy.

[1]  J. McNeal,et al.  Identification of the glycosaminoglycan keratan sulfate in the prostatic secretory cell , 2000, The Prostate.

[2]  V. Castronovo,et al.  Alteration of the cytoplasmic/nuclear expression pattern of galectin‐3 correlates with prostate carcinoma progression , 2000 .

[3]  R. Hurst,et al.  Loss of tissue transglutaminase as a biomarker for prostate adenocarcinoma , 2000, Cancer.

[4]  S. Assmann,et al.  Mass spectrometry. An essential tool in proteome analysis. , 2000, Plant physiology.

[5]  Richard D. Smith,et al.  Utility of accurate mass tags for proteome-wide protein identification. , 2000, Analytical chemistry.

[6]  F. España,et al.  Prostate–Specific Antigen Complexed to α1–Antichymotrypsin in the Early Detection of Prostate Cancer , 2000, European Urology.

[7]  L. Dogliotti,et al.  Circulating neuroendocrine markers in patients with prostate carcinoma , 2000, Cancer.

[8]  A. Majeed,et al.  Trends in prostate cancer incidence, mortality and survival in England and Wales 1971–1998 , 2000, BJU international.

[9]  H. Klocker,et al.  Elevated levels of serum secretoneurin in patients with therapy resistant carcinoma of the prostate. , 2000, The Journal of urology.

[10]  M. Rubin,et al.  Neuroendocrine expression in metastatic prostate cancer: evaluation of high throughput tissue microarrays to detect heterogeneous protein expression. , 2000, Human pathology.

[11]  D. Bostwick,et al.  Prostate-specific antigen as a marker of prostate disease , 2000, Virchows Archiv.

[12]  M. Resnick,et al.  Analysis of recent trends in prostate cancer incidence and mortality , 2000, The Prostate.

[13]  J. McNeal,et al.  Luminal contents of benign and malignant prostatic glands: correspondence to altered secretory mechanisms. , 2000, Human pathology.

[14]  H. Mameghan.  Prostate cancer and PSA screening. , 1999, Australian family physician.

[15]  Y. Ben-Ari,et al.  Acidic calponin immunoreactivity in postnatal rat brain and cultures: subcellular localization in growth cones, under the plasma membrane and along actin and glial filaments , 1999, The European journal of neuroscience.

[16]  N. Weigel,et al.  Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. , 1999, Human molecular genetics.

[17]  A. Gown,et al.  Distribution of calponin and smooth muscle myosin heavy chain in fine‐needle aspiration biopsies of the breast , 1999, Diagnostic cytopathology.

[18]  D. Pappin,et al.  The potential use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis — Preliminary findings , 1999, Electrophoresis.

[19]  J. McNeal,et al.  Characterization of cytoplasmic secretory granules (PSG), in prostatic epithelium and their transformation-induced loss in dysplasia and adenocarcinoma. , 1998, Human pathology.

[20]  K. Mori,et al.  Cloning of follistatin-related protein as a novel autoantigen in systemic rheumatic diseases. , 1998, International immunology.

[21]  D. English,et al.  Prostate cancer in Western Australia: trends in incidence and mortality from 1985 to 1996 , 1998, The Medical journal of Australia.

[22]  E. Yeh,et al.  Preferential Modification of Nuclear Proteins by a Novel Ubiquitin-like Molecule* , 1997, The Journal of Biological Chemistry.

[23]  P. Kantoff,et al.  Two differentially expressed genes in normal human prostate tissue and in carcinoma. , 1996, Cancer research.

[24]  H. S. Lee,et al.  Anti-oncogenic effects of tropomyosin: isoform specificity and importance of protein coding sequences. , 1996, Oncogene.

[25]  M. Resnick,et al.  Analysis of prostatic fluid: Evidence for the presence of a prospective marker for prostatic cancer , 1995, The Prostate.

[26]  A. Meikle,et al.  Correlation of serum concentrations of psa‐act complex with total psa in random and serial specimens from patients with bph and prostate cancer , 1995, Journal of clinical laboratory analysis.

[27]  D. Helfman,et al.  The molecular basis for tropomyosin isoform diversity , 1991, BioEssays : news and reviews in molecular, cellular and developmental biology.

[28]  L. Pinna.  Casein kinase 2: an 'eminence grise' in cellular regulation? , 1990, Biochimica et biophysica acta.

[29]  D. Salomon,et al.  Tropomyosins of human mammary epithelial cells: consistent defects of expression in mammary carcinoma cell lines. , 1990, Cancer research.

[30]  B. Cooperman,et al.  Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins. , 1990, The Journal of biological chemistry.

[31]  K L Gould,et al.  Substrate specificity of protein kinase C. Use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements. , 1986, European journal of biochemistry.

[32]  M. El-Maghrabi,et al.  Synthetic peptides corresponding to the site phosphorylated in 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as substrates of cyclic nucleotide-dependent protein kinases. , 1986, The Journal of biological chemistry.

[33]  K. Robson,et al.  Sequence homology between human alpha 1-antichymotrypsin, alpha 1-antitrypsin, and antithrombin III. , 1983, Biochemistry.