PubMed Health⌕ Search

Biomedical subjects

C Melle

Publications and source records attributed to C Melle.

5 recordsLinked to original sources
PubMed2005

ProteinChip technology reveals distinctive protein expression profiles in the urine of bladder cancer patients.

OBJECTIVE: Since accurate biomarkers for the early diagnosis or individual prognosis of the bladder carcinoma are still not available, we used the ProteinChip technology, to search for discriminating protein expressions associated with this cancer and its subtypes. METHODS: A training set consisting of 30 archival urine samples from bladder carcinoma patients and 30 urinary samples from healthy volunteers, was analyzed via ProteinChip technology and computer based data mining. Mass clusters of differentially expressed proteins were verified by a second set (test set) comprising 21 bladder carcinoma urine samples and 21 non-tumor urinary samples. Expression differences between carcinoma subtype sample groups of the initial training set were assessed by a trend test. RESULTS: Bladder carcinoma was segregated from control with a sensitivity and specificity of 80% and 90 to 97% in the trainings set, as well as 52 to 57% and 57 to 62% in the test set, respectively. Segregation of pooled tumor stages pT2-pT3 from stages pT1 and pTa was possible at the 53.3 kDa cluster of the CM10-chip array data derived rule base. CONCLUSION: ProteinChip technology together with adapted computer based data mining tools are useful for the rapid establishment of potential protein biomarkers.

Biomarkers, Tumor↗
PubMed1999

Surface plasmon resonance measurements reveal stable complex formation between p53 and DNA polymerase alpha.

Surface plasmon resonance measurements were used for detecting and quantifying protein-protein interactions between the tumor suppressor protein p53, the SV40 large T antigen (T-ag), the cellular DNA polymerase alpha-primase complex (pol-prim), and the cellular single-strand DNA binding protein RPA. Highly purified p53 protein bound to immobilized T-ag with an apparent binding constant of 2 x 10(8) M(-1). Binding of p53 to RPA was in the same order of magnitude with a binding constant of 4 x 10(8) M(-1), when RPA was coupled to the sensor chip via its smallest subunit, and 1 x 10(8) M(-1), when RPA was coupled via its p70 subunit. Furthermore, p53 bound human DNA polymerase alpha-primase complex (pol-prim) with a K(A) value of 1 x 10(10) m(-1). Both the p68 subunit and the p180 subunit of pol-prim could interact with p53 displaying binding constants of 2 x 10(10) m1(-1) and 5 X 10(9) M(-1), respectively. Complex formation was also observed with a p180/p68 heterodimer, and again with a binding constant similar. Hence, there was no synergistic effect when p53 bound to higher order complexes of pol-prim. A truncated form of p53, consisting of amino acids 1-320, bound pol-prim by four orders of magnitude less efficiently. Therefore, an intact C-terminus of p53 seems to be important for efficient binding to pol-prim. It was also tried to measure complex formation between p53, pol-prim, and T-ag. However there was no evidence for the existence of a ternary complex consisting of T-ag, pol-prim, and p53.

Animals↗
PubMed1977

[Breast cancer].

Explore the source record for details and available documents.

Adolescent↗
PubMedDate not supplied

ProteinChip system technology: a powerful tool to analyze expression differences in tissue-engineered blood vessels.

At the time of implantation, tissue-engineered constructs should resemble native tissues as closely as possible. At present, histology and biochemical methods are commonly used to compare tissue-engineered constructs with native tissue. A ProteinChip system based on surface-enhanced laser desorption/ionization time of flight mass spectrometry (SELDI) has been developed that allows visualization of complex protein profiles from biological samples. The aim of this study was to determine whether the ProteinChip system is a suitable tool with which to compare the protein expression profiles of tissue-engineered aortic blood vessels with native tissues. Tissue-engineered blood vessel substitutes were fabricated with poly-4-hydroxybutyrate scaffolds, ovine vascular cell seeding, and dynamic tissue culture conditions. Engineered, ovine aortic, and carotid tissues were homogenized and total protein was extracted. Samples were analyzed on ProteinChip arrays. Analysis yielded reproducible protein profiles from all samples. About 150 distinct protein peaks were detected. Comparative analysis with ProteinChip software revealed that the protein profiles from native aorta and native carotid arteries were similar whereas early tissue-engineered samples displayed more distinct deviations. In conclusion, ProteinChip system technology is rapid, reproducible, and highly sensitive in highlighting differentially expressed proteins in tissue-engineered blood vessel substitutes.

Animals↗