Publications from 2008

First author from Finsen Laboratory

Illemann, M., Bird, N., Majeed, A., Lærum, O.D., Lund, L.R., Danø, K. and Nielsen, B.S.:
Two Distinct Expession Patterns of Urokinase, Urokinase Receptor and Plasminogen Activator Inhibitor-1 in Colon Cancer Liver Metastases.
International Journal of Cancer, 124: 1860-1870.

Lund, I.K., Jögi, A., Rønø, B., Lund, L.R., Almholt, K., Gårdsvoll, H., Behrendt, N., Rømer, J. and Høyer-Hansen, G.:
Antibody-mediated targeting of the uPA proteolytic function. Neutralizes fibrinolysis in vivo.
J.Biol. Chem. 283: 32506-15.

Johansen, J.S., Lottenburger, T., Nielsen, H.J., Jensen, J.E.B., Svendsen, M.N., Kollerup, G. and Christensen, I.J.:
Diurnal, Weekly and Long Time Variation in Serum Concentrations of YKL-40 in Healthy Subjects.
Cancer Epidemiology, Biomarkers & Prevention, 17: 2603-8.

Rasch, M.G., Pass, J., Illemann, M., Høyer-Hansen, G. and Lund, I.K.:
Discrimination of different forms of the murine urokinase receptor on the cell surface using monoclonal antibodies.
J. Immunol. Meth., 339: 55-65.

Almholt, K., Juncker-Jensen, A., Green, K.A., Solberg, H., Lund, L.R. & Rømer, J.:
The plasminogen activation system in tissue remodelling and cancer invasion.
In The Cancer Degradome: Proteases and Cancer Biology.
Eds. Edwards, D., Høyer-Hansen, G., Blasi, F., Sloane, B.F.
Springer Verlag. Chapter 11.

Hillig, T., Engelholm, L.H. and Behrendt, N.:
The Endocytic Collagen Receptor, uPARAP/Endo180, in Cancer Invasion and Tissue Remodeling.
In The Cancer Degradome: Proteases and Cancer Biology
Eds. Edwards, D., Høyer-Hansen, G., Blasi, F., and Sloane, B.F.
Springer Verlag. Chapter 13.

Christensen, I.J., Pappot, H. and Høyer-Hansen, G.:
The plasminogen activation system as a source of prognostic markers in cancer.
In The Cancer Degradome: Proteases and Cancer Biology.
Eds. Edwards, D., Høyer-Hansen, G., Blasi, F., Sloane, B.F.
Springer Verlag. Chapter 28.

Jacobsen, B., Kjaergaard, M., Gårdsvoll, H. & Ploug, M.:
StStructure and inhibition of the urokinase-type plasminiogen activator receptor (uPAR).
In The Cancer Degradome: Proteases and Cancer Biology.
Eds. Edwards, D., Høyer-Hansen, G., Blasi, F., Sloane, B.F.
Springer Verlag. Chapter 34.

Almholt, K., Juncker-Jensen, A., Lærum, O.D., Danø, K., Johnsen, M., Lund, L.R. and Rømer, J.:
Metastasis is strongly reduced by the matrix metalloprotease inhibitor galardin in the MMTV-PymT transgenic breast cancer model.
Mol. Cancer Ther., 7: 2758-2767.

Hansen, L.V., Lærum, O.D., Illemann, M., Nielsen, B.S. and Ploug, M.: Altered expression of the urokinase receptor homologue, C4.4A in invasive areas of human esophageal squamous cell carcinoma.
Int. J. Cancer, 122: 734-741.

Rasch, M.G., Lund, I.K., Almasi, C.E. and Hoyer-Hansen, G.:
Intact and cleaved uPAR forms: diagnostic and prognostic value in cancer.
Front Biosci. 13: 6752-62.

Hillig, T., Engelholm, L.H., Ingvarsen, S., Madsen, D.H., Gårdsvoll, H., Larsen, J.K., Ploug, M., Danø, K., Kjøller, L. and Behrendt, N.:
A composite role of vitronectin and urokinase in the modulation of cell morphology upon expression of the urokinase receptor.
J.Biol.Chem. , 283: 15217-15223.

Kjaergaard, M., Hansen, L.V., Jacobsen, B., Gårdsvoll, H. and Ploug, M.:
Structure and ligand interactions of the urokinase receptor (uPAR).
Frontiers in Bioscience, 13: 5441-5461.

Green, K.A., Almholt, K.A., Ploug, M., Rønø, B., Johnsen, M., Castellino, F.J., Bugge, T.H., Rømer, J., and Lund, L.R.:
Pro-fibrinolytic effects of metalloproteinases during skin wound healing in the absence of plasminogen.
J. Invest. Dermatol., , 128: 2092-2101.

Nielsen, B.S., Egeblad, M., Rank, F., Askautrud, H.A., Pennington, C.J., Pedersen, T.X., Christensen, I.J., Edwards, D.R., Werb, Z. and Lund, L.R.: Matrix Metalloproteinase 13 is Induced in Fibroblasts in Polyoma Middle T Oncogenenduced Invasive Mammary Tumor, but Does Not Influence Progression. -i
PLoS ONE, 3: e2959.

Laerum, O.D., Illemann, M., Skarstein, A., Helgeland, L., Øvfrebø, K., Danø, K., and Nielsen, B.S.:
Chrohn`s disease but not chronic ulcerative colitis induces the expression of PAI-1 in enteric neurons.
Am. J. Gastroenterology, 103: 2350–2358

Ingvarsen, S., Madsen, D.H., Hillig, T., Lund, L.R., Holmbeck, K., Behrendt, N. and Engelholm, L.H.:
Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the the 72 kDa gelatinase, MMP-2, on fibroblasts and fibrosarcoma cells.
Biol.Chem., 389: 943 - 953.

Jacobsen, B. and Ploug, M.:
The urokinase receptor and its structural homologue C4.4A in cancer. Expression, prognosis and pharmacological inhibition.
Current Medicinal Chemistry, 15: 2559-73..


Joint publications with co-author from Finsen Laboratory

Backe, N., Rand K.D., Roepstorff, P., Ploug, M., and Jørgensen, T.J.D.:
Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry.
J Am Soc Mass Spectrom. 19: 1719-25.

Petri, A.L., Høgdall, C., Christensen, I.J., Simonsen, A.H., T’Jampens, D., Hellmann, M.-L., Kjaer, S.K., Fung, E.T. and Høgdall, E.:
Sample handling for mass spectrometric proteomic investigations of human urine.
Proteomics Clin. Appl. In press

Marquard, L., Gjerdrum, L.M., Christensen, I.J., Jensen, P.B., Sehested, M. and Ralfkiaer, E.:
Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma.
Histopathology. 53: 267-77.

Ytting, H., Christensen, I.J., Thiel, S., Jensenius, J.C. and Nielsen, H.J.:
Pre- and postoperative levels in serum of mannan-binding lectin associated serine protease-2 —a prognostic marker in colorectal cancer.
Human Immunology. 69: 414–420.

Schrohl, A.-S., Mueller, V., Christensen, I.J., Pantel, K., Thomssen, C. and Bruenner, N.:
A comparative study of Tissue Inhibitor of Metalloproteinases-1 levels in plasma and tumour tissue from patients with primary breast cancer and in plasma from patients with metastatic breast cancer.
Tumour Biol. 29: 181-187.

Frederiksen, C.B., Lomholt, A.F., Lottenburger, T., Davis, G.J., Dowell, B.L., Blankenstein, M.A., Christensen, I.J., Brünner, N. and Nielsen, H.J.:
Assessment of the biological variation of plasma tissue inhibitor of metalloproteinases-1.
The International Journal of Biological Markers, 23: 42-47.

Knudsen, L.S., Chistensen, I.J., Lottenburger, T., Svendsen, M.N., Nielsen, H.J., Nielsen, L., Petersen, K.H., Jensen, J.E.B., Kollerup, G. and Johansen, J.S.:
Pre-Analytical and biological variability in circulating IL-6 in healthy subjects and patients with rheumatoid arthritis.
Biomarkers. 13: 59-78.

Blacher, S., Jost, M., Melen, L., Lund, L.R., Rømer, J., Foidart, J.M., and Noël, A.:
Quantification of in vivo tumor invasion and vascularisation by computerized image analysis.
Microvascular Res. 75: 169-178.

Dejligbjerg, M., Grauslund, M., Christensen, I.J., Tjørnelund, J., Buhl Jensen, P. and Sehested, M.:
Identification of predictive biomarkers for the histone deacetylase inhibitor belinostat in a panel of human cancer cell lines.
Cancer Biomark. 4: 101-9.

Nøjgaard, C., Høst, N.B., Christensen, I.J., Poulsen, S.H., Egstrup, K., Price, P.A. and Johansen, J.S.:
Serum levels of YKL-40 increases in patients with acute myocardial infarction.
Coron Artery Dis. 19: 257-263.

Rasmussen, B.B., Andersson, M., Christensen, I.J. and Møller, S.:
Evaluation of and quality assurance in HER2 analysis in breast carcinomas from patients registered in Danish Breast Cancer Group (DBCG) in the period of 2002-2006. A nationwide study including correlation between HER-2 status and other prognostic variables.
Acta Oncol. 47: 784-8.

Schjoldager, K. T.-B.,G., Maltesen. H.R., Lund, L.R., Claesson, M.H., Sjöström, H., Troelsen, J.T., and Olsen J.:
Cellular cross-talk in the small intestinal mucosa: Postnatal lymphocytic immigration elicits a specific epithelial transcriptional response.
Am. J. Physiol., , Gastrointestinal. Liver Physiol. 294: G1335-G1343..

Larsen, A.K., Lametsch, R., Elce, J.S., Larsen, J.K., Thomsen, B., Larsen, M.R., Lawson, M.A., Greer, P.A. and Ertbjerg, P.:
Genetic disruption of calpain correlates with loss of membrane blebbing and differential expression of RhoGDI-1, cofilin and tropomyosin 1.
Biochemical J. 411: 657-666.

Talman, M.L., Rasmussen, B.B., Andersen, J. and Christensen, I.J.:
Estrogen Receptor analyses in the Danish Breast Cancer Cooperative Group. History, methods, prognosis and clinical implications.
Acta. Oncol., 47: 789-94.

Alyahya, G.A., Kolko, M., Prause, J.U., Nielsen, B.S., Wang, J. and Heegaard, S.:
Matrix metalloproteinase-2 is expressed in melanoma-associated spongiform scleropathy.
Invest Ophthalmol Vis Sci., 49: 2806-11.

Bülow, S., Bülow, C., Vasen, H., Järvinen, H., Björk, J. and Christensen, I.J.:
Colectomy and Ileorectal Anastomosis is still an Option for Selected Patients with Familial Adenomatous Polyposis.
Dis Colon Rectum, 51: 1318-23.

Li, Z.-B., Niu, G, Wang, H., He, L., Yang, L., Ploug, M., and Chen, X.:
Imaging of Urokinase-type Plasminogen Activator Receptor ExpressionUsing a 64Cu-Labeled Linear Peptide Antagonist by microPET.
Clin Cancer Res., 14: 4758 - 4766.

Bache, N., Rand, K.D., Roepstorff, P., Ploug, M. and Jørgensen, T.J.D.:
Hydrogen Atom Scrambling in Selectively Labeled Anionic Peptides Upon Collisional Activation by MALDI Tandem Time-of-Flight Mass Spectrometry.
J Am Soc Mass Spectrom., 19: 1719-25.

Iversen, L.H., Bülow, s., Christensen, I.J., Laurberg, S. and Harling, H.:
Postoperative medical complications are the main cause of early death after emergency surgery for colon cancer. A Nationwide study.
British J. Surgey. 95: 1012-1019.

Henic, E., Borgfeldt, C., Christensen, I. J., Casslén, B. and Høyer-Hansen, G.:
Cleaved forms of the urokinase plasminogen activator receptor in plasma enhance discrimination of benign from malignant disease and predict survival in patients with ovarian cancer.
Clin. Cancer Res., 14: 5785-5793.

Sørensen, N.M., Schrohl, A.S., Jensen, V., Christensen, I.J., Nielsen, H.J., Brünner, N.:
Comparative studies of tissue inhibitor of metalloproteinases-1 in plasma, serum and tumour tissue extracts from patients with primary colorectal cancer.
Scand. J. Gastroenterol. 43: 186-91.