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Angiogenic Protein

The Experts below are selected from a list of 195 Experts worldwide ranked by ideXlab platform

Calvin P. H. Vary – 1st expert on this subject based on the ideXlab platform

  • Cancer incidence in patients with hereditary hemorrhagic telangiectasia
    Journal of Cancer Research and Clinical Oncology, 2017
    Co-Authors: C.w. Duarte, A.w. Black, F L Lucas, Calvin P. H. Vary

    Abstract:

    © 2016, Springer-Verlag Berlin Heidelberg. Purpose: Hereditary hemorrhagic telangiectasia (HHT) is a genetic disorder characterized by deficiency in endoglin, an Angiogenic Protein. We previously showed that HHT, in which systemic endoglin expression is reduced, was associated with better survival outcomes in cancer patients (Duarte et al. in Cancer Epidemiol Biomarkers Prev 23:117–125, 2014). Here, we evaluated whether HHT was associated with reduced cancer incidence. Methods: A matched case–control analysis using SEER Medicare was conducted to evaluate the effect of HHT on diagnosis with breast, colorectal, lung, or prostate cancer between 2000 and 2007 (n = 633,162). Cancer and non-cancer patients were matched on age, sex, SEER registry region, and length of the ascertainment period for HHT. We assessed crude association using a McNemar’s test and then adjusted for demographic variables, cancer type, cancer stage, comorbidities, and ascertainment period with a conditional logistic regression model for cancer incidence. Results: The McNemar’s test showed no significant association between HHT and cancer incidence (p = 0.74). Adjusting for covariates with the conditional logistic regression model did not change the result [HHT odds ratio 0.978; 95 % CI (0.795, 1.204)]. The lack of association between HHT and cancer incidence is unexpected given the previously discovered significant association between HHT and improved survival outcomes (Duarte et al. in Cancer Epidemiol Biomarkers Prev 23:117–125, 2014). Conclusions: We conclude that the protective effect of reduced systemic endoglin expression in cancer is specific to cancer progression through its effect on vascularization and other stromal effects but does not extend to cancer initiation.

  • Cancer incidence in patients with hereditary hemorrhagic telangiectasia
    Journal of Cancer Research and Clinical Oncology, 2016
    Co-Authors: C.w. Duarte, A.w. Black, F L Lucas, Calvin P. H. Vary

    Abstract:

    Purpose
    Hereditary hemorrhagic telangiectasia (HHT) is a genetic disorder characterized by deficiency in endoglin, an Angiogenic Protein. We previously showed that HHT, in which systemic endoglin expression is reduced, was associated with better survival outcomes in cancer patients (Duarte et al. in Cancer Epidemiol Biomarkers Prev 23:117–125, 2014). Here, we evaluated whether HHT was associated with reduced cancer incidence.

Bert L Vallee – 2nd expert on this subject based on the ideXlab platform

  • An Angiogenic Protein from Bovine Serum and Milk — Purification and Primary Structure of Angiogenin-2
    FEBS Journal, 1997
    Co-Authors: Daniel J Strydom, Michael D Bond, Bert L Vallee

    Abstract:

    Bovine serum and milk contain a basic Angiogenic Protein that binds tightly to placental ribonuclease inhibitor. It was purified from both sources by ion-exchange and reversed-phase chromatographies. Its amino acid sequence revealed that it is a member of the ribonuclease superfamily. It contains 123 amino acids in a single polypeptide chain, is cross-linked by three disulfide bonds, is glycosylated at Asn33, and is 57% identical to bovine angiogenin. The amino-terminal and carboxyl terminal residues are pyroglutamic acid and proline, respectively. The Protein has ribonucleolytic activity that is similar to, but somewhat lower than, that of bovine angiogenin, i.e. very low relative to RNase. It is Angiogenically potent on chicken chorioallantoic membrane, but less so than angiogenin. The sequence and activities demonstrate that this Protein is a second, distinct, member of the angiogenin sub-family of pancreatic ribonucleases, and is referred to as angiogenin-2.

  • an Angiogenic Protein from bovine serum and milk purification and primary structure of angiogenin 2
    FEBS Journal, 1997
    Co-Authors: Daniel J Strydom, Michael D Bond, Bert L Vallee

    Abstract:

    Bovine serum and milk contain a basic Angiogenic Protein that binds tightly to placental ribonuclease inhibitor. It was purified from both sources by ion-exchange and reversed-phase chromatographies. Its amino acid sequence revealed that it is a member of the ribonuclease superfamily. It contains 123 amino acids in a single polypeptide chain, is cross-linked by three disulfide bonds, is glycosylated at Asn33, and is 57% identical to bovine angiogenin. The amino-terminal and carboxyl terminal residues are pyroglutamic acid and proline, respectively. The Protein has ribonucleolytic activity that is similar to, but somewhat lower than, that of bovine angiogenin, i.e. very low relative to RNase. It is Angiogenically potent on chicken chorioallantoic membrane, but less so than angiogenin. The sequence and activities demonstrate that this Protein is a second, distinct, member of the angiogenin sub-family of pancreatic ribonucleases, and is referred to as angiogenin-2.

K R Acharya – 3rd expert on this subject based on the ideXlab platform

  • biological and structural features of murine angiogenin 4 an Angiogenic Protein
    Biochemistry, 2007
    Co-Authors: Benedict Crabtree, D E Holloway, Matthew Douglas Baker, K R Acharya, Vasanta Subramanian

    Abstract:

    Murine angiogenin-4 (mAng-4) is a member of the pancreatic ribonuclease superfamily that is expressed in some endodermally derived organs. We now show that mAng-4 is Angiogenic using a thoracic aorta assay never before applied to the angiogenins. mAng-4, human angiogenin (hAng), and murine angiogenin-1 (mAng-1) stimulate the proliferation of IGR1 melanoma cells but do not stimulate the proliferation or migration of bovine corneal endothelial cells or primary mouse embryonic fibroblasts. In addition, we report the 3-D structure of mAng-4 at 2.02-A resolution. The structure shows that the residues forming the putative B1, P1, and B2 RNA-binding subsites occupy positions similar to their hAng counterparts. The B1 subsite is obstructed by Glu115 and Ile118. The obstruction is stabilized by a novel salt bridge between the C-terminal carboxyl group and the side chain of Arg99. Through mutational studies, we identify residues critical to the Angiogenic function of mAng-4. The effect of H12A and H112A mutations i…

  • the crystal structure of human placenta growth factor 1 plgf 1 an Angiogenic Protein at 2 0 a resolution
    Journal of Biological Chemistry, 2001
    Co-Authors: Shalini Iyer, D D Leonidas, G J Swaminathan, Domenico Maglione, Mauro Battisti, Marina Tucci, M G Persico, K R Acharya

    Abstract:

    Abstract The Angiogenic molecule placenta growth factor (PlGF) is a member of the cysteine-knot family of growth factors. In this study, a mature isoform of the human PlGF Protein, PlGF-1, was crystallized as a homodimer in the crystallographic asymmetric unit, and its crystal structure was elucidated at 2.0 A resolution. The overall structure of PlGF-1 is similar to that of vascular endothelial growth factor (VEGF) with which it shares 42% amino acid sequence identity. Based on structural and biochemical data, we have mapped several important residues on the PlGF-1 molecule that are involved in recognition of the fms-like tyrosine kinase receptor (Flt-1, also known as VEGFR-1). We propose a model for the association of PlGF-1 and Flt-1 domain 2 with precise shape complementarity, consider the relevance of this assembly for PlGF-1 signal transduction, and provide a structural basis for altered specificity of this molecule.