Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases

[1]  V. Quesada,et al.  Withdrawal: Identification and characterization of human and mouse ovastacin: A novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish. , 2019, Journal of Biological Chemistry.

[2]  P. Rosenstiel,et al.  Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB. , 2017, Cell reports.

[3]  P. Boor,et al.  Post-weaning epiphysiolysis causes distal femur dysplasia and foreshortened hindlimbs in fetuin-A-deficient mice , 2017, PloS one.

[4]  Dagmar Wachten,et al.  Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida , 2017, Molecular human reproduction.

[5]  Yiyue Zhang,et al.  Zebrafish nephrosin helps host defence against Escherichia coli infection , 2017, Open Biology.

[6]  J. Scheller,et al.  Meprin Metalloproteases Generate Biologically Active Soluble Interleukin-6 Receptor to Induce Trans-Signaling , 2017, Scientific Reports.

[7]  A. Tholey,et al.  Ectodomain shedding of CD99 within highly conserved regions is mediated by the metalloprotease meprin β and promotes transendothelial cell migration , 2017, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[8]  J. Dean,et al.  A Unique Egg Cortical Granule Localization Motif Is Required for Ovastacin Sequestration to Prevent Premature ZP2 Cleavage and Ensure Female Fertility in Mice , 2017, PLoS genetics.

[9]  A. Tholey,et al.  Characterization of post-translational modifications in full-length human BMP-1 confirms the presence of a rare vicinal disulfide linkage in the catalytic domain and highlights novel features of the EGF domain. , 2016, Journal of proteomics.

[10]  W. Jahnen-Dechent,et al.  Association of high fetuin-B concentrations in serum with fertilization rate in IVF: a cross-sectional pilot study. , 2016, Human reproduction.

[11]  P. Briza,et al.  Structure and Mechanism of an Aspartimide-Dependent Peptide Ligase in Human Legumain** , 2015, Angewandte Chemie.

[12]  R. Weiskirchen,et al.  Mammalian gamete fusion depends on the inhibition of ovastacin by fetuin-B , 2014, Biological chemistry.

[13]  Ellen F. Macnamara,et al.  SAS1B protein [ovastacin] shows temporal and spatial restriction to oocytes in several eutherian orders and initiates translation at the primary to secondary follicle transition , 2013, Developmental dynamics : an official publication of the American Association of Anatomists.

[14]  M. Okabe.  The cell biology of mammalian fertilization , 2013, Development.

[15]  C. Overall,et al.  Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength , 2013, Proceedings of the National Academy of Sciences.

[16]  H. Brandstetter,et al.  Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation , 2013, Proceedings of the National Academy of Sciences.

[17]  J. Dean,et al.  The molecular basis of gamete recognition in mice and humans. , 2013, Molecular human reproduction.

[18]  T. Renné,et al.  Fetuin-B, a liver-derived plasma protein is essential for fertilization. , 2013, Developmental cell.

[19]  C. Becker-Pauly,et al.  The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis , 2013, The Biochemical journal.

[20]  P. E. Van den Steen,et al.  Meprins process matrix metalloproteinase‐9 (MMP‐9)/gelatinase B and enhance the activation kinetics by MMP‐3 , 2012, FEBS letters.

[21]  F. Gomis-Rüth,et al.  Functional and structural insights into astacin metallopeptidases , 2012, Biological chemistry.

[22]  W. Bode,et al.  Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane , 2012, Proceedings of the National Academy of Sciences.

[23]  A. Chalaris,et al.  The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10 , 2012, Cellular and Molecular Life Sciences.

[24]  G. Multhaup,et al.  The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species* , 2012, The Journal of Biological Chemistry.

[25]  J. Olefsky,et al.  Fetuin-A: the missing link in lipid-induced inflammation , 2012, Nature Medicine.

[26]  F. García-Vázquez,et al.  Oocytes use the plasminogen-plasmin system to remove supernumerary spermatozoa. , 2012, Human reproduction.

[27]  Hui Yang,et al.  Secretome profile of mouse oocytes after activation using mass spectrum , 2012, Journal of Assisted Reproduction and Genetics.

[28]  J. Dean,et al.  Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy , 2012, The Journal of cell biology.

[29]  Olivier Barré,et al.  Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates , 2011, Molecular & Cellular Proteomics.

[30]  C. Overall,et al.  Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo* , 2011, The Journal of Biological Chemistry.

[31]  S. Vadon-Le Goff,et al.  Processing of procollagen III by meprins: new players in extracellular matrix assembly? , 2010, The Journal of investigative dermatology.

[32]  J. Hedrich,et al.  Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases. , 2010, Biochemistry.

[33]  R. Kappelhoff,et al.  Proenzyme Structure and Activation of Astacin Metallopeptidase* , 2010, The Journal of Biological Chemistry.

[34]  J. Hedrich,et al.  Let It Flow: Morpholino Knockdown in Zebrafish Embryos Reveals a Pro-Angiogenic Effect of the Metalloprotease Meprin α2 , 2010, PloS one.

[35]  V. Turk,et al.  Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes , 2009, BMC Evolutionary Biology.

[36]  A. Bernardi,et al.  Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases. , 2008, Journal of molecular biology.

[37]  J. S. Bond,et al.  Meprins, membrane-bound and secreted astacin metalloproteinases. , 2008, Molecular aspects of medicine.

[38]  S. Ricard-Blum,et al.  Insights into How CUB Domains Can Exert Specific Functions while Sharing a Common Fold , 2007, Journal of Biological Chemistry.

[39]  V. Magdolen,et al.  The α and β Subunits of the Metalloprotease Meprin Are Expressed in Separate Layers of Human Epidermis, Revealing Different Functions in Keratinocyte Proliferation and Differentiation , 2007 .

[40]  W. Lehmann,et al.  Proteolytic processing by matrix metalloproteinases and phosphorylation by protein kinase CK2 of fetuin-A, the major globulin of fetal calf serum. , 2007, Biochimie.

[41]  D. Greenspan,et al.  BMP1 controls TGFβ1 activation via cleavage of latent TGFβ-binding protein , 2006, The Journal of cell biology.

[42]  Víctor Quesada,et al.  Identification and Characterization of Human and Mouse Ovastacin , 2004, Journal of Biological Chemistry.

[43]  C. Chou,et al.  Purification and Cloning of an Endogenous Protein Inhibitor of Carp Nephrosin, an Astacin Metalloproteinase* , 2004, Journal of Biological Chemistry.

[44]  Neil D Rawlings,et al.  Evolutionary families of peptidase inhibitors. , 2004, The Biochemical journal.

[45]  J. Ochieng,et al.  Members of the cystatin superfamily interact with MMP-9 and protect it from autolytic degradation without affecting its gelatinolytic activities. , 2003, Biochimica et biophysica acta.

[46]  H. Nagase,et al.  Zymography of Metalloproteinases , 2003, Current protocols in protein science.

[47]  A. Schwarz,et al.  The serum protein α2–Heremans-Schmid glycoprotein/fetuin-A is a systemically acting inhibitor of ectopic calcification , 2003 .

[48]  F. Gomis-Rüth,et al.  Structural aspects of the metzincin clan of metalloendopeptidases , 2003, Molecular biotechnology.

[49]  T. Renné,et al.  Structural Basis of Calcification Inhibition by α2-HS Glycoprotein/Fetuin-A , 2003, The Journal of Biological Chemistry.

[50]  J. Harris,et al.  Differences in the Activation Mechanism between the α and β Subunits of Human Meprin , 2003 .

[51]  L. Matrisian,et al.  Interactions of alpha2-HS-glycoprotein (fetuin) with MMP-3 and murine squamous cell carcinoma cells. , 2002, International journal of oncology.

[52]  E. Sterchi,et al.  Activation of Human Meprin-α in a Cell Culture Model of Colorectal Cancer Is Triggered by the Plasminogen-activating System* , 2002, The Journal of Biological Chemistry.

[53]  J. Fox,et al.  BJ46a, a snake venom metalloproteinase inhibitor. Isolation, characterization, cloning and insights into its mechanism of action. , 2001, European journal of biochemistry.

[54]  J. Dennis,et al.  Regulation of human monocyte proMMP‐9 production by fetuin, an endogenous TGF‐β antagonist , 2000, Journal of cellular physiology.

[55]  S. Reyda,et al.  cDNA cloning, bacterial expression, in vitro renaturation and affinity purification of the zinc endopeptidase astacin. , 1999, The Biochemical journal.

[56]  A. Barrett,et al.  Inhibition of Mammalian Legumain by Some Cystatins Is Due to a Novel Second Reactive Site* , 1999, The Journal of Biological Chemistry.

[57]  F. Sablitzky,et al.  Cloning and Targeted Deletion of the Mouse Fetuin Gene* , 1997, The Journal of Biological Chemistry.

[58]  J. Kellermann,et al.  Limited Proteolysis of Human α2-HS Glycoprotein/Fetuin , 1996, The Journal of Biological Chemistry.

[59]  Howard C. Tenenbaum,et al.  Fetuin/α2-HS Glycoprotein Is a Transforming Growth Factor-β Type II Receptor Mimic and Cytokine Antagonist* , 1996, The Journal of Biological Chemistry.

[60]  P. Reinemer,et al.  The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases , 1995, Protein science : a publication of the Protein Society.

[61]  W. Bode,et al.  cystatins: protein inhibitors of cysteine proteinases , 2001 .

[62]  S. Strickland,et al.  Mouse ovarian granulosa cells produce urokinase-type plasminogen activator, whereas the corresponding rat cells produce tissue-type plasminogen activator , 1987, The Journal of cell biology.

[63]  A. Barrett,et al.  Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. , 1986, The Biochemical journal.

[64]  D. Belin,et al.  Plasminogen activator in mouse and rat oocytes: Induction during meiotic maturation , 1985, Cell.

[65]  J. Bieth,et al.  In vivo significance of kinetic constants of protein proteinase inhibitors. , 1984, Biochemical medicine.

[66]  J. Kyhse-Andersen.  Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. , 1984, Journal of biochemical and biophysical methods.

[67]  J. Cann,et al.  Fetuin as a trypsin inhibitor. , 1974, Archives of biochemistry and biophysics.

[68]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[69]  P. Edman,et al.  A method for the determination of amino acid sequence in peptides. , 1949, Archives of biochemistry.

[70]  H. Kowarzyk.  Structure and Function. , 1910, Nature.

[71]  R. Weiskirchen,et al.  Recombinant fetuin-B protein maintains high fertilization rate in cumulus cell-free mouse oocytes , 2017, Molecular human reproduction.

[72]  M. Ferguson-Pell,et al.  Users’ attitudes towards personal health records A cross-sectional pilot study , 2016 .

[73]  K. Brix,et al.  Proteases: Structure and Function , 2013, Springer Vienna.

[74]  E. Bongcam-Rudloff,et al.  Type 3 cystatins; fetuins, kininogen and histidine-rich glycoprotein. , 2009, Frontiers in bioscience.

[75]  V. Magdolen,et al.  The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation. , 2007, Journal of Investigative Dermatology.

[76]  J. Harris,et al.  Differences in the activation mechanism between the alpha and beta subunits of human meprin. , 2003, Biological chemistry.