LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Your last searches

  1. AU="Lundberg, Dianna M"
  2. AU="Liu, Jingbang"
  3. AU="Margherita De Rosa"
  4. AU="Feldman-Kiss, Damian"
  5. AU="Ristic, Snezana"
  6. AU="Ekott, Mabel Ikpim"
  7. AU="Maldonado-Huerta, Tatiana"
  8. AU="Giuseppe Musumeci"
  9. AU="Jacczak, Barbara"
  10. AU="Huang, XinMei"
  11. AU="Zhang, Wenyuan"
  12. AU="Powers, Ann M"
  13. AU="Werth, Annette Gravino Pietro Prevedello Giulio"
  14. AU="Lawson, J. S."
  15. AU="Gafuik, Christopher J"
  16. AU="Lubsandorzhiev, B K"
  17. AU="Ni, Connie W"
  18. AU="Halpern, Allan C"
  19. AU=Ratner Nancy
  20. AU="Lynch, Jeremy"
  21. AU=Krieger Nancy
  22. AU="Castro, Andrea"
  23. AU="de Souza, H Vieira"
  24. AU="Shou-Hsia Cheng" AU="Shou-Hsia Cheng"
  25. AU="Nawrocki, Eric P."
  26. AU="Su, Bo"
  27. AU="Silva, Carla G Bueno"
  28. AU="Paredes-Vazquez, Jose Gildardo"
  29. AU=Cen Gengyu AU=Cen Gengyu
  30. AU="Gosavi, Suresh"
  31. AU="Cheng, Canhong H"
  32. AU="Sakharkar, Amul"
  33. AU=Liu Bai
  34. AU=Baumeister A
  35. AU="Vasconcellos, Silvio A"
  36. AU="Etenko, A."
  37. AU="Gianluca Dini"
  38. AU="Pabon, Jonathan"
  39. AU="Samalantin, K M"
  40. AU="Babin, Patrick J"
  41. AU="Sesti, Giorgio"

Search results

Result 1 - 4 of total 4

Search options

  1. Article: VEGFR-1/Flt-1 inhibition increases angiogenesis and improves muscle function in a mouse model of Duchenne muscular dystrophy.

    Bosco, Jennifer / Zhou, Zhiwei / Gabriëls, Sofie / Verma, Mayank / Liu, Nan / Miller, Brian K / Gu, Sheng / Lundberg, Dianna M / Huang, Yan / Brown, Eilish / Josiah, Serene / Meiyappan, Muthuraman / Traylor, Matthew J / Chen, Nancy / Asakura, Atsushi / De Jonge, Natalie / Blanchetot, Christophe / de Haard, Hans / Duffy, Heather S /
    Keefe, Dennis

    Molecular therapy. Methods & clinical development

    2021  Volume 21, Page(s) 369–381

    Abstract: Duchenne muscular dystrophy is characterized by structural degeneration of muscle, which is exacerbated by localized functional ischemia due to loss of nitric oxide synthase-induced vasodilation. Treatment strategies aimed at increasing vascular ... ...

    Abstract Duchenne muscular dystrophy is characterized by structural degeneration of muscle, which is exacerbated by localized functional ischemia due to loss of nitric oxide synthase-induced vasodilation. Treatment strategies aimed at increasing vascular perfusion have been proposed. Toward this end, we have developed monoclonal antibodies (mAbs) that bind to the vascular endothelial growth factor (VEGF) receptor VEGFR-1 (Flt-1) and its soluble splice variant isoform (sFlt-1) leading to increased levels of free VEGF and proangiogenic signaling. The lead chimeric mAb, 21B3, had high affinity and specificity for both human and mouse sFlt-1 and inhibited VEGF binding to sFlt-1 in a competitive manner. Proof-of-concept studies in the
    Language English
    Publishing date 2021-03-23
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2872938-9
    ISSN 2329-0501 ; 2329-0501
    ISSN (online) 2329-0501
    ISSN 2329-0501
    DOI 10.1016/j.omtm.2021.03.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: Expression and purification methods for the production of recombinant human complement component C2.

    Norton, Angela W / Martini, Paolo G V / Cook, Lynette C / Alderucci, Scott / Lundberg, Dianna M / Fish, Susan M / Bedard, Charles / Gill, John / Tzianabos, Arthur O / Concino, Michael F

    Methods in molecular biology (Clifton, N.J.)

    2014  Volume 1100, Page(s) 61–74

    Abstract: Human complement component C2 is a critical factor of the classical complement pathway. Here we provide a method for the production of recombinant human C2 (rhC2) protein for research purposes. The human complement component C2 (hC2) is cloned from a ... ...

    Abstract Human complement component C2 is a critical factor of the classical complement pathway. Here we provide a method for the production of recombinant human C2 (rhC2) protein for research purposes. The human complement component C2 (hC2) is cloned from a human cDNA library by polymerase chain reaction and inserted in a mammalian expression vector (Martini et al., BMC Immunol 11:43, 2010). Transient transfection is utilized to express hC2 in a mammalian cell line, and the expressed C2 is harvested from the conditioned media. rhC2 is purified from the conditioned media by sequential steps of cation exchange and affinity column chromatography. The purified hC2 is characterized for protein purity, stability, and enzymatic activity. The recombinant hC2 activity is tested in a complement activation ELISA assay that measures classical, alternative, and lectin complement pathway activity in C2-depleted serum.
    MeSH term(s) Cell Line ; Chromatography, High Pressure Liquid ; Complement C2/biosynthesis ; Complement C2/chemistry ; Complement C2/genetics ; Complement C2/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Gene Expression ; Humans ; Recombinant Proteins
    Chemical Substances Complement C2 ; Recombinant Proteins
    Language English
    Publishing date 2014
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-62703-724-2_5
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Recombinant human complement component C2 produced in a human cell line restores the classical complement pathway activity in-vitro

    Martini Paolo GV / Cook Lynette C / Alderucci Scott / Norton Angela W / Lundberg Dianna M / Fish Susan M / Langsetmo Knut / Jönsson Göran / Lood Christian / Gullstrand Birgitta / Zaleski Kate J / Savioli Nancy / Lottherand Jason / Bedard Charles / Gill John / Concino Michael F / Heartlein Michael W / Truedsson Lennart / Powell Jan L /
    Tzianabos Arthur O

    BMC Immunology, Vol 11, Iss 1, p

    an alternative treatment for C2 deficiency diseases

    2010  Volume 43

    Abstract: Abstract Background Complement C2 deficiency is the most common genetically determined complete complement deficiency and is associated with a number of diseases. Most prominent are the associations with recurrent serious infections in young children and ...

    Abstract Abstract Background Complement C2 deficiency is the most common genetically determined complete complement deficiency and is associated with a number of diseases. Most prominent are the associations with recurrent serious infections in young children and the development of systemic lupus erythematosus (SLE) in adults. The links with these diseases reflect the important role complement C2 plays in both innate immunity and immune tolerance. Infusions with normal fresh frozen plasma for the treatment of associated disease have demonstrated therapeutic effects but so far protein replacement therapy has not been evaluated. Results Human complement C2 was cloned and expressed in a mammalian cell line. The purity of recombinant human C2 (rhC2) was greater than 95% and it was characterized for stability and activity. It was sensitive to C1s cleavage and restored classical complement pathway activity in C2-deficient serum both in a complement activation ELISA and a hemolytic assay. Furthermore, rhC2 could increase C3 fragment deposition on the human pathogen Streptococcus pneumoniae in C2-deficient serum to levels equal to those with normal serum. Conclusions Taken together these data suggest that recombinant human C2 can restore classical complement pathway activity and may serve as a potential therapeutic for recurring bacterial infections or SLE in C2-deficient patients.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Specialties of internal medicine ; RC581-951 ; Internal medicine ; RC31-1245 ; Medicine ; R ; DOAJ:Allergy and Immunology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
    Subject code 616
    Language English
    Publishing date 2010-08-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    More links

    Kategorien

  4. Article ; Online: Recombinant human complement component C2 produced in a human cell line restores the classical complement pathway activity in-vitro: an alternative treatment for C2 deficiency diseases.

    Martini, Paolo G V / Cook, Lynette C / Alderucci, Scott / Norton, Angela W / Lundberg, Dianna M / Fish, Susan M / Langsetmo, Knut / Jönsson, Göran / Lood, Christian / Gullstrand, Birgitta / Zaleski, Kate J / Savioli, Nancy / Lottherand, Jason / Bedard, Charles / Gill, John / Concino, Michael F / Heartlein, Michael W / Truedsson, Lennart / Powell, Jan L /
    Tzianabos, Arthur O

    BMC immunology

    2010  Volume 11, Page(s) 43

    Abstract: Background: Complement C2 deficiency is the most common genetically determined complete complement deficiency and is associated with a number of diseases. Most prominent are the associations with recurrent serious infections in young children and the ... ...

    Abstract Background: Complement C2 deficiency is the most common genetically determined complete complement deficiency and is associated with a number of diseases. Most prominent are the associations with recurrent serious infections in young children and the development of systemic lupus erythematosus (SLE) in adults. The links with these diseases reflect the important role complement C2 plays in both innate immunity and immune tolerance. Infusions with normal fresh frozen plasma for the treatment of associated disease have demonstrated therapeutic effects but so far protein replacement therapy has not been evaluated.
    Results: Human complement C2 was cloned and expressed in a mammalian cell line. The purity of recombinant human C2 (rhC2) was greater than 95% and it was characterized for stability and activity. It was sensitive to C1s cleavage and restored classical complement pathway activity in C2-deficient serum both in a complement activation ELISA and a hemolytic assay. Furthermore, rhC2 could increase C3 fragment deposition on the human pathogen Streptococcus pneumoniae in C2-deficient serum to levels equal to those with normal serum.
    Conclusions: Taken together these data suggest that recombinant human C2 can restore classical complement pathway activity and may serve as a potential therapeutic for recurring bacterial infections or SLE in C2-deficient patients.
    MeSH term(s) Adult ; Cell Line, Transformed ; Child ; Complement C1/immunology ; Complement C1/metabolism ; Complement C2/genetics ; Complement C2/metabolism ; Complement C2/therapeutic use ; Complement C3/immunology ; Complement C3/metabolism ; Complement Pathway, Classical/drug effects ; Humans ; Immunologic Deficiency Syndromes/complications ; Immunologic Deficiency Syndromes/drug therapy ; Immunologic Deficiency Syndromes/genetics ; Lupus Erythematosus, Systemic/complications ; Lupus Erythematosus, Systemic/drug therapy ; Lupus Erythematosus, Systemic/genetics ; Protein Binding/drug effects ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Recombinant Proteins/therapeutic use ; Recurrence ; Streptococcal Infections/complications ; Streptococcal Infections/drug therapy ; Streptococcal Infections/genetics ; Streptococcus pneumoniae/immunology
    Chemical Substances Complement C1 ; Complement C2 ; Complement C3 ; Recombinant Proteins
    Language English
    Publishing date 2010-08-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1471-2172
    ISSN (online) 1471-2172
    DOI 10.1186/1471-2172-11-43
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top