Literature DB >> 3839290

Molecular characterization and expression of the gene encoding human erythroid-potentiating activity.

J C Gasson, D W Golde, S E Kaufman, C A Westbrook, R M Hewick, R J Kaufman, G G Wong, P A Temple, A C Leary, E L Brown.   

Abstract

Erythropoietin is the primary physiological regulator of erythropoiesis; however, in vitro studies have identified another class of mediators which appear to be important in stimulating erythroid progenitors. These factors have generally been referred to as burst-promoting activities (BPA), because they stimulate the growth of early erythroid progenitors referred to as burst-forming units-erythroid (BFU-E) which give rise to colonies of up to thousands of haemoglobinized cells. We recently reported purification of a burst-promoting activity from medium conditioned by the Mo T-lymphoblast cell line infected with human T-cell lymphotropic virus type II (HTLV-II). This purified glycoprotein of relative molecular mass (Mr) 28,000 also stimulates colony formation by more mature erythroid precursors (CFU-E) and is therefore referred to as erythroid-potentiating activity (EPA). Purified EPA specifically stimulates human and murine cells of the erythroid lineage, unlike murine interleukin-3 (IL-3) which stimulates precursor cells from all haematopoietic lineages. We report here the isolation of a complementary DNA molecular clone encoding EPA and its use in producing EPA in COS (monkey) cells and CHO (Chinese hamster ovary) cells. We also define the organization of the EPA gene in human DNA.

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Year:  1985        PMID: 3839290     DOI: 10.1038/315768a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  53 in total

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Review 2.  MMPs and TIMPs--an historical perspective.

Authors:  J Frederick Woessner
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3.  Tissue inhibitor of metalloproteinase 1 regulates resistance to infection.

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Review 5.  Metalloproteinases and their natural inhibitors in inflammation and immunity.

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Journal:  Nat Rev Immunol       Date:  2013-09       Impact factor: 53.106

Review 6.  Cytokine functions of TIMP-1.

Authors:  Christian Ries
Journal:  Cell Mol Life Sci       Date:  2013-08-28       Impact factor: 9.261

Review 7.  Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion.

Authors:  Dimitra Bourboulia; William G Stetler-Stevenson
Journal:  Semin Cancer Biol       Date:  2010-05-12       Impact factor: 15.707

Review 8.  The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity.

Authors:  Keith Brew; Hideaki Nagase
Journal:  Biochim Biophys Acta       Date:  2010-01-15

9.  Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.

Authors:  G I Goldberg; B L Marmer; G A Grant; A Z Eisen; S Wilhelm; C S He
Journal:  Proc Natl Acad Sci U S A       Date:  1989-11       Impact factor: 11.205

10.  Immunohistochemical study on tissue inhibitors of metalloproteinases in normal and pathological human livers.

Authors:  Y Fukuda; M Imoto; Y Koyama; Y Miyazawa; I Nakano; M Hattori; F Urano; S Kodama; K Iwata; T Hayakawa
Journal:  Gastroenterol Jpn       Date:  1991-02
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