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Titolo:
Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies
Autore:
Ries, A; Gohring, W; Fox, JW; Timpl, R; Sasaki, T;
Indirizzi:
Max Planck Inst Biochem, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany Univ Virginia, Sch Med, Dept Microbiol, Charlottesville, VA 22908 USA UnivVirginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 19, volume: 268, anno: 2001,
pagine: 5119 - 5128
SICI:
0014-2956(200110)268:19<5119:RDOMNA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SEQUENCE; EXTRACELLULAR-MATRIX COMPONENTS; HEPARAN-SULFATE PROTEOGLYCAN; LEUKOCYTE RESPONSE INTEGRIN; GROWTH-FACTOR PRECURSOR; COLLAGEN TYPE-IV; STRUCTURAL CHARACTERIZATION; EPITHELIAL MORPHOGENESIS; GLYCOPROTEIN ENTACTIN; CELL ATTACHMENT;
Keywords:
basement membranes; monoclonal antibodies; protein interactions; recombinant production;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Timpl, R Max Planck Inst Biochem, Klopferspitz 18 A, D-82152 Martinsried, Germany Max Planck Inst Biochem Klopferspitz 18 A Martinsried Germany D-82152
Citazione:
A. Ries et al., "Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies", EUR J BIOCH, 268(19), 2001, pp. 5119-5128

Abstract

The basement membrane protein, nidogen-1, was previously shown to consist of three globular domains, G1 to G3, and two connecting segments. Nidogen-1is a major mediator in the formation of ternary complexes with laminins, collagen IV, perlecan and fibulins. In the present study, we have produced recombinant proteins of these predicted domains in mammalian cells and used these proteins for crystallographic and binding epitope analyses. These fragments included G1, G2, the rod domain and a slightly larger G3 structure; all were obtained in good yields and were shown to be properly folded usingelectron microscopy. Surface plasmon resonance assays demonstrated high affinity binding (K-d = 3-9 nM) of domain G2 for collagen IV, perlecan domainIV-1 and fibulin-2, and a more moderate K-d for fibulin-1C. Domain G3 contained high affinity binding sites for the laminin gamma1 chain and collagenIV (K-d = 1 nM) and weaker binding sites for fibulin-1C and fibulin-2. A moderate binding affinity was also observed between domain G1 and fibulin-2,while no activity could be detected for the nidogen rod domain. Together, these data indicate the potential of nidogen-1 for multiple interactions within basement membranes. A similar binding repertoire was also identified for seven rat monoclonal antibodies that bound with K-d = 2-30 nM to either G1, G1-G2, G2, the rod domain or G3. Three of the antibodies showed strongly reduced binding to G2 and G3 after complex formation with either a perlecan domain or laminin-1.

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Documento generato il 26/11/20 alle ore 19:00:24