Thrombospondin binding to specific sequences within the A alpha- and B beta-chains of fibrinogen.

Bacon-Baguley, Theresa; Ogilvie, M L; Gartner, T. Kent; Walz, Daniel A.

doi:10.1016/s0021-9258(19)39978-8

Cited by 29 publications

(3 citation statements)

References 52 publications

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“…250 amino acids, together with the comparable portion of the 7 chain, constitutes the most highly conserved part of the entire fibrinogen molecule, its functional significance is not fully understood. Two functional domains have been assigned to this region thus far: a Ca2+ binding site on the 7 chain (Varadi & Scheraga, 1986) and a thrombospondin binding domain on the 0 chain (Bacon- Baguley et al, 1990).…”

Section: Resultsmentioning

confidence: 99%

The .beta. chain of chicken fibrinogen contains an atypical thrombin cleavage site

Weissbach¹,

Oddoux²,

Procyk³

et al. 1991

Biochemistry

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A cDNA corresponding to almost the entire coding region of the mRNA for the beta chain of chicken fibrinogen was sequenced. At the protein level, significant homology to the beta subunits of other vertebrate fibrinogens was found, with the highest degree of amino acid identity localized in the C-terminal region. In general, features conserved in the fibrinogens from other species also characterize the chicken sequence, including the cysteine motifs bordering an alpha-helical permissive region of fixed length and a single glycosylation site in the C-terminal region. However, the site of thrombin-catalyzed cleavage, which in other species consists of an Arg-Gly peptide bond, is instead an Arg-Ala bond in the chicken beta chain. The Ala was confirmed directly from a sequencing analysis of the purified beta chain of chicken fibrin. This finding may explain the observed slow clotting time of chicken fibrinogen relative to that of other species.

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Section: Resultsmentioning

confidence: 99%

The .beta. chain of chicken fibrinogen contains an atypical thrombin cleavage site

Weissbach¹,

Oddoux²,

Procyk³

et al. 1991

Biochemistry

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“…Our results suggested that the lipoplexes were held in the scaffold for up to 144 h of incubation at 37 °C. Fibrinogen is the “sticky” component of the fibrin gel and has been shown to bind to various biomolecules such as fibronectin, vitronectin, myosin, thrombospondin, basic fibroblast growth factor (bFGF), transforming growth factor-β, and VEGF . Considering this, we studied the interaction of fibrinogen with lipofectin, hoping to understand why lipoplexes were retained inside the scaffold.…”

Section: Discussionmentioning

confidence: 99%

Fibrin−Lipoplex System for Controlled Topical Delivery of Multiple Genes

et al. 2009

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Nonviral gene delivery via natural biomacromolecules show great promise as controlled release systems while avoiding the associated drawbacks with viral gene delivery such as immunogenicity and safety issues. Here, a fibrin-lipoplex system for topical delivery of multiple genes is described. In vitro release analysis showed efficient retention of the lipoplexes in the fibrin scaffold. The biomolecular interaction between fibrinogen and liposomes was investigated qualitatively using surface plasmon resonance. The strong binding between the lipoplexes and the fibrinogen component of the scaffold was observed and that could explain the in vitro release profile observed in our studies. Both in vitro and in vivo transfection studies using multiple reporter genes were performed to establish the bioactivity of released lipoplexes. The ability of the lipoplexes to transfect fibroblasts in vitro was shown to be maintained even after extended periods of encapsulation within the scaffold. Furthermore, in a rabbit ear ulcer model, the fibrin-lipoplex system was shown to have significantly higher transfection efficiency for two reporter genes at day 7 when compared to lipoplexes alone, suggesting that this fibrin-lipoplex system is suitable for extended release of lipoplexes for topical gene delivery applications.

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“…Fibrin has the capacity to bind other blood-borne, provisional matrix proteins including ¢bronectin (Makogonenko et al, 2002), xxi vitronectin (Preissner and Jenne, 1991), and thrombospondin (Bacon-Baguley et al, 1990). The ability of ¢brin to convey these matrix proteins to the early wound clearly ampli¢es the ability of the ¢brin clot to support tissue cell migration (Greiling and Clark, 1997).…”

mentioning

confidence: 99%

Fibrin Is a Many Splendored Thing

Clark

2003

Journal of Investigative Dermatology

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Thrombospondin binding to specific sequences within the A alpha- and B beta-chains of fibrinogen.

Cited by 29 publications

References 52 publications

The .beta. chain of chicken fibrinogen contains an atypical thrombin cleavage site

The .beta. chain of chicken fibrinogen contains an atypical thrombin cleavage site

Fibrin−Lipoplex System for Controlled Topical Delivery of Multiple Genes

Fibrin Is a Many Splendored Thing

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