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  • Title: Inhibition of cryogelation by the novel synthetic peptide (Gly-Arg-Lys-Lys-Thr): recognition site of extra domain A containing fibronectin for heparin in cryogelation.
    Author: Miyamoto K, Kobayashi D, Maeda R, Ito T, Komai T.
    Journal: Int J Biol Macromol; 2003 Jan 15; 31(4-5):207-15. PubMed ID: 12568929.
    Abstract:
    Cryogel is a physical gel formed by the heterophilic aggregation of extra domain A (EDA) containing fibronectin [EDA(+)FN], plasma fibronectin (pFN), fibrinogen (Fbg) and heparin (Hep) in the blood of rheumatoid arthritis (RA) patients. In cryogelation EDA(+)FN cross-links to form an interaggregate of cryogel with Hep. In the present study, we determined the recognition structure of Hep for EDA(+)FN by using oligo- and desulfonated-Hep. The affinity constant (KA) (1.2 x 10(8) per M) of oligo-Hep for EDA(+)FN did not change with a decrease in number-average molecular weight (4.9 x 10(4)-->6.0 x 10(3)). The KA-value of desulfonated-Hep for EDA(+)FN decreased from 3.2 x 10(8) to 1.0 x 10(7) per M with a decrease in the sulfonation ratio (7.0-->4.3%). We also determined the recognition structure of EDA(+)FN for Hep by an inhibition experiment on the heparin binding domain II (HepII) in EDA(+)FN with the synthetic peptides, Arg-Arg-Ala-Arg (RRAR), Asp-Gln-Ala-Arg (DNAR), Ile-Lys-Tyr-Glu-Lys (IKYEK), and Gly-Arg-Lys-Lys-Try (GRKKT). The GRKKT sequence clearly inhibited bonding between EDA(+)FN and Heps containing oligo- and desulfonated-Hep. The amount of cryogel formed in the RA-patient model plasma corresponded to the EDA(+)FN concentration in cryogel (36.7%) normalized by the EDA(+)FN concentration in plasma. When GRKKT was added to plasma, the EDA(+)FN concentration fell to 10.5%. These results demonstrated that inhibition of cryogelation in plasma could progress to a novel treatment for RA.
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