46. An antibody with ability to discriminate between fragment D/D-dimer formed by matrix metalloproteinases or plasmin

Kudryk, Bohdan J.; Ahadi, M.; Rohoza, A.; Callender, S.; Schnuer, Jamie; Bini, A.

doi:10.1097/00001721-199810000-00066

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“…Monoclonal Antibodies. MoAb/T54 was recently developed in our laboratory (35). MoAb/T54 reacts with D-like core fragments found in MMP-3 digests of Fg and XL-Fb and corresponding fragments present in MMP-7 digests of these same substrates.…”

Section: Methodsmentioning

confidence: 99%

Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH₂-Terminal Sequences of Late-Stage Digest Fragments

Bini

Schnuer

et al. 1999

Biochemistry

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Matrix metalloproteinases (MMPs) participate in physiological remodeling of the extracellular matrix. Recently we determined that both fibrinogen (Fg) and cross-linked fibrin (XL-Fb) are substrates for selected MMPs. Specifically, XL-Fb clots were solubilized by MMP-3 (stromelysin 1) by cleavage at gamma Gly 404-Ala 405, resulting in a D-like monomer fragment. Similarly, MMP-7 (matrilysin) and MT1-MMP (membrane type 1 matrix metalloproteinase) solubilized XL-Fb clots. However, the molecular mass of fragment D-dimer, obtained after MMP-7 and MT1-MMP degradation of XL-Fb, is similar to that of fragment D-dimer from plasmin degradation ( approximately 186 kDa). In contrast, fragment D-like monomer, from MMP-3 degradation of both fibrinogen (Fg) and XL-Fb, is similar to fragment D from plasmin degradation of Fg ( approximately 94 kDa). Reduced chains from MMP-3, MMP-7, and MT1-MMP digests of Fg and XL-Fb were subjected to direct sequence analyses and D/D-dimer alpha-chain showed cleavage at both alpha Asp 97-Phe 98 and alpha Asn 102-Asn 103. Degradation of the beta-chain resulted in microheterogeneity of cleavage sites at beta Asp 123-Leu 124, beta Asn 137-Val 138, and beta Glu 141-Tyr 142, whereas all three enzymes cleaved the gamma-chain at gamma Thr 83-Leu 84. In both Fg and XL-Fb, several cleavage sites obtained by proteolysis with MMP-3, MMP-7, and MT1-MMP were found to be in very close proximity to those obtained by plasmin on these same substrates. That does not occur with other MMPs such as MMP-1, -2, and -9 and MT2-MMP. The degradation of XL-Fb by MMPs suggests both plasmin-dependent and independent mechanisms of fibrinolysis that might be relevant in inflammation, angiogenesis, arthritis, and atherosclerosis.

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Section: Methodsmentioning

confidence: 99%

Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH₂-Terminal Sequences of Late-Stage Digest Fragments

Bini

Schnuer

et al. 1999

Biochemistry

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46. An antibody with ability to discriminate between fragment D/D-dimer formed by matrix metalloproteinases or plasmin

Cited by 1 publication

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Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH₂-Terminal Sequences of Late-Stage Digest Fragments

Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH₂-Terminal Sequences of Late-Stage Digest Fragments

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46. An antibody with ability to discriminate between fragment D/D-dimer formed by matrix metalloproteinases or plasmin

Cited by 1 publication

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Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH2-Terminal Sequences of Late-Stage Digest Fragments

Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH2-Terminal Sequences of Late-Stage Digest Fragments

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Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH₂-Terminal Sequences of Late-Stage Digest Fragments

Characterization of Stromelysin 1 (MMP-3), Matrilysin (MMP-7), and Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Derived Fibrin(ogen) Fragments D-Dimer and D-like Monomer: NH₂-Terminal Sequences of Late-Stage Digest Fragments