Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pooled plasma from 40 patients with severe disseminated intravascular coagulation (DIC) secondary to septic conditions was subjected to gel permeation chromatography on Sephacryl S-500 HR after sample pretreatment with KSCN for dissociation of non-covalent fibrin complexes. Fibrin antigen in eluates was detected by an array of ELISA tests, using two monoclonal antibodies against fibrin degradation product D-dimer, a monoclonal antibody against an epitope generated by plasmin cleavage of the D-domain, and an antibody against the neo-N-terminus of the alpha-chain of fibrin exposed by cleavage of fibrinopeptide A. Tag antibodies were a polyclonal antibody against the fibrinogen/ fibrin D-domain, a POD-conjugated version of the monoclonal antibody against fibrin alpha-chain neo-N-terminus, and a polyclonal antibody against fibrinopeptide A. Most fibrin-related material present in the pooled DIC plasma was of higher molecular mass than fibrinogen. Fibrin polymers were reactive with antibodies against D-dimer, plasmin cleaved D-domain, and fibrin alpha-chain neo-N-terminus. Part of the polymers reacted with antibodies against fibrinopeptide A, indicating presence of fibrinogen or desA-fibrin monomer within the covalently linked complex. In conclusion, the primary analytes detected by monoclonal antibodies for D-dimer, plasmin-specific epitopes of fibrin degradation products, as well as sites exposed by fibrinopeptide cleavage in plasma from patients with disseminated intravascular coagulation are high molecular weight factor XIIIa-crosslinked fibrin complexes, containing plasmin-cleaved D-domains, intact fibrin monomer units, and fibrinogen or desA-fibrin monomer.
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PMID:Fibrin detected in plasma of patients with disseminated intravascular coagulation by fibrin-specific antibodies consists primarily of high molecular weight factor XIIIa-crosslinked and plasmin-modified complexes partially containing fibrinopeptide A. 930 56

Vascular endothelial growth factor (VEGF) is a homodimeric glycoprotein that promotes angiogenesis and vascular hyperpermeability and interacts with two receptors, fms-like tyrosine kinase (Flt-1) and kinase domain-containing region (KDR). In situ localization in the pregnant human uterus revealed that VEGF mRNA is expressed primarily by the maternal decidua, whereas the receptor Flt-1 is expressed primarily by chorionic vascular endothelium and trophoblast cells-in particular, the extravillous trophoblast (EVT). We examined whether the mRNA and protein of VEGF and its receptors are expressed by invasive human first-trimester EVT cells propagated in culture and whether VEGF influences EVT cell proliferation, migration, and invasiveness. Proliferation was assessed by the uptake of [3H]thymidine. Invasion and migration across transwells were assessed by the degree of cellular transgression of a Millipore membrane coated, respectively, with and without Matrigel. Results of immunocytochemical and reverse transcription-polymerase chain reaction analysis revealed that both protein and mRNA of VEGF, Flt-1, and KDR were expressed by cultured normal EVT cells as well as their premalignant derivative produced by SV-40 Tag-immortalization, and BeWo choriocarcinoma cells. Under serum-free conditions, exogenous VEGF121 (the non-heparin-binding isoform) stimulated proliferation of all three cell lines in a concentration-dependent manner. The effects were abolished with a VEGF-neutralizing antibody. The same stimulatory effects on EVT cells were also seen with exogenous VEGF165 (a heparin-binding isoform), only after a cleaving of the heparin-binding domain with plasmin or a blocking of heparin binding sites with excess soluble heparan sulphate proteoglycans (HSPGs), suggesting a regulatory role of HSPGs. However, VEGF121 and VEGF165 (with and without the HSPG pretreatment) had no effect on normal EVT cell migration or invasiveness. Thus, VEGF may provide a dual role in angiogenesis and EVT cell proliferation during normal placental development.
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PMID:Vascular endothelial growth factor stimulates proliferation but not migration or invasiveness in human extravillous trophoblast. 971 65