Methods for the Determination of Plasmin, Antiplasmin and Plasminogen by Means of the Substrate S-2251

Friberger, P.; Knös, M.; Gustavsson, S.; Aurell, L.; Claeson, Göran

doi:10.1055/s-0039-1680387

Cited by 23 publications

(9 citation statements)

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“…Plasminogen in nasal secretion was determined as previously described (Friberger et al 1978). Of each nasal secretion sample, 200 ml were added to 100 ml of 10,000 U/ml streptokinase solution (Daiichi Pure Chemicals, Tokyo, Japan), and incubated for 5 min at 37C.…”

Section: Plasminogen Determination Of Nasal Secretionmentioning

confidence: 99%

Expression profiles of fibrinolytic components in nasal mucosa

Sejima

Madoiwa

Mimuro

et al. 2004

Histochem Cell Biol

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Components of the fibrinolytic pathway contribute to diverse pathways in many tissues, in addition to their well-recognized role in degradation of fibrin clots. In this study of nasal mucosa, we investigated the presence of mRNA of tissue-type plasminogen activator (t-PA), urokinase-type plasminogen activator (u-PA), plasminogen activator inhibitor-1 (PAI-1), and plasminogen activator inhibitor-2 (PAI-2) using reverse transcription polymerase chain reaction (RT-PCR) and in situ hybridization, and compared these results with their localization in immunostained tissues. According to real-time RT-PCR results, t-PA, u-PA, PAI-1, and PAI-2 mRNA were noted in human nasal mucosa. Particularly, expression of u-PA and PAI-1 mRNA was significantly high in allergic nasal mucosa in comparison with normal mucosa. t-PA mRNA was detected in endothelial cells and epithelium in normal nasal mucosa. t-PA mRNA was detected in mucous cells of allergic submucosal glands, but not in normal glands. In allergic rhinitis, u-PA and PAI-2 mRNA were detected in mucinous cells and epithelium, and PAI-1 mRNA was detected in serous cells and epithelium. Expression of u-PA and PAI-1 mRNA in normal nasal tissues was decreased in contrast to that in allergic nasal tissues. u-PA staining was observed in mucous cells of allergic submucosal glands and the staining pattern of PAI-2 was similar to that of u-PA. PAI-1 was present in serous cells of submucosal glands from allergy samples, while epithelial cells were almost devoid of stain. In contrast, with allergy, immunohistochemical staining of t-PA was negative in submucosal glands, though positive in endothelial cells and epithelium. However, the expression of t-PA mRNA in allergic nasal mucosa was noted in mucous cells. In fibrin autography of nasal discharge, u-PA was markedly activated in the allergic patient. These results suggest that t-PA synthesized in mucous cells is promptly secreted and modifies watery nasal discharge in allergic rhinitis, and that u-PA activity may help the passage of large amounts of rhinorrhea by also reducing its viscosity. A lot of cellular infiltration (eosinophils in particular) was recognized in allergic nasal mucosa. It is most likely that the modifications in expression of PAs and PAIs are due to the local release of cytokines or growth factors from these inflammatory and immune cells.

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Section: Plasminogen Determination Of Nasal Secretionmentioning

confidence: 99%

Expression profiles of fibrinolytic components in nasal mucosa

Sejima

Madoiwa

Mimuro

et al. 2004

Histochem Cell Biol

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“…Estimation of the plasminogen level of blood was performed by a photometric method using chromogenic substrate S-2251 obtained from Kabi Vitrum, Sweden. The antiplasmins in plasma samples were estimated by chromogenic assay using substrate S-2251 [6]. The global fibrinolytic activity (euglobulin fibrinolytic activity) was determined pre and post occlusion following the method recommended by Stormorken et al [7], using euglobulin clot lysis time (ECLT) and fibrin plate lysis [8].…”

Section: Laboratory Investigationsmentioning

confidence: 99%

Thrombophilia in ethnic Arabs in Kuwait

Mohanty

Das

Alhussain

et al. 1996

Annals of Hematology

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One hundred and thirty unrelated patients with recurrent deep venous thrombosis were studied over a period of 4 years (1986-1990) in order to determine the possible etiology. Protein C levels were estimated in plasma both by chromogenic substrate assay and by immunoassay. Protein S levels in plasma was determined by immunoassay using antisera to human protein S. Antithrombin III (AT-III) was assayed using monospecific rabbit antiserum to human AT-III. Fifteen patients were found to have hereditary protein C deficiency (11.52%). Family studies revealed autosomal recessive inheritance in one patient and a dominant pattern in the remaining 14 patients. Protein S deficiency was found in eight cases (6.1%), AT-III deficiency was established in five cases (3.8%) and a fibrinolytic defect in 33 cases (25.4%). Thrombosis of visceral and cerebral vessels and a positive family history were more frequently found among patients who had hereditary deficiency of one or the other antithrombotic factor. Thrombophlebitis of superficial veins was found to be very common in patients with protein C and protein S deficiency and virtually absent in AT-III deficiency. The high frequency of protein C and protein S deficiency in this ethnic group is attributed to the high frequency of consanguinity.

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“…3 The mesenteric veins are a rare but characteristic site of thrombosis in congenital AT III defi ciency, accounting for 8% of reported cases. 4,5 We confi rmed familial AT III defi ciency in our patient. Before enhanced CT scanning became readily available, an objective diagnosis of MVT was diffi cult to establish.…”

Section: Discussionmentioning

confidence: 52%

Superior Mesenteric and Portal Vein Thrombosis Caused by Congenital Antithrombin III Deficiency: Report of a Case

Shibahara

Tatsuta

Orita³

et al. 2007

Surg Today

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A 50-year-old man presented with a 24-h history of gradually worsening abdominal pain. Enhanced computed tomography showed segmental dilation of the small intestine, wall thickening, and ascites, as well as thrombosis of the superior mesenteric vein (SMV) and portal vein. Thus, an emergency laparotomy was performed, which revealed segmental intestinal infarction caused by the thrombosis in the SMV and portal vein. We resected the necrosed intestine and performed anastomosis. The patient was given intravenous heparin and nafamostat mesilate as anticoagulation therapy. The abdominal pain again recurred 4 days after this operation, necessitating a second laparotomy. Segmental congestion of the intestine was found and another resection was done, after which he recovered rapidly. Blood chemistry subsequently revealed an antithrombin III deficiency, which was confirmed to be inherent, after screening his family. Thus, laboratory testing for these proteins may help define the cause of mesenteric venous thrombosis.

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Methods for the Determination of Plasmin, Antiplasmin and Plasminogen by Means of the Substrate S-2251

Cited by 23 publications

References 0 publications

Expression profiles of fibrinolytic components in nasal mucosa

Expression profiles of fibrinolytic components in nasal mucosa

Thrombophilia in ethnic Arabs in Kuwait

Superior Mesenteric and Portal Vein Thrombosis Caused by Congenital Antithrombin III Deficiency: Report of a Case

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