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1.
Fertil Steril ; 93(8): 2581-7, 2010 May 15.
Article in English | MEDLINE | ID: mdl-19962139

ABSTRACT

OBJECTIVE: To examine the impact of unfractionated heparin and low-molecular-weight heparins (LMWHs) on the decidualization of human endometrial stromal cells (ESCs) in vitro. DESIGN: In vitro experiment. SETTING: Research laboratory at a medical university center. PATIENT(S): Premenopausal women undergoing hysterectomy for benign reasons. INTERVENTION(S): The ESCs were isolated from hysterectomy specimens, decidualized in vitro using progesterone and 17beta-estradiol, and incubated with unfractionated heparin and three different LMWHs. MAIN OUTCOME MEASURE(S): Insulin-like growth factor-binding protein (IGFBP) 1, PRL, and insulin-like growth factor (IGF) I were measured using ELISA and real-time reverse-transcription polymerase chain reaction. Cell viability was determined by a fluorometric assay. Intracellular cyclic adenosine 3',5'-monophosphate (cAMP) was measured using a luminescent assay. RESULT(S): Heparin dose- and time-dependently delayed the production of IGFBP-1 and amplified the levels of PRL and IGF-I in ESCs during decidualization in vitro. Similar effects were seen under the influence of the three different LMWHs. Intracellular cAMP was increased in decidualizing ESCs under the influence of heparin and LMWHs. CONCLUSION(S): Unfractionated heparin as well as LMWHs are able to modulate the decidualization of human ESCs in vitro and therefore might be useful to control endometrial differentiation and receptivity in assisted reproduction.


Subject(s)
Decidua/physiology , Endometrium/cytology , Heparin, Low-Molecular-Weight/physiology , Heparin/physiology , Cyclic AMP/metabolism , Female , Humans , Insulin-Like Growth Factor Binding Protein 1/metabolism , Insulin-Like Growth Factor I/metabolism , Prolactin/metabolism , Stromal Cells/cytology
2.
An. med. interna (Madr., 1983) ; 25(1): 4-8, ene. 2008. tab
Article in Es | IBECS | ID: ibc-62972

ABSTRACT

Antecedentes y métodos: Se dispone de datos limitados sobre la utilidad de la profilaxis secundaria de la trombosis venosa profunda (TVP) con heparinas de bajo peso molecular (HBPM). Comparamos dos cohortes de pacientes diagnosticados de TVP. Un grupo tratado con HBPM y otro grupo tratado con anticoagulantes orales. Se valoró la seguridad a la terminación del tratamiento anticoagulante, al año y para la incidencia de fracturas a los 2,5 años. La seguridad se evaluó por la tasa de hemorragias mayores y de fracturas y la eficacia por la tasa de recidiva trombótica precoz (durante el tratamiento anticoagulante) y al año. Resultados: de 65 pacientes tratados con HBPM, presentaron una tasa de hemorragia mayor de 1,5% (IC95% 0,08-9,40) y de fractura de7,7% (IC95% 2,87-17,75), presentaron recidiva temprana 1,5% (IC 95% 0,08-9,40) y recidiva al año 3% (IC95% 0,53-11,64). De 118 pacientes tratados con anticoagulantes orales presentaron una tasa de hemorragia mayor de 3,4% (IC95% 1,09 a 8,97), odds ratio 0,33, una tasa de fractura de 11% (IC95% 16,23 a 18,44), odds ratio 0,66, recidiva temprana de 5% (IC95% 2,08 a 11,20), odds ratio 0,60 y recidiva al año de 3,4% (IC95% 1,09 a 8,97), odds ratio 0,33. Conclusiones: La profilaxis secundaria de la trombosis venosa profunda con HBPM es al menos tan eficaz y segura como el tratamiento con anticoagulantes orales. El tratamiento con HBPM no ha causado incremento de las fracturas


Background and methods: The available data on the utility of low molecular-weight heparins (LMWH) in the secondary prophylaxis of deep vein thrombosis (DVT) are limited. We compared two cohorts of patients diagnosed of DVT. One group followed treatment with LMWH and the other group did with oral anticoagulants (acenocoumarol). Safety was evaluated by the rate of major hemorrhage and 2.5-years period fracture rate, and efficacy was evaluated as the rate of early recurrence and one-year recurrence rate. Results: Of 65 patients treated with LMWH, the hemorrhagic rate was 1.5% (95% CI 0.08-9.40), fracture rate was 7.7% (95% CI 2.87-17.75), early recurrence was 1.5% (95% CI 0.08-9.40) and one-year recurrence was 3% (95% CI 53-11.64). In 118 patients treated with oral anticoagulants the hemorrhagic rate was 3.4% (95% CI 1.09-8.97), odds ratio 0.33, the fracture rate was11% (95% CI 16.23-18.44), odds ratio 0.66, the early recurrence ratewas 5% (95% CI 2.08-11.20), odds ratio 0.60 and one-year recurrence was 3.4% (95%CI 1.09-8.97), odds ratio 0.33. Conclusions: Secondary prophylaxis of DVT with LMWH is as safeand effective as classical treatment with oral anticoagulants. In this study the 2.5-year period fracture rate was similar in both groups of treatment


Subject(s)
Humans , Male , Female , Middle Aged , Venous Thrombosis/therapy , Heparin/therapeutic use , Anticoagulants/therapeutic use , Heparin, Low-Molecular-Weight/therapeutic use , Cohort Studies , Heparin, Low-Molecular-Weight/administration & dosage , Heparin, Low-Molecular-Weight/physiology , Heparin, Low-Molecular-Weight/supply & distribution
4.
J Muscle Res Cell Motil ; 9(3): 233-40, 1988 Jun.
Article in English | MEDLINE | ID: mdl-2842375

ABSTRACT

We have isolated and purified an activity from amoebae of Physarum polycephalum that reduces the flow birefringence of a solution of F-actin in a Ca2+-dependent manner. The purified activity from 100 g of amoebae consisted of 1 mg of a 40,000 mol. wt protein. DNase I-affinity chromatography demonstrated that the protein binds to Physarum actin in a Ca2+-dependent manner, and the binding is not reversed by excess EGTA. Viscometric measurement indicated that the protein (i) accelerates polymerization of G-actin, and (ii) severs F-actin, in a Ca2+-dependent manner. Thus, the protein appeared functionally similar to the fragmin previously isolated from Physarum plasmodia (plasmodial fragmin). However, the two proteins had slightly different mobilities on urea-SDS-PAGE, and antibodies raised against the two proteins scarcely cross-reacted with each other. Hence, we conclude that the two proteins are closely related to but are different from each other, and we have named the novel protein 'myxamoebal fragmin'. Immunoblot analysis indicated that myxamoebal and plasmodial fragmins are specifically present in amoebae and plasmodia, respectively. Results of immunofluorescence staining suggest that the synthesis of plasmodial fragmin is switched on coordinately with the synthesis of the heavy chain of plasmodial myosin and other plasmodium-specific contractile proteins during the apogamic differentiation of amoebae to plasmodia.


Subject(s)
Heparin, Low-Molecular-Weight/isolation & purification , Physarum/analysis , Plasmodium/analysis , Actins/metabolism , Animals , Cell Differentiation , Heparin, Low-Molecular-Weight/physiology , Physarum/cytology
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