Evidence for the Existence of Foetal Fibrinogen

Witt, I.; Müller, Hannelore; Künzer, W

doi:10.1055/s-0038-1651331

Cited by 58 publications

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“…The antithrombin-binding and thrombin-binding results provide significant preliminary evidence for the hypothesis that age-related structural differences in hemostatic proteins play a significant role in the response of this system to anticoagulants. This idea is consistent with previous studies that have identified a ÔfetalÕ form of fibrinogen [18], as well as a ÔneonatalÕ form of protein C [19], which demonstrated differences in sialic acid content and variation in the number of single-chained molecules, respectively. In addition, antithrombin is known to exist in two glycoforms, a-antithrombin and bantithrombin.…”

Section: Discussionsupporting

confidence: 93%

“…As well as differences in heparin binding to plasma proteins across the age-groups, interindividual differences among the individuals from the same age-group were observed (data not shown). The average number and range of individual protein bands automatically detected on silver-stained gels were: 15 (13-18) for day 1; 16 (14-19) for day 3; 18 (16)(17)(18)(19)(20) for < 1 year; 18 (13-22) for 1-5 years; 18 (17-20) for 6-10 years; 17 (3-21) for 11-16 years; and 16 (13)(14)(15)(16)(17)(18)(19)(20) for adults.…”

Section: Statisticsmentioning

confidence: 99%

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Age‐specific differences in binding of heparin to plasma proteins

Ignjatović

Straka

Summerhayes

et al. 2010

Journal of Thrombosis and Haemostasis

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Summary. Background: Clinically significant age-related differences in the anticoagulation effect of heparin have previously been established in vitro as well as in different clinical settings in vivo. These differences were hypothesized to be due to the age-specific differences in binding of heparin to plasma proteins. Objectives: The aim of this project was to investigate global agerelated differences in heparin binding to plasma proteins. Patients/Methods: Heparin-binding proteins were identified by incubating heparin-coated magnetic beads with plasma samples from neonates, children and adults, and purifying the proteins that were bound to the beads in this reaction system. Results: These results provide the first preliminary evidence of age-related differences in the total number and concentration of proteins bound to heparin. The results also suggest, for the first time, that there are age-related differences of heparin binding to antithrombin and thrombin. Conclusions: The results of this study, although preliminary, support and contribute to the explanation of the mechanism of age-related differences in the effect of heparin observed previously in vitro and in vivo.

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Section: Discussionsupporting

confidence: 93%

Section: Statisticsmentioning

confidence: 99%

Age‐specific differences in binding of heparin to plasma proteins

Ignjatović

Straka

Summerhayes

et al. 2010

Journal of Thrombosis and Haemostasis

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“…Functional anomalies of fibrinogen [1], prothrombin [2,3], hemoglobin [4,5], and human plasminogen (PLG) [6], have been described in full-term newborns, and physi cal differences between fetal and adult pro teins have been documented, especially regardingthe hemoglobin chains [5]. A variant adult PLG has been described in which a sin gle amino acid substitution of alanine by threonine near the active site histidine resi due caused the formation of an inactive plas min (PLN) [7], This variant PLG was char acterized by isoelectric focusing analyses and high-performance liquid chromatography (HPLC) [8].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Human Normal, Full-Term, Fetal and Adult Plasminogen by Physical and Chemical Analyses

Summaria

1989

Pathophysiol Haemos Thromb

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Human fetal plasminogen was isolated from fetal cord blood obtained from full-term normal newborns. Two fetal plasminogen preparations were characterized by physical analyses and compared to adult human Glu-plasminogen. The protein concentration of plasminogen in each full-term fetal plasma was approximately 50% of the concentration found in adult plasma. The specific activity of the isolated plasminogen from both full-term fetal plasmas was 28.8 ± 1.5 IU/mg protein, approximately the same as that of adult Glu-plasminogen. No significant difference was observed in the rate at which plasmin was generated from the normal fetal plasminogen and the adult Glu-plasminogen using streptokinase, urokinase, and tissue plasminogen activator. Electrophoretic analyses in an acrylamide gel/sodium dodecyl sulfate dissociating system showed that the fetal plasminogens and the adult Glu-plasminogen were the same molecular size. Analyses in an acrylamide gel isoelectric focusing system indicated that fetal and adult plasminogen both contained the same twelve isoelectric forms, however, there was a slight difference in the distribution of the isoelectric forms. The fetal and adult plasminogens both contained 792 ± 1 amino acid residues, and there were no significant differences in amino acid composition between the fetal and adult preparations. These comparisons indicate that normal, full-term, fetal and adult Glu-plasminogen are identical.

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“…The most extensive infomation exists for fibrinogen which sheep. The adult sheep received 100 pCi of '25~-labeled fetal is thought to exist in a fetal form with an increased sialic acid fibrinogen, 100 pCi of I3'I-labeled adult fibrinogen, and/or 100 content in the newborn infant (3)(4)(5)(6). l-here is no infomation on pCi of Iz5I-labeled albumin, whereas the newborn lambs radioactivity in a weir-type y-scintillation eounter that allowed 249 for correction if both '''I and I3'I were used.…”

mentioning

confidence: 99%

Fibrinogen Has a Rapid Turnover in the Healthy Newborn Lamb

et al. 1988

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ABSTRACT. The half-lives for coagulation factors in the the response of the "fetal" fibrinogen to thrombin in vivo. Many healthy newborn infant are not known and may be different of these questions can only be asked ethically in an animal model than for the adult. We measured the half-life for fetal of newborn coagulation. We have used the sheep model to sheep fibrinogen and compared it to the half-life of adult investigate the clearance and response to thrombin of "fetal" and sheep fibrinogen. Fibrinogen was purified from adult and adult fibrinogen. Our results show that fibrinogen, whether adult fetal sheep plasma and radiolabeled with either '251 or 13'I. or fetal, has a faster turnover in the newborn compared to the The half-lives for these fibrinogens were determined in the adult and that both adult and fetal fibrinogen have a similar adult sheep and newborn lamb. In addition, the fetal and response in vivo to thrombin. adult sheep fibrinogens were compared by reptilase time, thrombin clotting time, sialic acid content, and the behavior of the N-glycans derived from these fibrinogens on the MATERIALS AND METHODS immobilized lectin, Sepharose-concanavalin A. Finally, the ~~i~~l model, plasma for purification of fibrinogen was obin vivo response of coinjected radiolabeled fibrinogens to tained from adult sheep and from fetal lambs at approximately increasing doses of infused thrombin was determined. The 100 days gestation with tern being 147 days gestation. T~ obtain fetal sheep fibrinogen differed from the adult as indicated the fetal plasma, the pregnant ewe was given an epidural anesby a prolonged reptilase time and an increased sialic acid thetic supplemented with sedative doses of sodium pentobarbital content residues/340 Kd versus adult: 8-9 by continuous intravenous infusion. The fetal lamb was partially residues1340 Kd). The latter was also reflected in differing delivered in a breech position through a uterine incision. silastic chromotographic profiles for the N-gl~cans on Se~harose-catheters were placed in the fetal lamb's femoral artery and the concanavalin A. The half-lives for both the adult and fetal fetal blood obtained. fibrinogen were significantly more rapid in the newborn Fibrinogen purification. Blood for fibrinogen purification was lamb (fetal: 47 2-0 h; adult: 46 2-4 h, mean SEM) collected into polypropylene tubes containing 3.8% sodium citthan in the adult (fetal: 116 f 6.5 h; adult: 121 f 6.9 h). rate and EACA. A fraction of the blood obtained was centrifuged Finally, the adult and fetal sheep fibrinogen responded to at 3000 x g for 20 min and multiple aliquots of the plasma thrombin in an identical fashion in the intact animal. In sample frozen at -70" c for future coagulation assay. ~h~ summary, both adult and fetal fibrinogen have faster half-remaining plasma was used for fibrinogen purification according lives in the lamb compared to the adult, despite a higher to the method of Straughn and Wagner (7). In brief, the fibrinsialic acid content for the fetal fibrinogen. We speculate ...

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Evidence for the Existence of Foetal Fibrinogen

Cited by 58 publications

References 0 publications

Age‐specific differences in binding of heparin to plasma proteins

Age‐specific differences in binding of heparin to plasma proteins

Comparison of Human Normal, Full-Term, Fetal and Adult Plasminogen by Physical and Chemical Analyses

Fibrinogen Has a Rapid Turnover in the Healthy Newborn Lamb

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