Physicochemical and Biological Properties of Human and Canine Plasmins

Takeda, Yosuke; Nakabayashi, Masao

doi:10.1172/jci107533

Cited by 13 publications

(6 citation statements)

References 15 publications

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“…The molecular weight of plasmin monomer is approximately 32,000 (27) and is much smaller than those of FDP and albumin. Only the monomer type of plasmin is detected in vivo (Y. Takeda, personal communication).…”

Section: Discussionmentioning

confidence: 92%

Urine Plasmin-Like Substances as an Index of Kidney Allograft Rejections

Fukao¹,

Kashiwagi²,

Kajiwara³

et al. 1977

Transplantation

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SUMMARYUsing solid state radioimmunoassays developed by the first author, changes in the urine level of plasmin-like substances (PLS) and fibrin degradation products (FDP) before and after human kidney transplantation were determined in 49 transplant patients. Averages of urine PLS and FDP in a normal population of 51 persons were 0.13 ± 0.10 (SD) and 0.14 ± 0.07 μg/ml, respectively. In all transplant patients there was an initial rise of both PLS and FDP in urine immediately after transplantation. This elevation peaked on days 4 and 5 and the PLS and FDP levels returned to normal range within 2 weeks in patients without evidence of rejection. A secondary rise of urine PLS was detected before or with a rise in serum creatinine in all of the patients experiencing rejections. Of 11 patients who showed a rejection episode within 2 weeks of transplantation, the secondary rise of urine PLS was detectable in 55% of the patients slightly before the serum creatinine level changes; of 6 patients with a rejection episode more than 2 weeks after transplantation, 100% showed a secondary PLS rise 6.7 ± 2.3 (SE) days before the serum creatinine increased. The appearance of the secondary rise of urine FDP in the rejecting recipients was slightly later than the rise of PLS. Serial determination of urine PLS levels following human kidney transplantation appears to be an early index of rejections which occurs more than 2 weeks after transplantation, although the clinical usefulness of this measurement is probably limited.Several reports indicate that following human kidney transplantation fibrin degradation products (FDP) appear in urine and that the amount of urine FDP increases during graft rejection (1)(2)(3)5,9,21,25). It has been suggested that the appearance of FDP in urine is the result of the digestive effect of plasmin on fibrin which has been deposited on kidney capillary beds during rejection (25). To date, urine plasmin or plasminogen levels after kidney transplantation have not been studied. A very sensitive radioimmunoassay system (solid state radioimmunoassay) has been developed by the first author in order to measure substances which have common antigenicity to heterologous antiplasminogen antibodies. Using this assay, changes in the levels of these plasmin-like substances (PLS) in urine before and after human kidney allotransplantation have been studied and correlated with FDP levels and with rejection episodes. MATERIALS AND METHODS PatientsForty-nine kidney transplants were studied. Sixteen patients received kidneys from living related donors and 33 from cadaveric donors. The recipients were treated with triple immunosuppressive therapy consisting of cyclophosphamide or azathioprine, prednisone, and antilymphocyte globulin. The onset of rejection was designated as the day when serum creatinine was considered to have increased significantly. Increase of urine protein and decrease of urine sodium or urine volume were considered supporting evidence for rejection. Serum creatinines and other renal chemical paramet...

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Section: Discussionmentioning

confidence: 92%

Urine Plasmin-Like Substances as an Index of Kidney Allograft Rejections

Fukao¹,

Kashiwagi²,

Kajiwara³

et al. 1977

Transplantation

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“…To examine the possibility that an abnormality in neuraminic acid might be responsible for the apparent increase in molecular weight of the nonfunctional inhibitors, the inhibitor preparations were incubated with varying concentrations of neuraminidase for I It is not clear why the glycerol-activated plasmin-Ci inactivator complex failed to remain intact in the presence of SDS and urea. One possibility is suggested by the study of Takeda and Nakabayashi, which demonstrated that glycerolactivated plasmin underwent autodigestion and therefore possessed a lower molecular weight than did freshly activated plasmin (13). These considerations have suggested that the degraded enzyme may have a deficiency in binding sites and hence may form a complex with C!…”

Section: Resultsmentioning

confidence: 99%

Studies on human plasma C1 inactivator-enzyme interactions. II. Structural features of an abnormal C1 inactivator from a kindred with hereditary angioneurotic edema.

Harpel¹,

Hugli²,

Cooper³

1975

J. Clin. Invest.

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A B S T R A C T The function and several of the structural features of the C! inactivator protein isolated from the plasma of a mother and daughter with the variant form of hereditary angioneurotic edema have been examined. These abnormal inhibitors shared immunologic identity with the normal C! inactivator protein; however, they were inactive in inhibiting the functional activity of Cis. Analysis of the abnormal inhibitors by sodium dodecyl sulfate (SDS) acrylamide gel electrophoresis suggested that each consisted of a single polypeptide chain, the mobility of which was slower than that of the normal C1 inactivator. The apparent molecular weight of the patients' inhibitors was 109,000 daltons as contrasted to 105,000 daltons, that of the normal C1 inactivator. The abnormal inhibitors failed to form a complex with Cls or plasmin as analyzed by SDS-acrylamide gels. The large proteolytic derivatives resulting from the plasmin-and trypsin-induced degradation of the abnormal inhibitors were approximately 3,000 daltons heavier than the corresponding products derived from normal C1 in-A preliminary report of this study appeared in abstract form (1974. J. Clin. Invest. 53: 31 a).

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“…It is our feeling that the fibrinogen molecule, whether *I-labelled or not is quite delicate. This may be partly due to its propensity to accompany plasminogen or adsorb to plasmin [259] during purification. Thus we take great care with our preparations for metabolic experiments.…”

Section: Satisfactory Labelling Of Fibrinogen With Radioactive Iodinementioning

confidence: 99%

Fibrinogen Synthesis, Distribution and Degradation

Reeve¹,

Franks²

2008

Semin Thromb Hemost

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Fibrinogen is a plasma protein of approximately 340,000 daltons containing everal per cent carbohydrate [169]. It is at least chiefly synthesized in the liver [156]. On exposure to thrombin it loses peptides [169] and forms long thin solid fibers [82]. These under the influence of fibrinase, Factor XIII [126,133], become markedly insoluble in the blood and tissue fluids, unless attacked by proteolytic enzymes such as plasmin [225]. Collections of intertwined fibers block holes in vessels thereby inhibiting blood loss, sometimes block the lumen of vessels thereby causing thrombosis, sometimes circulate in the blood stream till they lodge in vessels to cause emboli [72] and probably form a matrix for cell growth as in wound healing [7,278] and neoplastic spread [4]. A number of the many recent reviews of various aspects of fibrinogen behavior are noted below. Particularly relevant to what follows are reviews of the molecular structure of fibrinogen [169], the effects of proteolytic enzymes on fibrinogen [137], the pathways of catabolism of fibrinogen [167], the polymerization of fibrin monomers [63], the plasma and tissue fibrinogenolytic and fibrinolytic enzyme systems [152] and the control of protein synthesis in metazoan cells [168,271,232]. This review attempts to describe the physiology and pathophysiology of fibrinogen as it is synthesized, distributed to the blood stream and tissue fluids and catabolized, and to relate its somewhat extraordinary behavior to a few relevant features of what is known about other proteins. This requires discussion of some recent methods for studying fibrinogen metabolism and presentation of a picture of the fibrinogen molecule in continual motion from the time during which it is synthesized till the time when it is broken down through one or other of its several possible catabolic pathways. Also, this requires, because of the resulting clarification-and perhaps some readers may think this unfortunate-the use of some elementary mathematics of rate processes, which we try to keep as simple as possible and the use of which is

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Physicochemical and Biological Properties of Human and Canine Plasmins

Cited by 13 publications

References 15 publications

Urine Plasmin-Like Substances as an Index of Kidney Allograft Rejections

Urine Plasmin-Like Substances as an Index of Kidney Allograft Rejections

Studies on human plasma C1 inactivator-enzyme interactions. II. Structural features of an abnormal C1 inactivator from a kindred with hereditary angioneurotic edema.

Fibrinogen Synthesis, Distribution and Degradation

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