Free Form Plenoptic Video Acquisition and Visualization System

Summary Aim: The cellular joint infiltrate in rheumatoid arthritis patients is rich in CD4-positive T-helper lymphocytes and macrophages, rendering anti-CD4 monoclonal antibodies (mAbs) suitable for specific immunoscintigraphy of human/ experimental arthritis. Following intravenous injection, however, mAbs are present both in the free form and bound to CD4-positive, circulating monocytes and T-cells. Thus, the present study aimed at analyzing the relative contribution of the free and the cell-bound component to the imaging of inflamed joints in experimental adjuvant arthritis (AA). Methods: AA rat peritoneal macrophages or lymph node T-cells were incubated in vitro with saturating amounts of 99mTc-anti-CD4 mAb (W3/25) and injected i.v. into rats with AA. Results: In vitro release of 99mTc-anti-CD4 mAb from the cells was limited (on average 1.57%/h for macrophages and 0.84%/h for T-cells). Following i.v. injection, whole body/joint scans and tissue measurements showed only negligible accumulation of radioactivity in inflamed ankle joints (tissue: 0.22 and 0.34% of the injected activity, respectively), whereas the radioactivity was concentrated in liver (tissue: 79% and 71%, respectively), kidney, and urinary bladder. Unlike macrophages, however, anti-CD4 mAb-coated T-cells significantly accumulated in lymphoid organs, the inflamed synovial membrane of the ankle joints, as well as in elbow and knee joints. Conclusion: While the overall contribution of cell-bound mAbs to the imaging of arthritic joints with anti-CD4 mAbs is minimal, differential accumulation of macrophages and T-cells in lymphoid organs and the inflamed synovial membrane indicates preferential migration patterns of these 2 cell populations in arthritic rats. Although only validated for 99mTc-anti-CD4 mAbs, extrapolation of the results to other anticellular mAbs with similar affinity for their antigen may be possible.

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Immunoreactivity of Tissue Plasminogen Activator and of Its Inhibitor Complexes

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646605 ◽

1989 ◽

Vol 61 (03) ◽

pp. 409-414 ◽

Cited By ~ 70

Author(s):

M Rånby ◽

G Nguyen ◽

P Y Scarabin ◽

M Samama

Keyword(s):

Plasminogen Activator ◽

Tissue Plasminogen Activator ◽

Degradation Products ◽

Gel Filtration ◽

Free Form ◽

Enzyme Linked Immunosorbent Assay ◽

Plasma Samples ◽

Significant Difference ◽

Tissue Plasminogen ◽

Pai 1

SummaryAn enzyme linked immunosorbent assay (ELISA) based on goat polyclonal antibodies against human tissue plasminogen activator (tPA) was evaluated. The relative immunoreactivity of tPA in free form and tPA in complex with inhibitors was estimated by ELISA and found to be 100, 74, 94, 92 and 8l% for free tPA and tPA in complex with PAI-1, PAI-2, α2-antiplasmin and C1-inhibitor, respectively. Addition of tPA to PAI-1 rich plasma resulted in rapid and total loss of tPA activity without detectable loss of ELISA response, indicating an immunoreactivity of tPA in tPA/PAI-1 complex of about l00%. Three different treatments of citrated plasma samples (acidification/reneutralization, addition of 5 mM EDTA or of 0.5 M lysine) prior to determination by ELISA all resulted in increased tPA levels. The fact that the increase was equally large in all three cases along with good analytical recovery of tPA added to plasffi, supported the notion that all tPA antigen present in plasma samples is measured by the ELISA. Analysis by ELISA of fractions obtained by gel filtration of plasma from a patient undergoing tPA treatment identified tPA/inhibitor complexes and free tPA but no low molecular weight degradation products of tPA. Determinations of tPA antigen were made at seven French clinical laboratories on coded and randomized plasma samples with known tPA antigen content. For undiluted samples there was no significant difference between the tPA levels found and those known to be present. The between-assay coefficient of variation was 7 to 10%. In conclusion, the ELISA appeared suited for determination of total tPA antigen in human plasma samples.

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The Different Forms of Antithrombin III in Serum

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651855 ◽

1977 ◽

Vol 38 (02) ◽

pp. 0494-0503 ◽

Cited By ~ 18

Author(s):

D. S Pepper ◽

D Banhegyi ◽

J. D Cash

Keyword(s):

Molecular Weight ◽

Affinity Chromatography ◽

Human Serum ◽

Degradation Product ◽

Antithrombin Iii ◽

Gel Filtration ◽

Free Form ◽

Polymeric Form ◽

At Iii ◽

Human Thrombin

SummaryAntithrombin III (AT III) complexes were isolated from human serum by affinity chromatography and gel filtration. In the first step of the preparation, using heparin-agarose chromatography, we observed that the complexed form of AT III bound less strongly to the gel than the free form and that about half of the AT III was free. With further purification a 2.5 × 105 molecular weight complex was isolated. Using 125I labelled human thrombin, this complex was radioactive indicating the presence of thrombin. Only in a synthetic thrombin-AT III system was a 9 × 104 molecular weight complex detected, but not in serum. These facts suggest that in serum AT III complexes may exist in a polymeric form. Also, an AT III antigen derived from the original AT III molecule, but not complexed, was isolated which may be a degradation product.Abbreviations used: AT-III, antithrombin III. Hepes, N-2-Hydroxyethylpiperazine-N-2-Ethanesulphonic acid.

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Effect of Depolymerized Holothurian Glycosaminoglycan (DHG) on Tissue Factor Pathway Inhibitor: In Vitro and In Vivo Studies

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657643 ◽

1997 ◽

Vol 78 (02) ◽

pp. 864-870 ◽

Cited By ~ 9

Author(s):

Hideki Nagase ◽

Kei-ichi Enjyoji ◽

Yu-ichi Kamikubo ◽

Keiko T Kitazato ◽

Kenji Kitazato ◽

...

Keyword(s):

Tissue Factor ◽

Tissue Factor Pathway Inhibitor ◽

Factor Xa ◽

Free Form ◽

Initial Reaction ◽

Extrinsic Pathway ◽

Factor Xa Inhibition ◽

Tissue Factor Pathway

SummaryDepolymerized holothurian glycosaminoglycan (DHG) is a glycosaminoglycan extracted from the sea cucumber Stichopus japonicusSelenka. In previous studies, we demonstrated that DHG has antithrombotic and anticoagulant activities that are distinguishable from those of heparin and dermatan sulfate. In the present study, we examined the effect of DHG on the tissue factor pathway inhibitor (TFPI), which inhibits the initial reaction of the tissue factor (TF)-mediated coagulation pathway. We first examined the effect of DHG on factor Xa inhibition by TFPI and the inhibition of TF-factor Vila by TFPI-factor Xa in in vitro experiments using human purified proteins. DHG increased the rate of factor Xa inhibition by TFPI, which was abolished either with a synthetic C-terminal peptide or with a synthetic K3 domain peptide of TFPI. In contrast, DHG reduced the rate of TF-factor Vila inhibition by TFPI-factor Xa. Therefore, the effect of DHG on in vitroactivity of TFPI appears to be contradictory. We then examined the effect of DHG on TFPI in cynomolgus monkeys and compared it with that of unfractionated heparin. DHG induced an increase in the circulating level of free-form TFPI in plasma about 20-fold when administered i.v. at 1 mg/kg. The prothrombin time (PT) in monkey plasma after DHG administration was longer than that estimated from the plasma concentrations of DHG. Therefore, free-form TFPI released by DHG seems to play an additive role in the anticoagulant mechanisms of DHG through the extrinsic pathway in vivo. From the results shown in the present work and in previous studies, we conclude that DHG shows anticoagulant activity at various stages of coagulation reactions, i.e., by inhibiting the initial reaction of the extrinsic pathway, by inhibiting the intrinsic Xase, and by inhibiting thrombin.

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Correlational Methods for Analysis of Dance Movements

Dance Research ◽

10.3366/drs.2011.0021 ◽

2011 ◽

Vol 29 (supplement) ◽

pp. 283-304 ◽

Cited By ~ 8

Author(s):

Timothy R. Brick ◽

Steven M. Boker

Keyword(s):

Motion Capture ◽

Mirror Symmetry ◽

Cross Correlation ◽

The Other ◽

Free Form ◽

Motion Capture Data ◽

Complex Interactions ◽

Dance Movements ◽

Time Lagged ◽

Insight Into

Among the qualities that distinguish dance from other types of human behavior and interaction are the creation and breaking of synchrony and symmetry. The combination of symmetry and synchrony can provide complex interactions. For example, two dancers might make very different movements, slowing each time the other sped up: a mirror symmetry of velocity. Examining patterns of synchrony and symmetry can provide insight into both the artistic nature of the dance, and the nature of the perceptions and responses of the dancers. However, such complex symmetries are often difficult to quantify. This paper presents three methods – Generalized Local Linear Approximation, Time-lagged Autocorrelation, and Windowed Cross-correlation – for the exploration of symmetry and synchrony in motion-capture data as is it applied to dance and illustrate these with examples from a study of free-form dance. Combined, these techniques provide powerful tools for the examination of the structure of symmetry and synchrony in dance.

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ISOLATION AND IDENTIFICATION OF 16-OXOOESTRADIOL-17β IN HUMAN PLACENTAE

Acta Endocrinologica ◽

10.1530/acta.0.xxxii0195 ◽

1959 ◽

Vol XXXII (II) ◽

pp. 195-208 ◽

Cited By ~ 13

Author(s):

E. Diczfalusy ◽

Anne-Marie v. Münstermann

Keyword(s):

Ethanol Extract ◽

Full Term ◽

Free Form ◽

Isolation And Identification ◽

Human Placentae

ABSTRACT From the ethanol extract of 100 full term placentae approximately 200 μg of an α-ketolic Kober chromogen have been isolated in a »free« form. The evidence obtained indicates that this α-ketolic Kober chromogen is identical with 16-oxooestradiol-17β.

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