Differences in polyamine availability and insertion into fibronectins released from normal and transformed cells

Roch, Anne-Marie; Quash, G.; Ripoll, Huguette; Mardon, M.

doi:10.1042/bj2100137

Cited by 12 publications

(3 citation statements)

References 32 publications

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“…polyamines in human plasma [9]. These polyamines could be bound to cellular proteins within the tumour and then released into the circulation as demonstrated for fibronectin in cellular culture media [26], or could be excreted in the free state in plasma and bound to existing plasma proteins by the action of factor XIII as we have shown previously [12] These observations lend support to the existence of naturally occurring y-glutamyl-polyamine bonds. However, they do not allow us to differentiate between a decrease in individual glutamine residues of the same or different proteins.…”

supporting

confidence: 63%

Protein‐bound polyamines in the plasma of mice grafted with the Lewis lung carcinoma

et al. 1987

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Protein-bound polyamines were isolated from the plasma of mice using antipolyamine antibodies covalently linked to magnetic latex spheres. Their subsequent separation by polyacrylamide gel electrophoresis (PAGE) showed that in plasma from normal mice, 3 proteins (27, 55 and 82 kDa) carrying polyamines could be visualized, whereas in mice bearing the Lewis lung carcinoma at least 8 other proteins of higher molecular mass (5 of 94,110,130,145 and 160 kDa, and 3 of > 170 kDa) had bound polyamines. These protein-bound polyamines could be detected from the first week after tumour graft; they increased during the second and third week but decreased thereafter. These proteins were not bound by immunolatex spheres preincubated with spermine bound to a protein-carrier insulin. Moreover, the appearance of these protein-bound polyamines was not a consequence of the inflammatory process since in mice infected with heat-inactivated Brucella abortus, with the exception of a 65 kDa protein, polyamines were bound to the same proteins found in normal mice. In mice grafted with the Lewis lung carcinoma the concomitant decrease in transglutaminase-mediated polyamine (e.g. putrescine) binding capacity of plasma proteins provides additional evidence for the presence in vivo of polyamines already bound to plasma proteins.

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supporting

confidence: 63%

Protein‐bound polyamines in the plasma of mice grafted with the Lewis lung carcinoma

et al. 1987

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“…In plasma, FXIII is a zymogen that is activated by thrombin in the presence of calcium and plays an important role in blood coagulation by establishing N ε (γ‐ l ‐glutamyl)lysine cross‐links between fibrin chains [5]. As well as this well‐known physiological property, other plasma proteins cross‐linked by FXIII are α2 anti‐plasmin [6], factor V [7] and fibronectin [8].…”

Section: Introductionmentioning

confidence: 99%

Development and evaluation of a modified colorimetric solid‐phase microassay for measuring the activity of cellular and plasma (Factor XIII) transglutaminases

Thomas

Alaoui

Massignon

et al. 2006

Biotech and App Biochem

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Plasma TG (transglutaminase) [FXIII (Factor XIII)] stabilizes fibrin and plays an essential role in haemostasis. In the present paper, we report a simple colorimetric assay for measuring FXIII activity. The advantage of this approach, compared with all the other solid-phase assays described so far for measuring TG activity, is that the first substrate, namely the synthetic dipeptide, N-benzyloxycarbonyl-L-Gln-L-Gly, is coupled covalently by its C-terminus with amine-substituted polystyrene plates. Covalent coupling eliminates the problem of desorption of proteins such as casein and N,N'-dimethylcasein (first substrates) when 'blocking' buffers containing proteins, e.g. BSA, are employed, or when samples of plasma or cell homogenates are used. The principle of the assay itself is based on the incorporation of the well-known second substrate, 5-(biotinamido)pentylamine, into the gamma-carboxamide of glutamine in the immobilized dipeptide. The amount of biotinylated amine bound to the plate, as measured by the phosphatase activity of Extravidin phosphatase attached to the biotin moiety, is directly proportional to the TG activity. The method shows strong correlation (r = 0.96) with the radiometric assay for FXIII activity. For plasma samples, a linear response was obtained in the range 0-1.33 i.u. (international unit)/ml, versus the Behring standard. In a preliminary clinical investigation, the method was applied to normal and pathological plasma samples from patients with liver failure and disseminated intravascular coagulation. In the isolation of TG from guinea-pig liver, it was used to measure enzyme activity after each purification step. This method is rapid, sensitive and can easily be applied to routine clinical analyses and to specific research problems.

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“…In some cases, polyamines linked to particular proteins have been isolated [3,24,251. In animals, post-translation covalent linkages of polyamines to numerous proteins have been demonstrated.…”

Section: Introductionmentioning

confidence: 99%

Transglutaminase-like activity in Chrysanthemum leaf explants cultivated in vitro in relation to cell growth and hormone treatment

1995

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In Chrysanthemum leaf explants cultivated in vitro the capacity to covalently link polyamines to protein substances exists. This plant enzyme activity shows some similarities with mammalian transglutaminases. In foliar explants cultured on a medium promoting bud or root formation increasing levels of transglutaminase-like activity occurred during the first days of culture when cell multiplication was rapid then the levels declined as the rate of cell division decreased and differentiation occurred. Undifferentiated callus exhibited low transglutaminase-like activity. Transglutaminase-like activity also increased in rapidly proliferating and growing organs (roots and buds initiated from the foliar explants) and decreased during maturity. The relationship among transglutaminases-like activity, cell division, bud and root formation is discussed.Abbreviations: TGase = transglutaminase; BA = benzyladenine; 2,4-D = 2,4-dichlorophenoxyacetic acid; Put = putrescine; Spd = spermidine.-

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Differences in polyamine availability and insertion into fibronectins released from normal and transformed cells

Cited by 12 publications

References 32 publications

Protein‐bound polyamines in the plasma of mice grafted with the Lewis lung carcinoma

Protein‐bound polyamines in the plasma of mice grafted with the Lewis lung carcinoma

Development and evaluation of a modified colorimetric solid‐phase microassay for measuring the activity of cellular and plasma (Factor XIII) transglutaminases

Transglutaminase-like activity in Chrysanthemum leaf explants cultivated in vitro in relation to cell growth and hormone treatment

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