Polyamines as physiological substrates for transglutaminases.

Folk, J.E.; Park, M.H.; Chung, Soo Il; Schrode, James; Lester, Eric P.; Cooper, Herbert L.

doi:10.1016/s0021-9258(19)85760-5

Cited by 293 publications

(14 citation statements)

References 25 publications

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“…PAs were reported to regulate the activity of TGase in many functions, including cell differentiation, post-translational protein modification, kinase activity, wound healing, and signal transduction [ 88 , 89 , 90 ]. Mammalian tissue transglutaminase (TG2) catalyzes protein post-translational change by adding PAs into protein or forming epsilon lysine bonds in an inter- or intramolecular cross-link manner [ 91 , 92 ]. On the other hand, a higher enzyme activity of TG2 was found to be associated with various neuropathological conditions (acute and chronic) such as amyotrophic lateral sclerosis (ALS), Huntington’s disease, Alzheimer’s disease, and Parkinson’s disease [ 93 , 94 ].…”

Section: Types Structures and Functions Of Pasmentioning

confidence: 99%

Polyamines: Functions, Metabolism, and Role in Human Disease Management

et al. 2021

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Putrescine, spermine, and spermidine are the important polyamines (PAs), found in all living organisms. PAs are formed by the decarboxylation of amino acids, and they facilitate cell growth and development via different cellular responses. PAs are the integrated part of the cellular and genetic metabolism and help in transcription, translation, signaling, and post-translational modifications. At the cellular level, PA concentration may influence the condition of various diseases in the body. For instance, a high PA level is detrimental to patients suffering from aging, cognitive impairment, and cancer. The levels of PAs decline with age in humans, which is associated with different health disorders. On the other hand, PAs reduce the risk of many cardiovascular diseases and increase longevity, when taken in an optimum quantity. Therefore, a controlled diet is an easy way to maintain the level of PAs in the body. Based on the nutritional intake of PAs, healthy cell functioning can be maintained. Moreover, several diseases can also be controlled to a higher extend via maintaining the metabolism of PAs. The present review discusses the types, important functions, and metabolism of PAs in humans. It also highlights the nutritional role of PAs in the prevention of various diseases.

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Section: Types Structures and Functions Of Pasmentioning

confidence: 99%

Polyamines: Functions, Metabolism, and Role in Human Disease Management

et al. 2021

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“…Cell lysates were prepared with cells from 10 dishes (0.1 ml of washed cells) by suspending the cells in 4 ml of PBS, sonicating them (10 s at 70 W), and finally centrifuging them for 30 min at 25 000 g. The lysates were treated with solid (NH % ) # SO % (40-80 % saturation cut) and the precipitate was hydrolysed in 6 M HCl at 110 mC for 18 h. The hydrolysates were applied to 0.5 cmi4 cm columns of AG 50i2 (H + form, 200-400 mesh) and eluted with 30 ml of 1 M HCl, 20 ml of 3 M HCl and 30 ml of 6 M HCl. The hypusine contained in the 3 M HCl fraction was determined by using a reverse-phase HPLC method described elsewhere [9,31].…”

Section: Isolation Purification and Identification Of Hypusinementioning

confidence: 99%

Interferon α2 recombinant and epidermal growth factor modulate proliferation and hypusine synthesis in human epidermoid cancer KB cells

Caraglia

Passeggio

Beninati

et al. 1997

Biochemical Journal

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We previously found that interferon alpha2 recombinant (IFNalpha) increases the expression of epidermal growth factor receptor (EGF-R) in the human epidermoid cancer KB cell line. Here we report the effects of IFNalpha and epidermal growth factor (EGF) on KB cell cycle kinetics. IFNalpha (1000 i.u./ml) for 48 h decreased the S-phase fraction and diminished the expression of Ki67 and proliferating cell nuclear antigen on KB cells. Incubation of IFNalpha-treated KB cells with 10 nM EGF for 12 h reversed these effects. We then studied several biochemical markers of cell proliferation. Ornithine decarboxylase activity was decreased to about one-tenth by IFNalpha and partly restored by EGF. Hypusine is contained only in eukaryotic initiation factor 5A and its levels are correlated with cell proliferation. IFNalpha decreased hypusine synthesis by 75%; exposure of cells to EGF for 12 h restored hypusine synthesis almost completely. We also studied the effects of IFNalpha on the cytotoxicity of the recombinant toxin TP40, which inhibits elongation factor 2 through EGF-R binding and internalization. IFNalpha greatly enhanced the TP40-induced inhibition of protein synthesis in KB cells. In conclusion, IFNalpha, which affects protein synthesis machinery and increases EGF-R expression, enhances the tumoricidal activity of TP40 and hence could be useful in the setting of anti-cancer therapy.

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“…Protein-conjugate polyamines levels in transfected Balb-C 31"3 cells (24 h after confluency was reached) were measured by addition of 3Hputrescine (5/~Ci) to the culture medium followed by isolation and quantitation of conjugated glutamines (Piacentini et al, 1988). Determination of radiolabeled derivatives was performed on aliquots of enzymatic digests of the acid-insoluble fraction, using the automated ion exchange chromatography procedure as described previously (Folk et al, 1980).…”

Section: Quantitation Of Protein-conjugate Polyamines and E-(~-glutamyl)-lysinementioning

confidence: 99%

Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion.

Gentile

Thomázy

Piacentini

et al. 1992

The Journal of Cell Biology

226

150

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Abstract. Tissue transglutaminase is a cytosolic enzyme whose primary function is to catalyze the covalent cross-linking of proteins. To investigate the functions of this enzyme in physiological systems, we have established lines of Balb-C 3T3 fibroblasts stably transfected with a constitutive tissue transglutaminase expression plasmid. Several cell lines expressing high levels of catalytically active tissue transglutaminase have been isolated and characterized. Transglutaminasetransfected cells showed morphologic features quite distinct from their nontransfected counterparts. Many of the cells showed an extended and very flattened morphology that reflected increased adhesion of the cells to the substratum. Other cells, particularly those showing the highest levels of intracellular transglutaminase expression, showed extensive membrane blebbing and cellular fragmentation. The results of these experiments suggest that the induction and activation of tissue transglutaminase may contribute both to changes in cellular morphology and adhesiveness.

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Polyamines as physiological substrates for transglutaminases.

Cited by 293 publications

References 25 publications

Polyamines: Functions, Metabolism, and Role in Human Disease Management

Polyamines: Functions, Metabolism, and Role in Human Disease Management

Interferon α2 recombinant and epidermal growth factor modulate proliferation and hypusine synthesis in human epidermoid cancer KB cells

Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion.

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