Selective polyamine-binding proteins spermine binding by an androgen-sensitive phosphoprotein

Liang, Tehming; Mezzetti, Gabriele; Chen, Chunshing; Liao, Shutsung

doi:10.1016/0304-4165(78)90374-4

Cited by 37 publications

(18 citation statements)

References 23 publications

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“…Oxidized spermine has also been found to combine with nucleotides and DNA (Eilon & Bachrach, 1969). Polyamines in general are known to bind to many substances including glass, but there is also evidence of specific binding of spermine to phosphoprotein (Liang et al, 1978). We have shown that the dioxidized form also binds to an uncharacterized component in serum.…”

Section: Discussionmentioning

confidence: 72%

Evidence for serum binding of oxidized spermine and its potent G1-phase inhibition of cell proliferation

Gaugas¹,

Dewey²

1979

Br J Cancer

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Summary.-Serum polyamine oxidase (EC 1.4.3.4) is known to react in vitro with radio-labelled spermine4+ to produce di-oxidized spermine which must incorporate the label. Di-oxidized spermine was compatible with a radio-labelled compound2+ separated from the reaction mixture by ion-exchange chromatography. The compound was measured and had a half-life of about 2-3 h in tissue culture medium. It also rapidly and tightly bound to an unidentified serum component (gel-filtration chromatography indicated a complex of mol. wt 70,000) so that dissociation required treatment with strong acid (ION HCI). Findings suggest that the di-oxidized spermine, in either its free cationic or bound form, potently arrested cell proliferation. This arrest was non-cytotoxic and was confined to the G1 phase of the cell cycle. Products of di-oxidized spermine autodegradation, including trace amounts of stable and cytotoxic acrolein (arrested S phase), were unlikely to have contributed significantly to the arrest.

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Section: Discussionmentioning

confidence: 72%

Evidence for serum binding of oxidized spermine and its potent G1-phase inhibition of cell proliferation

Gaugas¹,

Dewey²

1979

Br J Cancer

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“…Such a primary disorder in polyamine metabolism could be any of the following: (a) overactivity in one or more enzymes of polyamine biosynthesis (4,22); (b) deficient activity in enzyme(s) responsible for oxidizing (4,22) or conjugating the polyamines (23); (c) augmented binding of polyamines by cytoplasmic proteins or RNA (3,5). Then the observed increased basal levels of polyamines would result.…”

Section: Discussionmentioning

confidence: 99%

“…Urine from the boys with DMD and K were measured during a 5-d control period followed by a the normal boys was collected while they were on an ad lib. 5 University's Clinical Trials Commllittee and with the informed consent of subject or parents, as appropriate.…”

Section: Introductionmentioning

confidence: 99%

Abnormal Polyamine Metabolism in Hereditary Muscular Dystrophies

Rudman¹,

Kutner²,

Chawla³

et al. 1980

J. Clin. Invest.

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A B S T R A C T Previous studies showed hyperresponsiveness to human growth hormone (hGH) in men with myotonic or limb girdle dystrophies (MMD or LGD). Because polyamines may mediate some actions of hGH, we have nlow investigated polyamine metabolisimi in these and other dystrophies.Under metabolic balance study conditions, serum and urine levels of putrescine (Pu), spermidine (Sd), spermine (Smn), and cadaverine (Cd) were measured in six normal meni (36-44 yr), four men with MMD (38-44 yr), and three men with LGD (30-36 yr), before and durinig treatment with 0.532 U/kg body wt 314/d of hGH. Daily balances of N, P, and K were also monitored. In the normal subjects, hGH did not influence elemental balances or serum and urine polyamines. In MMD, hGH caused significant retention of N, P, and K (P < 0.005). Basal levels of Smn anid Cd were significantly elevated above niormal (P < 0.005), and Pu, Smn, and Cd increased two-to fourfold above basal during hGH treatment (P < 0.005). In LGD, hGH also caused retention of N, P, and K. Basal levels of nearly all the polyamiines (not serumi Pu) were significantly above normal in serum and urine (P < 0.05). During hGH treatmenit, all fotur polyamines rose significantly above basal (P < 0.005).Serum and urine polyaminie levels in five boys with Duchenne muscular dystrophy, age 8-13, did not differ from those in five age-matched normal boys.Skeletal muscle polyamines were measured in five men (31-40 yr) without muscle disease and in three meni with LGD (30-38 yr). Average concentrationis of Pu, Sd, Sm, and Cd were 46, 306, 548, and 61 nmol/g wet wt in LGD and 1, 121, 245, and 14 in the normnal subjects, respectively (P < 0.05 in each instance).Received for publication 9 Jutly 1979 and in revised form 14 September 1979. Polyamnines were determined in skeletal muscle, liver, kidnlley, and brain of male mice with hereditary muscular dystrophy and in age-and sex-mnatched normal controls. Pu, Sd, Sm, and Cd levels were two to three timiies higher than nonrnal in muscle, but did not differ in liver, kidney, and brain. Similar findings were made in miiale hamsters with hereditary dystrophy anid in their conitrols. The abnormality in hamster mnuscle polyamiinies appeared between 1 and 6 wk of age and( persisted or intensified until 30 wk.These data reveal abniormalities of polyamnine metabolism in men with MMD, in mnen with LGD, and in mice or hamsters with hereditary muscular dystrophy. The polyamine disorder could be related to dystrophic patients' hyperresponsiveness to hGH.

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“…[4] Additionally, some proteins that specifically recognize PUT, SPD, or SPM are known to be involved in biological functions. [5,6] The different roles of the polyamines should be derived from their structural differences. Therefore, conformation studies of SPM may provide a clue to answer this question.…”

Section: Introductionmentioning

confidence: 99%

Conformations of Spermine in Adenosine Triphosphate Complex: The Structural Basis for Weak Bimolecular Interactions of Major Cellular Electrolytes

Maruyoshi

Yamaguchi

Demura

et al. 2011

Chemistry A European J

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Selectively (2)H- and (13)C-labeled spermines (SPM) were efficiently synthesized and analyzed by NMR spectroscopy to determine the spin-spin coupling constants for six conformationally relevant bonds. SPM that is composed of three alkyl moieties, a butanylene, and two propanylene chains undergoes a conformational change when interacting with multivalent anions (e.g., adenosine triphosphate (ATP), ATP-Mg(2+) , and tripolyphosphate). Upon interaction with ATP, the C-C bonds, which affect the distance between the neighboring pairs of ammonium groups (i.e., N1/N5 and N5/N5'), increase the population of gauche rotamers by 17-20% relative to those in the 4 HCl salt of SPM. However, the trend in increments of the gauche conformers for the SPM-ATP complex profoundly differs from that of the spermidine (SPD)-ATP complex. This implies that SPM may preferentially recognize the adenyl group of ATP rather than the tripolyphosphate moiety. This may account for the higher affinity of SPM to ATP-Mg(2+) than with that of SPD, which chiefly interacts with β- and γ-phosphates and is easily replaced by Mg(2+) . These results may provide a clue for the further understanding of the structural basis of polyamine biological functions.

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Selective polyamine-binding proteins spermine binding by an androgen-sensitive phosphoprotein

Cited by 37 publications

References 23 publications

Evidence for serum binding of oxidized spermine and its potent G1-phase inhibition of cell proliferation

Evidence for serum binding of oxidized spermine and its potent G1-phase inhibition of cell proliferation

Abnormal Polyamine Metabolism in Hereditary Muscular Dystrophies

Conformations of Spermine in Adenosine Triphosphate Complex: The Structural Basis for Weak Bimolecular Interactions of Major Cellular Electrolytes

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