Distribution of hypusione, N6(-4amino-2-hydroxybutyl)-2, 6-diaminohexanoic acid, in mammalian organs

Nakajima, Teruo; Matsubayashi, T; Kakimoto, Yasuo; Sano, Isamu

doi:10.1016/0304-4165(71)90095-x

Cited by 30 publications

(26 citation statements)

References 9 publications

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“…When hypusine and lysine excretion are compared for the 10 juvenile controls, although the numbers studied are small, no obvious race or sex differences are seen and values are similar to those reported for Japanese children [1]. Hypusine excretion is 7-10 times higher in the patients with familial hyperlysinemia than in normal infants and children.…”

Section: Resultssupporting

confidence: 55%

“…With 10 ml hyperlysinemic serum, we were not able to demonstrate hypusine. Because the method permits detection of 2 nmol/sample, this finding indicates that serum hypusine levels for patients with hyperlysinemia were less than 20 nmol/100 ml, the value reported for normal human serum by Nakajima et al [1].…”

Section: Resultsmentioning

confidence: 49%

“…Hypusine content has thus far been reported only for certain mammalian tissues [1,2], where the largest amounts have been found in brain, liver, and kidney. The remarkable variance of levels of hypusine in urine between subjects with hyperlysinemia and normal subjects seems hardly likely to be the result of dietary differences.…”

Section: Discussionmentioning

confidence: 99%

“…Using an aliquot of the 24-hr sample containing 20 mg creatinine, the basic aliphatic amino acids were separated from the urine by the method outlined by Nakajima et al [1]. Serum from the subjects with hyperlysinemia was deproteinated with 10 volumes of 6% trichloroacetic acid [1] and similarly treated. Chromatography was carried out on the 22-cm column of an automatic amino acid analyzer [5] using a standard resin [6] with 0.38 M sodium citrate buffer, pH 4.25, which contained 0.57 M NaCl.…”

Section: Methodsmentioning

confidence: 99%

“…They deduced its chemical structure, and showed it to be composed of two moieties: hydroxyputrescine and lysine. A few months later, the same group [1] reported that hypusine was also to be found in rat and rabbit brain and in rat liver, kidney, muscle, and blood. They also demonstrated hypusine in human urine and blood.…”

Section: Introductionmentioning

confidence: 92%

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Excretion of Hypusine by Children and by Patients with Familial Hyperlysinemia

Woody

Pupene

1973

Pediatr Res

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ExtractThree children with familial hyperlysinemia were found to excrete, respectively, 1,934 nmol/24 hr, 730 nmol/24 hr, and 1,121 nmol/24 hr hypusine and 16.1 mmol/24 hr, 7.0 mmol/24 hr, and 16.6 mmol/24 hr lysine. Ten juvenile control subjects excreted 35-253 nmol/24 hr (mean 156 nmol/24 hr) hypusine and 0.2-1.5 mmol/24 hr (mean 0.7 mmol/24 hr) lysine. Three infant control subjects were found to excrete 156 nmol/24 hr, 60 nmol/24 hr, and 77 nmol/24 hr hypusine. Serum levels of hypusine for subjects with hyperlysinemia were normal (less than 20 nmol/100 ml). SpeculationPatients with familial hyperlysinemia excrete both hypusine and lysine at levels 7-10 times higher than those observed for control subjects, while serum levels of hypusine in patients with hyperlysinemia are not elevated. These findings suggest that hypusine may be an endometabolite of lysine and not further metabolized or utilized.

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Section: Resultssupporting

confidence: 55%

Section: Resultsmentioning

confidence: 49%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 92%

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Excretion of Hypusine by Children and by Patients with Familial Hyperlysinemia

Woody

Pupene

1973

Pediatr Res

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Heat stress‐induced loss of eukaryotic initiation factor 5A (eIF‐5A) in a human pancreatic cancer cell line, MIA PaCa‐2, analyzed by two‐dimensional gel electrophoresis

Takeuchi

Nakamura

Fujimoto³

et al. 2002

Electrophoresis

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Alterations of intracellular proteins during the process of heat stress-induced cell death of a human pancreatic cancer cell line, MIA PaCa-2, were investigated using two-dimensional gel electrophoresis (2-DE), agarose gel electrophoresis, and cell biology techniques. Incubation of MIA PaCa-2 at 45 degrees C for 30 min decreased the cell growth rate and cell viability without causing chromosomal DNA fragmentation. Incubation at 51 degrees C for 30 min suppressed cell growth and again led to death without DNA fragmentation. The cell death was associated with the loss of an intracellular protein of M(r) 17,500 and pI 5.2 on 2-DE gel. This protein was determined to be eukaryotic initiation factor SA (eIF-5A) by microsequencing of the N-terminal region of peptide fragments obtained by cyanogen bromide treatment of the protein blotted onto a polyvinylidene difluoride (PVDF) membrane. The sequences detected were QXSALRKNGFVVLKGRP and STSKTGXHGHAKVHLVGID, which were homologous with the sequence of eIF-5A from Gln 20 to Pro 36 and from Ser 43 to Asp 61, respectively. Furthermore, the result of sequencing suggested that the protein was an active form of hypusinated eIF-5A, because Lys 46 could be detected but not Lys 49, which is the site for hypusination. These results suggest that loss of the active form of eIF-5A is an important factor in the irreversible process of heat stress-induced death of MIA PaCa-2 cells.

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Two Hypusine‐Containing Proteins Identified by Metabolic Labeling in Chick Embryo Fibroblasts

Dou

Chen

1989

J Chinese Chemical Soc

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Incubation of various cultured mammalian cells under growth‐stimulatory condition with [3H]putrescine or [3H]spermidine results in a labeling of an 18, 000‐dalton protein (Cell, 1982, 29, 791; BBA, 1983, 756, 395). The labeling is due to post‐translational conversion of a lysine residue to hypusine residue, using the butylamino moiety derived from spermidine. In order to search for an abundant source for the purification of this protein, we have examined possible existence of this hypusine‐containing 18, 000‐dalton protein (hyp‐18k) in chick embryos by the metabolic labeling method. Metabolic labeling of chick embryo fibroblasts, prepared from the Day 11 embryos, by [3H]putrescine resulted in two prominently labeled protein bands. Mr=18, 000 and 20, 000, as shown by sodiun dodecyl sulfate‐polyacrylamide gel electrophoresis and fluorography. Two‐dimensional gel analysis indicated that the labeled 20, 000‐dalton protein had a pI value of 5.5 and the labeled 18, 000‐dalton protein exhibited isoform structures with pI values ranging from 4.6 to 5.1. Peptide map analysis showed that these two proteins are similar but not identical. Both labeled proteins contained radioactive hypusine residue and exhibited strong binding to Cibacron Blue dye. The time course of the metabolic labeling of these two proteins, however, differed dramatically. The labeling of the 18, 000‐dalton protein appeared early and continued to increase 24 h after serum stimulation. In contrast, the labeling of the 20, 000‐dalton protein became prominent only after much longer period of incubation.

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Distribution of hypusione, N6(-4amino-2-hydroxybutyl)-2, 6-diaminohexanoic acid, in mammalian organs

Cited by 30 publications

References 9 publications

Excretion of Hypusine by Children and by Patients with Familial Hyperlysinemia

Excretion of Hypusine by Children and by Patients with Familial Hyperlysinemia

Heat stress‐induced loss of eukaryotic initiation factor 5A (eIF‐5A) in a human pancreatic cancer cell line, MIA PaCa‐2, analyzed by two‐dimensional gel electrophoresis

Two Hypusine‐Containing Proteins Identified by Metabolic Labeling in Chick Embryo Fibroblasts

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