Total micrografting hair transplantation using a new hair implanter.
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Hair↗
Biomedical subjects
I H Kim
Publications and source records attributed to I H Kim.
Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma.
A 65-kDa molecular mass of thiol-specific antioxidant protein was purified from human plasma and identified as human serum albumin (HSA) by the analysis of amino-terminal amino acid sequence. This protein exhibited the preventive effects against the inactivation of glutamine synthetase activity and the peroxidation of lipid by a metal-catalyzed oxidation system. These antioxidant activities were supported by a thiol-reducing equivalent such as DTT and reduced glutathione. The thiol-specific antioxidant activity of HSA was greatly activated by halide ion, especially by chloride ion. HSA showed a significant capability to destroy H2O2 in the presence of reduced glutathione, resulting in the production of oxidized glutathione. Both the preventive activity against the glutamine synthetase inactivation and the peroxidase activity were completely abolished by the reactions of HSA with N-ethylmaleimide and iodoacetate, chemical modification agents for sulfhydryl of protein, only in the presence of thiol-reducing equivalent such as DTT. These results suggest that serum albumin acts as a major and predominate antioxidant exerting a glutathione-linked thiol peroxidase activity which removes reactive oxygen species such as H2O2 within blood plasma.
Amino Acid Sequence↗
Identification of promoter in the 5'-flanking region of the E. coli thioredoxin-linked thiol peroxidase gene: evidence for the existence of oxygen-related transcriptional regulatory protein.
E. coli thiol peroxidase (Tpx) linked to the thioredoxin as an in vivo thiol regenerating system acts as an antioxidant enzyme removing peroxides and H2O2. In order to elucidate the mechanism regulating tpx gene expression in E. coli in response to oxygen stress, we made 5' progressive deletions of upstream region from tpx gene, and fused to lacZ gene. LacZ activity was increased 6-fold by oxygen stress and inverted repeat sequence located between -47 and -33 nt was proven to be essential for the oxygen response of tpx promoter. Primer extension experiment and analysis of upstream sequence revealed transcription start point, -10, and -35 regions, which are in good agreements with the consensus sequences recognized by E sigma 70. Northern hybridization showed that expression of tpx gene is regulated at the transcriptional level. DNA binding assays using inverted repeat sequence including -35 region provides preliminary evidence that expression of tpx requires additional transcriptional factor in response to oxygen stress.
Amino Acid Sequence↗
Radiotherapy of intracranial germinomas.
Between 1980 and 1992, 32 patients with intracranial germinomas were treated with radiation. All patients were confirmed histopathologically prior to treatment. Of the 32 intracranial germinomas reviewed, 14 were located in the suprasellar region, 12 in the basal ganglia and thalamus, four in the pineal, and two in both the pineal and suprasellar regions. Three patients had subarachnoid seeding. Craniospinal irradiation was undertaken for 29 patients. The median dose of 54 Gy was delivered to the tumor bed, 36 Gy to the whole brain and 24 Gy to the spinal axis. Five and 10-year survival rates were 96.9 and 96.9%, respectively. Local control was achieved in all patients except one who died of persistent tumor after 2 months following radiotherapy. No intracranial recurrence or spinal metastasis were found. Tumor site did not relate to the prognosis. One patient developed severe intellectual deterioration, three patients had vertebral growth impairment. The present study confirms the excellent result with radiotherapy alone for patients with germinomas.
Adolescent↗
Decursin: a cytotoxic agent and protein kinase C activator from the root of Angelica gigas.
A cytotoxic compound was purified from the root of Angelica gigas Nakai by silica gel chromatography and preparative HPLC. As a result of the structure analysis by mass, IR, 1H-NMR, and 13C-NMR spectrometry, the effective compound was identified as decursin, a pyranocoumarin characterized originally from Angelica decursiva Fr. et Sav. In vitro cytotoxicity testing showed that decursin displayed toxic activity against various human cancer cell lines, for which the ED50 of decursin was about 5-16 micrograms/ml. On the other hand, decursin displayed relatively low cytotoxicity against normal fibroblasts. Decursin also activated protein kinase C (PKC) in vitro, which indicates that the cytotoxic activity of decursin may be related to the protein kinase C activation.
Animals↗
Mutation and Mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family.
A novel thioredoxin-linked thiol peroxidase (Px) from Escherichia coli has been reported previously (M. K. Cha, H. K. Kim, and I. H. Kim, J. Biol. Chem. 270:28635-28641, 1995). In an attempt to perform physiological and biochemical characterizations of the thiol Px, a thiol Px null (tpx) mutant and a functional-residue mutant of thiol Px were produced. The tpx mutant was viable in aerobic culture but grew more slowly than the wild-type cells. The difference in growth rate became more pronounced when oxidative-stress-inducing reagents, such as peroxides and paraquat, were added to the cultures. The viability of the individual tpx mutant under oxidative stress was much lower than that of wild-type cells. tpx mutants growing aerobically respond to paraquat with a sixfold greater induction of Mn-superoxide dismutase than that of the wild-type cells. The deduced amino acid sequence of the thiol Px was found to be from 42 to 72% identical to the sequences of proteins from Haemophilus influenzae (ToxR regulon), Vibrio cholerae (ToxR regulon), and three kinds of streptococci (coaggregation-mediating adhesins), suggesting that they all belong to a new thiol Px family. Alignment of the amino acid sequences of the thiol Px family members showed that one cysteine, which corresponds to Cys-94 in E. coli thiol Px, is perfectly conserved. The substitution of serine for this cysteine residue resulted in complete loss of Px activity. These results suggest that the members of the thiol Px family, including E. coli thiol Px, have a functional cysteine residue and function in vivo as peroxidases.
Amino Acid Sequence↗
A new observation of Hb Yamagata with a different nucleotide substitution: beta 132 AAA-->AAT.
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Adult↗
Effects of tretinoin pretreatment on TCA chemical peel in guinea pig skin.
This study was done to characterize the structural changes in the tretinoin pretreatment on trichloroacetic acid(TCA) chemical peel. In guinea pigs, the right halves pretreated with tretinoin and the left halves treated nothing were compared in their structural changes after TCA chemical peel. Epidermal thickness in the tretinoin pretreated group was almost the same in the first and second week. But epidermis of the TCA group increased continuously. In the first week, mitotic figures in the epidermis were more increased in the TCA group, but those in hair follicles were more increased in the tretinoin pretreated group. In the second week, mitotic figures in the epidermis were almost same in both group, but in hair follicles of the tretinoin pretreated group, mitotic figures were much more increased. In alcian blue staining, glycosaminoglycan was stained much more strongly in dermis of the TCA group in first week, but was more strongly stained in the tretinoin pretreated group in second week. On electron microscopic findings, the fibroblasts in upper dermis were larger and had plentier cytoplasm with more organelles in the tretinoin pretreated group. Conclusively, tretinoin pretreatment on TCA chemical peel sustained the effects of TCA longer and showed synergistic effects of TCA and induced enhanced wound healing.
Animals↗
Serum cholesterol level as an indicator of allograft liver function.
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Autoanalysis↗
Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell.
A thiol-dependent antioxidant protein (HRPRP) was previously reported as a predominant antioxidant protein in human red blood cell (RBC). The analysis of amino acid sequence of HRPRP with those of human PRP-like gene products indicates that HRPRP is identical to brain PRP (HPRP). This protein act as a peroxidase linked to thioredoxin (Trx)/thioredoxin reductase (TR). Until now, there was no evidence for Trx/TR system in RBC. The existence of the Trx/TR system in RBC was immunologically determined. A 58-kDa protein showing TR activity was partially purified from human RBC and characterized. Our results reveal that HRPRP act as a new type of peroxidase supported by Trx/TR system in human RBC.
Amino Acid Sequence↗
Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli.
Three different molecular masses (24, 22, and 20 kDa) of antioxidant proteins were purified in Escherichia coli. These proteins exhibited the preventive effects against the inactivation of glutamine synthetase activity and the cleavage of DNA by a metal-catalyzed oxidation system capable of generating reactive oxygen species. Their antioxidant activities were supported by a thiol-reducing equivalent such as dithiothreitol. Analysis of the amino-terminal amino acid sequences and the immunoblots between 24- and 22-kDa proteins indicates that the 24-kDa protein is an intact form of the 22-kDa protein that was previously identified 22-kDa subunit (AhpC) of E. coli alkyl hydroperoxide reductase (AhpC/AhpF). We isolated and sequenced an E. coli genomic DNA fragment that encodes 20-kDa protein. Comparison of the deduced amino acid sequence of the 20-kDa protein with that of AhpC revealed no sequence homology. A search of a data bank showed that the 20-kDa protein is a new type of antioxidant enzyme. The synthesis of this novel 20-kDa protein was increased in response to oxygen stress during growth. The 20-kDa protein resides mainly in the periplasmic space of E. coli, whereas the 24-kDa AhpC resides mainly in the matrix. The 20-kDa protein was functionally linked to the thioredoxin as an in vivo thiol-regenerating system and exerted a peroxidase activity. This 20-kDa protein is thus named "thiol peroxidase," which could act as an antioxidant enzyme removing peroxides or H2O2 within the catalase- and peroxidase-deficient periplasmic space of E. coli.
Amino Acid Sequence↗
Reoxygenation and rehypoxiation in the SCCVII mouse tumor.
PURPOSE: To test the hypothesis that, following preferential killing of tumor hypoxic cells, the fraction of hypoxic cells in the tumor will reestablish itself to pretreatment levels (rehypoxiation) with the same kinetics as for reoxygenation. METHODS AND MATERIALS: Mouse squamous cell carcinoma VII (SCCVII) tumors were treated with a single dose of 10 Gy or a single dose of the bioreductive hypoxic cell cytotoxin, tirapazamine (SR 4233, 0.2 mmol/kg), which preferentially kills hypoxic cells within the tumor. Hypoxic fractions were determined by the paired survival curve technique using the in vivo-in vitro clonogenic assay 0-24 h after treatment. RESULTS: Immediately after irradiation with 10 Gy, the hypoxic fraction of the tumors increased to 80% and rapidly returned to pretreatment levels 3-6 h later. Within 1 h of injecting tirapazamine, the hypoxic fraction fell to 0.57% (about 7% of pretreatment levels) and returned to pretreatment levels 3-5 h later. CONCLUSION: The return to pretreatment levels of hypoxia among tumor cells surviving a single dose of radiation (reoxygenation) and of the hypoxic cell toxin tirapazamine (rehypoxiation) was rapid and occurred with similar kinetics for the two processes. These data support the hypothesis that reoxygenation and rehypoxiation are different manifestations of the same phenomenon and result from fluctuating tumor blood flow which creates acute hypoxia.
Animals↗
Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin.
A protector protein from Saccharomyces cerevisiae specifically prevents the inactivation of enzymes caused by a thiol/Fe3+/O2 metal-catalyzed oxidation system but not by an ascorbate/Fe3+/O2 system. Ascorbate/Fe3+/O2-mediated damage of enzymes could be prevented by the protector protein only in the presence of reduced thiol. We demonstrate that two proteins from yeast, thioredoxin plus another protein having properties similar to that expected to thioredoxin reductase, when presented with NADPH and the yeast protector protein prevented inactivation of E. coli glutamine synthetase by the ascorbate/Fe3+/O2 system. This system also removes hydrogen peroxide effectively. We also demonstrate evidence suggesting that the NADPH-dependent thioredoxin system reactivates protector protein by reversible disulfide-dithiols exchange.
Amino Acid Sequence↗
The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions.
The complete cDNA encoding human thiol-specific antioxidant protein (PRP) was isolated from a human brain cDNA library in the lambda Zap expression vector. An open reading frame (ORF) was identified and found to encode a polypeptide of 197 aa with a M(r) of 21,729. The cDNA contained 98 bp of 5'-untranslated sequence (UTR) and 259 bp of 3'-UTR containing a poly(A) signal, AATAAA. Expression of the human PRP cDNA in Escherichia coli yielded a functionally active protein. The observed local sequence homologies between human PRP and other homologous proteins whose functions have not yet been defined give important insight into elucidating the biochemical function of a new protein family which has highly conserved regions containing cysteine.
Amino Acid Sequence↗
Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein.
A thiol-specific antioxidant protein (Protector Protein, PRP) was purified from human red blood cells (RBC). The PRP exists as a predominant protein in human RBC, which showed distinct thiol-specific antioxidant activities in the presence of dithiothreitol (DTT) as a reducing equivalent. The human RBC PRP (HRPRP) completely inhibited visible absorption spectral changes of oxyhemoglobin, DNA cleavage, and the peroxidation of RBC membrane by a nonenzymatic Fe3+/O2/thiol mixed-function oxidation system capable of generating hydroxyl radical. These observations suggest that HRPRP could act as a new type of antioxidant protein to maintain the RBC integrity by scavenging reactive oxygen species.
Antioxidants↗
Temperature-dependent modification of divalent cation flux in the rat parotid gland basolateral membrane.
Divalent cation (Mn2+, Ca2+) entry into rat parotid acinar cells is stimulated by the release of Ca2+ from the internal agonist-sensitive Ca2+ pool via a mechanism which is not yet defined. This study examines the effect of temperature on Mn2+ influx into internal Ca2+ pool-depleted acini (depl-acini, as a result of carbachol stimulation of acini in a Ca(2+)-free medium for 10 min) and passive 45Ca2+ influx in basolateral membrane vesicles (BLMV). Mn2+ entry into depl-acini was decreased when the incubation temperature was lowered from 37 to 4 degrees C. At 4 degrees C, Mn2+ entry appeared to be inactivated since it was not increased by raising extracellular [Mn2+] from 50 microM up to 1 mM. The Arrhenius plot of depletion-activated Mn2+ entry between 37 and 8 degrees C was nonlinear, with a change in the slope at about 21 degrees C. The activation energy (Ea) increased from 10 kcal/mol (Q10 = 1.7) at 21-37 degrees C to 25 kcal/mol (Q10 = 3.0) at 21-8 degrees C. Under the same conditions, Mn2+ entry into basal (unstimulated) cells and ionomycin (5 microM) permeabilized depl-acini exhibit a linear decrease, with Ea of 7.8 kcal/mol (Q10 = 1.5) and 6.2 kcal/mol (Q10 < 1.5), respectively. These data suggest that depletion-activated Mn2+ entry into parotid acini is regulated by a mechanism which is strongly temperature dependent and distinct from Mn2+ entry into unstimulated acini.(ABSTRACT TRUNCATED AT 250 WORDS)
Animals↗
Treatment outcome and prognostic factors of medulloblastoma.
Medulloblastoma, once a tumor with a dismal prognosis, is one of the most common primary brain tumors of childhood. As the methods of treatment have been continuously refined, the outcome has improved remarkably during the last few decades. The outcome of 78 medulloblastoma patients, which were managed from 1972 to 1992 at the Department of Neurosurgery of Seoul National University Hospital, were analyzed to calculate the 3-year and 5-year survival rates (3yS and 5yS). Of those, 52 cases which were treated after July 1982 were studied 1) to calculate the 3yS and 5yS, 2) to figure out the prognostic factors of survival, and 3) to investigate the role of adjuvant chemotherapy ('8-drugs-in-a-day' protocol: CCNU, cisplatin, vincristine, hydroxyurea, procarbazine, cytosine arabinoside, methylprednisolone and cyclophosphamide). The 3yS and 5yS of the 78 patients were 57.4% and 47.3%, respectively. Of the 52 patients treated after July 1982, the 3yS and 5yS were 67.8% and 64.1%, respectively. The latest recurrence was at 56 months after surgery. All the recurrences were within the risk period of Collins' rule. Of the prognostic factors studied by univariate analysis (age, sex, Chang's classification T- and M-stages, extent of surgical removal, and chemotherapy), Chang's classification M-stage and sex were the statistically significant factors (p = 0.028 and 0.024 respectively). On multivariate analysis, only the M-stage was statistically significant (p = 0.004). Adjuvant chemotherapy had different influences in different patient groups. Only in the 'poor risk' group, did adjuvant chemotherapy have a strong tendency to better outcome (p = 0.069). Further data collection and analysis will lead to better treatment modalities and better outcome for this most common primary malignant brain tumor in childhood.
Adolescent↗
Surgery for seizure-related structural lesions of the brain with intraoperative acute recording(ECoG) and functional mapping.
Epilepsy surgery has been demonstrated to be an effective alternative treatment for intractable partial or localization related epilepsy. Primary intracranial neoplasms and other structural lesions of the brain are important etiological factors in patients with partial seizure disorders. A neuroimaging identified lesion in patients with seizures, not necessarily medically refractory, may also be an indication for surgery in selected patients. Twelve patients operated on under local or general anesthesia for resection surgery underwent intraoperative recording(electrocorticogram) and/or functional mapping by electrical stimulation or somatosensory evoked potentials-(SSEPs) for identification of the secondary epileptogenic area and/or functional area; 2 meningiomas, 5 astrocytomas, 1 gangliocytoma, 1 abscess, 1 small AVM, 1 cysticercosis and one gliosis by previous intracerebral hemorrhage with middle cerebral artery(MCA) aneurysm. Among these, additional corticectomy or anterior temporal lobectomy was performed in eleven patients. All the patients did well after surgery with good outcomes as seizure free in nine(75%) out of 12 patients with 11.9 months of follow-up period, without any neurological deficits. Intraoperative recording and functional mapping of adjacent areas of the structural lesions of the brain are useful in surgery and can guide the extent of further resection.
Adolescent↗