• 제목/요약/키워드: Rh

검색결과 2,737건 처리시간 0.028초

Relationships between Skin Cancers and Blood Groups - Link between Non-melanomas and ABO/Rh Factors

  • Cihan, Yasemin Benderli;Baykan, Halit;Kavuncuoglu, Erhan;Mutlu, Hasan;Kucukoglu, Mehmet Burhan;Ozyurt, Kemal;Oguz, Arzu
    • Asian Pacific Journal of Cancer Prevention
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    • 제14권7호
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    • pp.4199-4203
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    • 2013
  • Background: This investigation focused on possible relationships between skin cancers and ABO/Rh blood groups. Materials and Methods: Between January 2005 and December 2012, medical data of 255 patients with skin cancers who were admitted to Kayseri Training and Research Hospital, Radiation Oncology and Plastic Surgery Outpatient Clinics were retrospectively analyzed. Blood groups of these patients were recorded. The control group consisted of 25701 healthy volunteers who were admitted to Kayseri Training and Research Hospital, Blood Donation Center between January 2010 and December 2011. The distribution of the blood groups of the patients with skin cancers was compared to the distribution of ABO/Rh blood groups of healthy controls. The association of the histopathological subtypes of skin cancer with the blood groups was also investigated. Results: Of the patients, 50.2% had A type, 26.3% had O type, 16.1% had B type, and 7.5% had AB blood group with a positive Rh (+) in 77.3%. Of the controls, 44.3% had A type, 31.5% had 0 type, 16.1% had B type, and 8.1% had AB blood group with a positive Rh (+) in 87.8%. There was a statistically significant difference in the distribution of blood groups and Rh factors (A Rh (-) and 0 Rh positive) between the patients and controls. A total of 36.8% and 20.4% of the patients with basal cell carcinoma (BCC) had A Rh (+) and B Rh (+), respectively, while 39.2% and 27.6% of the controls had A Rh (+) and B Rh (+), respectively. A significant relationship was observed between the patients with BCC and controls in terms of A Rh (-) (p=0.001). Conclusion: Our study results demonstrated that there is a significant relationship between non-melanoma skin cancer and ABO/Rh factors.

Dioxygen Binding to Dirhodium(Ⅱ, Ⅱ), (Ⅱ, Ⅲ), and (Ⅲ, Ⅲ) Complexes. Spectroscopic Characterization of $[Rh_{2}(ap)_{4}(O_{2})]^{+},\;Rh_{2}(ap)_{4}(O_{2}),\;and\;[Rh_{2}(ap)_{4}(O_{2})]^-$, where ap=2-anilinopyridinate Ion

  • Lee, Jae-Duck;Yao, Chao-Liang;Capdevielle, Francoise J.;Han, Bao-Cheng;Bear, John L.;Kadish, Karl M.
    • Bulletin of the Korean Chemical Society
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    • 제14권2호
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    • pp.195-200
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    • 1993
  • The neutral, reduced, and oxidized 2,2-trans isomers of $Rh_2(ap)_4$ (ap=2-anilinopyridinate) were investigated with respect to dioxygen binding in $CH_2Cl_2$ containing 0.1 M tetrabutyl-ammonium perchlorate. $Rh_2(ap)_4$ binds dioxygen in nonaqueous media and forms a $Rh^{II}Rh^{III}$ superoxide complex, $Rh_2(ap)_4(O_2)$. This neutral species was isolated and is characterized by UV-visible and IR spectroscopy, mass spectrometry and cyclic voltammetry. It can be reduced by one electron at $E_{1/2}$ = -0.45 V vs. SCE in $CH_2Cl_2$ and gives ${[Rh_2(ap)_4(O_2)]}^-$ as demonstrated by the ESR spectrum of a frozen solution taken after controlled potential reduction. The superoxide ion in ${[Rh_2(ap)_4(O_2)]}^-$ is axially bound to one of the two rhodium ions, both of which are in a +2 oxidation state. $Rh_2(ap)_4(O_2)$ can also be stepwise oxidized in two one-electron transfer steps at $E_{1/2}$ = 0.21 V and 0.85 V vs. SCE in $CH_2Cl_2$ and gives ${[Rh_2(ap)_4(O_2)]}^+$ followed by ${[Rh_2(ap)_4(O_2)]}^{2+}$. ESR spectra demonstrate that the singly oxidized complex is best described as ${[Rh^{II}Rh^{III}(ap)_4(O_2)]}^+$ where the odd electron is delocalized on both of the two rhodium ions and the axial ligand is molecular oxygen.

Actions of a Gonadotropin-Releasing Hormone Antagonist on Gonadotropin II and Androgenic Steroid Hormone Secretion in Precocious Male Rainbow Trout

  • Kim Dae-Jung;Han Chang-Hee;Aida Katsumi
    • Fisheries and Aquatic Sciences
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    • 제3권1호
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    • pp.37-43
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    • 2000
  • We used a mammalian GnRH antagonist, $[Ac-3,4-dehydro-Pro^1,\;D-p-F-Phe^2,\;D-Trp^{3.6}]$-GnRH, to examine the details of the salmon type gonadotropin-releasing hormone (sGnRH) and GnRH agonist analog $(Des-Gly^{10}$[d-Ala^6]-ethylamide GnRH; GnRHa) functions in the control of maturational gonadotropin (GTH II) secretion, in precocious male rainbow trout, in both in vivo and in vitro experiments. In the in vivo study, plasma GTH II levels increased by sGnRH or GnRHa treatment, but the response was more rapid and stronger in the GnRHa treatment group. The increase in GTH II was significantly suppressed by the GnRH antagonist, while the antagonist had no effect on basal GTH II levels in both groups. The GnRH antagonist showed stronger suppression of GTH II levels in the sGnRH treatment fish than in the GnRHa treatment fish. In addition, plasma androgenic steroid hormones (testosterone and 11-ketotestosterone) increased by the sGnRH or GnRHa treatment. The GnRH antagonist significantly inhibited the increases in plasma androgenic steroid hormone levels stimulated by the sGnRH or GnRHa, while the antagonist had no effect on basal androgenic steroid hormone levels in both groups. In the in vitro study, treatment with sGnRH or GnRHa increased GTH II release from the cultured dispersed pituitary cells, but the response was stronger in the GnRHa treatment group. The increase in GTH II release by GnRH was suppressed by adding the GnRH antagonist, dose­dependently. On the other hand, basal release of GTH II did not decrease by the GnRH antagonist treatment in both groups. These results suggest that the GnRH antagonist, $[Ac-3,4-dehydro-Pro^1,\;D-p-F-Phe^2,\;D-Trp^{3.6}]-GnRH$, used in this study is effective in blocking the action of GnRH-induced GTH II release from the pituitary gland both in vivo and in vitro.

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귀금속촉매하에서 암모니아의 전환반응 (Ammonia Conversion in the Presence of Precious Metal Catalysts)

  • 장현태;박윤국;고용식
    • Korean Chemical Engineering Research
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    • 제46권4호
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    • pp.806-812
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    • 2008
  • 귀금속촉매 존재하에서 암모니아 전환반응은 배가스내의 암모니아를 처리하는데 중요한 기술이다. 과잉용액 함침법을 이용하여 $Pt-Rh/Al_2O_3$, $Pt-Rh/TiO_2$, $Pt-Rh/ZrO_2$, $Pt-Pd/Al_2O_3$, $Pd-Rh/Al_2O_3$, $Pd-Rh/TiO_2$, $Pd-Rh/ZrO_2$, $Pt-Pd-Rh/Al_2O_3$, $Pd/Ga-Al_2O_3$, $Rh/Ga-Al_2O_3$, 그리고 $Ru/Ga-Al_2O_3$의 촉매를 제조하였다. 제조된 촉매는 1/4"의 반응기에 $10,000{\sim}50,000hr^{-1}$의 공간속도 조건하에서 촉매활성능 실험을 수행하였다. 암모니아의 초기농도는 2,000 ppm (나머지는 공기)으로 유지하였다. $T_{50}$는 암모니아 전환율이 50%일 때를 나타내는 온도를, $T_{90}$은 90%의 전환율일 때의 온도를 나타낸다. 알루미나를 담지체로 사용했을때의 $T_{50}$$T_{90}$은 다른 담체를 사용했을때의 $T_{50}$$T_{90}$보다 훨씬 낮았다. Pd-Rh촉매의 경우 $Al_2O_3$를 담체로 사용하였을 때 $ZrO_2$$TiO_2$보다 저온 활성이 우수하게 나타났다. 황산화물의 피독실험 결과 본 연구에서는 최종적으로 $Pt-Rh/Al_2O_3$ 촉매가 다른 촉매에 비하여 우수함을 보였다. 실험결과 Pt-Rh가 암모니아 전환공정에서 유용한 촉매라는 사실을 알 수 있다.

The New Strategy of Formulation of Human Growth Hormone Aggregate within PLGA Microspheres for Sustained Release

  • 김홍기;박태관
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2000년도 춘계학술발표대회
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    • pp.541-545
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    • 2000
  • For the sustained release formulation of recombinant human growth hormone (rhGH), dissociable rhGH aggregates were microencapsulated within poly(D,L-lactic-co-glycolic acid) [PLGA] microparticles. rhGH aggregates with 2 - 3 m Particle diameter were first produced by adding a small volume of aqueous rhGH solution into a partially water miscible organic solvent phase(ethyl acetate) containing PLGA. These rhGH aggregates were then microencapsulated within PLGA polymer phase by extracting ethyl acetate into an aqueous phase pre-saturated with ethyl acetate. The resultant microparticles were 2 - 3 m in diameter similar to the size of rhGH aggregates, suggesting that PLGA polymer was coated around the protein aggregates. Release profiles of rhGH from these microparticles were greatly affected by changing the volume of the incubation medium. The release rhGH species consisted of mostly monomeric form with having a correct conformation. This study reveals that sustained rhGH release could be achieved by microencapsulating reversibly dissociable protein aggregates within biodegradable polymers.

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흰쥐 태아 뇌에서 GnRH 신경세포의 초기발생과정 (Prenatal Development of Gonadotropin Releasing Hormone (GnRH) Neurons in the Rat Brain)

  • 이영기;최완성
    • 한국동물학회지
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    • 제34권4호
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    • pp.491-499
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    • 1991
  • The present experiment was carried out 1) to study the developmental topography of GnRH neuronal system and 2) to characterize the cellular localization of GnRH neurons in the prenatal brain development of the rat. At embryonic day (I) 14.5, immunoreactive cell bodies of GnRH were first seen in the nasal septum and in the ganglion terminate located in the ventral protion of the caudal olfactory bulb. Two days later (E 16.5), GnRH-containing neurons were observed at the level of olfactory tubercle and diagonal band of Broca, which is the first appearance in the intracerebral region. From 118.5, the topographic pattern of immunoreactive GnRH perikarya was similar to that of adult rats. The present data suggest that GnRH neurons were originated from the nasal septum and gradually extended to the hvpothalamic regions with increasing fetal age.

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CHO 세포에서 생산된 재조합 Erythropoietin (EPO)의 약효 (Efficacy of Recombinant Erythropoietin from CHO Cells)

  • 김석준;하병집;이동억;오명석;김달현;박관하;김현수
    • Biomolecules & Therapeutics
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    • 제2권4호
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    • pp.343-346
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    • 1994
  • In vivo activity of recombinant human erythropoietin (rh-EPO) has been examined using polycythemic model in mice and acute hemorrhage model in rats. The number of reticulocytes in blood stream was increased after a single injection of rh-EPO depending on the dosage of rh-EPO in polycythemy model. It seemed that optimal dose of rh-EPO for polycythemic mice was around 1-10 U/kg. Rh-EPO also showed the effectiveness for increase of reticulocyte numbers both in male and female rats after bleeding. The number of reticulocytes and the change of hemoglobin concentration in the blood stream of normal rats has been examined after injection of rh-EPO. The maximum value of reticulocyte was observed on the 6th day of the injection in these normal rats. In addition, the increase of reticulocyte and the concentration of hemoglobin were dependent on the dosage of rh-EPO. The increase of hemoglobin concentration was continued to the 9th day after injection. In this study, the efficacy of rh-EPO was confirmed in both mice and rats.

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천연형 사람 적혈구 조혈인자의 항원성시험 (Antigenicity Study of Recombinant Human Erythropoietin)

  • 강경구;조현;백남기;김원배
    • Biomolecules & Therapeutics
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    • 제6권1호
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    • pp.50-55
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    • 1998
  • Antigenic potential of a recombinant human erythropoietin (rhEPO) produced by Dong-A charm. Co. Ltd. was examined by active systemic anaphylaxis (ASA) test in guinea pigs, mouse-rat passive cutaneous anaphylaxis (PCA) reaction and passive hemagglutination (PHA) test. In ASA test, rhEPO induced the signs of restlessness, rubbing or licking nose, sneezing and coughing in the animals immunized with rhEPO 1000 lU/kg alone or rhEPO 1000 lU/kg incorporated into Freund\\\\`s complete adjuvant. In the mouse-rat PCA test, only one of six sera from the animals immunized with rhEPO 1000 lUng incorporated into Alum showed positive result. In the PHA test, rhEPO revealed negative results in all of the rhEPO-immunized groups. From these results, rhEPO was considered to produce IgE in guinea pigs and mice, but not IgG and/or IsM in mice. The results of this study were similar to those of the other recombinant human erythropoietin and these positive results were thought to be caused due to the fact that rhEPO were heterogeneous proteins to guinea pigs and mice. Considering the fact that rhErO has an identical structure with indigenous human erythropoietin, rhEPO is not thought to cause immunological problems in clinical use.

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In situ hybridization법에 의한 북방산개구리 뇌에서 GnRH mRNA를 함유한 세포의 분포 연구 (Neuroanatomical Localization of Cells Containing Gonadotropin Releasing Hormone mRNA in the Brain of Frog, Rana dvbowskii, by in situ Hybridization)

  • 최완성;김정우
    • 한국동물학회지
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    • 제37권3호
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    • pp.304-310
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    • 1994
  • Using in situ hybridization, we have mapped the anatomical localization of perikarya containing myNA that codes for sonadotropin releasing hormone (GnRH) in the brains of female frogs, R. dybowskii. DNA olisomers, with sequences complementary to the GnRH portion of pro-GnRH myNA sequence, were synthesized and hybridized to paraformaldehvde-fixed, sagittal sections of the whole brain stem. The distribution of the GnRH mRNA containing cell bodies was similar to that described for GnRH peptide by immunohistochemistrv. That is, cells containing GnRH mRNA were observed in the medial septal area, anterior preoptic area, ventromedial hvpothalamus and infundibular regions. However, another cell groups which contains GnRH mRNAs were also detected by in situ hybridization in the bed nucleus of hippocampal commissure, preoptic area, nucleus infundibularis dorsalis, mesencephalic nuclei and intermediolateral cell column of spinal cord areas. These results demonstrate the feasibility of using in situ hybridization as a strategy to study the distribution of GnRH neurons and the detection of GnRH gene expression in the vertebrates.

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Multivesicular Liposomes for Oral Delivery of Recombinant Human Epidermal Growth Factor

  • Li Hong;An Jun Hee;Park Jeong-Sook;Han Kun
    • Archives of Pharmacal Research
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    • 제28권8호
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    • pp.988-994
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    • 2005
  • The purpose of the present study was to prepare multivesicular liposomes with a high drug loading capacity and to investigate its potential applicability in the oral delivery of a peptide, human epidermal growth factor (rhEGF). The multivesicular liposomes containing rhEGF was prepared by a two-step water-in-oil-in-water double emulsification process. The loading efficiency was increased as rhEGF concentration increased from 1 to 5mg/mL, reaching approximately $60\%$ at 5 mg/mL. Approximately $47\%$ and $35\%$ of rhEGF was released from the multivesicular liposomes within 6 h in simulated intra-gastric fluid (pH 1.2) and intra-intestinal fluid (pH 7.4), respectively. rhEGF-loaded multivesicular liposomes markedly suppressed the enzymatic degradation of the peptide in an incubation with the Caco-2 cell homogenate. However, the transport of rhEGF from the multivesicular liposomes to the basolateral side of Caco­2 cells was two times lower than that of the rhEGF in aqueous solution. The gastric ulcer healing effect of rhEGF-loaded multivesicular liposomes was significantly enhanced compared with that of rhEGF in aqueous solution; the healing effect of the liposomes was comparable to that of the cimetidine in rats. Collectively, these results indicate that rhEGF-loaded multivesicular liposomes may be used as a new strategy for the development of an oral delivery system in the treatment of peptic ulcer diseases.