• Title/Summary/Keyword: 면역 조직 화학

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Component proteins in crud extract of adult Paragonimus westermani purified by immunoaffinity chromatography using monoclonal antibodes (친화성크로마토그래피로 순수분리한 폐흡충 성충 성분단백질의 성상)

  • Kang, Shin-Yong;Kong, Yoon;Cho, Seung-Yull
    • Parasites, Hosts and Diseases
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    • v.29 no.4
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    • pp.363-370
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    • 1991
  • 인체감염이 다발하는 폐흡충증의 혈청학적 진단에서 항원으로 사용하는 성충추출액은 여러단계의 질환 이행과정을 진단하는 항원으로서 문제가 있다. 이를 해결하려면 먼저 추출액내의 성분단백질의 성상을 파악할 필요가 있다. 이 연구에서는 폐흡충 성충 추출액으로 면역시킨 BALB/c mice의 비장세포와 SP2/0 형질세포종 세포를 세포융합하여 제작한 단세포군항체를 이용하여 친화성크로마토그래피로 폐흡충 성충의 구성단백질의 일부를 순수분리하고 성상을 관찰하였다. 그 결과는 다음과 같다. 1. 세포융합으로 PFCK-21, PFCK-44, PFCK-136, PFCK-189 등 4종류의 단세포군 항체를 얻었다. 그중 PFCK-21과 PFCK44는 17k Da, PFCK-136은 23, 46, 92 kDa 단백질에 반응하였고 PFCK-189는 여러종류의 단백질에 반응하였다. 2. PFCK-44 단세포군항체를 고리로 친화성 크로마토그래피를 실시하여 분리한 성분 단백질은 disc-PAGE상 4번째에 위치하고 분자량이 17 kDa로 알려진 단밸질이었다. 이 단밸질은 17 kDa의 monomer로 판단하였다. 면역조직화학염색을 실시한 결과 이 단밸질은 장관 상피세포에 반응하고 있었다. 3. PFCK-136 단세포군항체로 순수분리한 단밸질은 disc-PAGE상 1번 단밸질(440 kDa)이었으며 환원성 SDS-PAGE에서는 23 kDa 단밸질이었다. 면역조직화학염색으로 이 단세포군항체는 충란내 세포에 강하게 반응하고 있었다.

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Clinical and Immunohistochemical Characteristics of Malignant Aortic Body Tumor in a Pekingese Dog (페키니즈에서 발생한 악성 대동맥체 종양의 임상양상과 면역조직화학적 특성)

  • Kim, Won-Jung;Kim, Seung-Gon;Lee, Chang-Min;Kim, Dae-Young;Park, Hee-Myung
    • Journal of Veterinary Clinics
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    • v.31 no.5
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    • pp.407-411
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    • 2014
  • A 12-year-old castrated male Pekingese dog was presented with weakness, exercise intolerance, and an episode of coughing started 2 weeks earlier upon presentation. Physical examination revealed a grade II/VI left systolic heart murmur. Echocardiographic examination revealed a pericardial effusion and a mass at the heart base located beside the left atrium. The mass beside the left atrium was also visible on the thoracic radiograph after drainage of the pericardial effusion. An aortic body tumor was definitely diagnosed based on postmortem histopathological examination and immunohistochemical staining for specific markers. The dog lived 234 days after diagnosis with only medical management and without recurrence of the pericardial effusion.

Effect of CIMT on the Functional Improvement and BDNF Expression in Hemiplegic Rats Whose Somatomotor Area was Removed (체성운동영역이 제거된 편마비 흰쥐에서 억제 유도치료가 기능향상과 BDNF 발현에 미치는 효과)

  • Lim, Chang-Hun;Hwang, Bo-Gak
    • The Journal of the Korea Contents Association
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    • v.8 no.9
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    • pp.194-203
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    • 2008
  • CIMT(Constraint Induced Movement Therapy) is to improve the function and use of damaged upper limbs by not only confinement of unaffected limbs' exercise but also inducement of affected limbs' one. The purpose of the study is to verify the effect of CIMT by means of motor behaviour test and immunohistochemistry, using animal models. This study was analyzed using 40 male Sprague-Dawley rats as the experimental groups and 40 ones as the control groups. The rats were divided into two random groups : one group as an experimental group which was operated on under anesthesia and removed somatomotor regions with CIMT and the other as the control group without CIMT.Postural Reflex Test, Beam Walking Test, Limb Placement Test and Immunohistochemistry were run on the day 1, 3 , 7 and day 14 following surgery to each 10 rat. As a result, this study demonstrates that CIMT might be an effect method to verify the plasticity of central nervous system as motor behaviour test made all high scores (p<.05) and BDNF was high too in experimental groups.

Identification of Epidermal Growth Factor Receptor(EGF-R) and Transforming Growth $Factor-{\alpha}(TGF-{\alpha})$ in both Malignant Gastric Adenocarcinoma and Adjacent Non-malignant Gastric Mucosa (위암조직과 정상조직에서의 표피성장인자 수용체와 변환성장인자의 규명)

  • 정차권
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.23 no.2
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    • pp.340-347
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    • 1994
  • The specimens used in this study were obtained from patients with primary gastric carcinoma and adjacent non-malignant mucosa from the same patients. Using the techniques of immunocyto chemicstry and in situ hybridization, transforming growth $factor-{\alpha}(TGF-{\alpha})$ and epiderimal growth factor receptor (EGF-R) nRNAs were identified. $TGF-{\alpha}$ was observed in macrophages and dividing tumor cells but, not in normal cells. EGF-R was observed both in malignant and non-malignant gastric tissues. Although normally, $TGF-{\alpha}$ is not seen in normal gastric tissues, $TGF-{\alpha}$ was discovered in the adjacent non-malignant tissue of histolgically normal, which strongly suggest that $TGF-{\alpha}$ is involved in the differentiation of cancer cells. Immunocytochemicstry using EMB-11 antibody identified the existence of macrophages which express $TGF-{\alpha}$ and EGF-R mRNA. Protein products of EGF-R was identfified using monoclonal antibody. Cancer cells were also identified in the non-malignant normal tissues by the method of immunocytochemicstry using carcino embryonic antigen (CEA)antibody. It is considered that the activity of $TGF-{\alpha}$ increased as tumor cell prolifierates. Immunocytochemistry and in situ hybridization techniques can be used to diagnose gastric cancer along with the use of ${\alpha}-feto$ protein and CEA.

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Integration of immunohistochemical reactions into Electrochemical and Optical Analyses of Biochips (면역 조직화학 반응이 통합된 바이오칩의 전기화학 및 광학적 분석)

  • Choi Hyoung Gil;Hong Eun Kyoung;Lee Seung-Won;Yoon Hyun C.
    • KSBB Journal
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    • v.20 no.2 s.91
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    • pp.123-128
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    • 2005
  • We have addressed two important issues of immunosensing biochips, including the construction of antibody functionalized suface for efficient affinity reactions and the development of a signal registration strategy that converts biospecific reactions into highly quantifiable electrochemical and/or optical signals. The developed immunoassay reaction is an integrated version of enzyme-mediated immunoprecipitaion reaction, which is widely used in immunohistochemistry, and electrochemical signaling reaction. For the evaluation of analytical performance of fabricated immunosensing biochips, signaling for mouse IgG in antiserum was conducted. Applications of the developed strategy have been found for the evaluation of histology chemicals and for the signal amplification for array-type biochip analysis.

Immunohistochemical Detection of p53, erbB-2 and CEA Oncoprotein in Lung Cancer; Clinical Correlations (폐암 환자에서 면역조직화학 염색을 통한 p53, erbB-2, CEA 종양단백 발현과 임상적 의의)

  • Jeong, Seong-Su;Kang, Dong-Won;Lee, Gyu-Seung;Ko, Dong-Seok;Suh, Jae-Chul;Kim, Geun-Hwa;Shin, Kyoung-Sang;Kim, Ju-Ock;Song, Gyu-Sang;Kim, Sun-Young
    • Tuberculosis and Respiratory Diseases
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    • v.45 no.4
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    • pp.766-775
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    • 1998
  • Background : The prognosis of patients with lung cancer is still poor. Lung cancer exhibits a variable clinical outcome, even in those patients with same stage. Numerous reports suggest that oncogene expression might playa role in explaining the variability of response and survival But many of these reports are still under debate. So we studied the clinical relevance of oncogene expression in Korean lung cancer patients. Immunohistochemistry of p53, erbB-2, CEA expression was performed. Method: From March, 1992 until March, 1997, 120 patients with lung cancer were reviewed. p53, erbB-2, and CEA expression were detected on paraffin-embedded tumor blocks with the use of monoclonal antibodies. The survival and response has correlated with the expressibility of p53, erbB-2, and CEA oncoprotein Results: Overall, the expression rates of p53, erbB-2, and CEA were 33.7%, 59.3%, and 32.6% respectively. Expression rates were not correlated to cell type or stage. Compared with response to chemotherapy, no correlation was found. The expression of p53, erbB-2, or CEA was not correlated with 2-year survival. With simultaneous applications of p53, erbB-2, and CEA, patients with 2 or more expressions also did not show poor response to chemotherapy. Conclusion: We conclude the p53, erbB-2, and CEA expression are clinically less useful in predicting response to chemotherapy or survival.

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Purification of the Yolk Protein, and Identification of the Synthetic Site of Its Precursor in Eriocheir japonicus (Decapoda, Brachiura) (동남참게(Eriocheir japonicus)의 난황단백질 정제와 그 전구체의 합성부위 구명)

  • HAN Chang-Hee;BAE Hyun-Hwan
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.25 no.5
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    • pp.432-442
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    • 1992
  • To identify the histological site of synthesis of yolk protein precursor, vitellogenin, by immunocytochemical method in the freshwater crab Eriocheir japonicus, we purified the yolk protein, vitellin, from crude egg extracts, and prepared the anti-rabbit serum against vitellin. Then, the site of vitellogenin synthesis was demonstrated by immunotytochemical method with PAP(peroxidase-antiperoxidase) reaction using the rabbit antiserum aganist vitellin. Female specific serum protein was identified in female serum by immunoelectrophoresis and Ouchterlony's immunodiffusion test for mature male and female sera. Based on the immunoelectrophoresis and Ouchterlony's diffusion test for mature male and female sera and crude egg extracts using antiserum against vitellogenic female serum absorbed with male serum, the female specific serum protein was identified as vitellogenin, detected in female serum only. The major yolk protein, vitellin, was purified from the crude egg extracts by DEAE-cellulose ion exchange chromatography, followed by sepharose CL-4B gel filteration chromatography. The molecular weight of vitellin was estimated to be about 245,000 dalton by sepharose CL-4B gel filteration chromatography. from the results of immunological analysis for vitellin, it was found that the vitellin antiserum contained the antibody against vitellogenin. In the results of immunocytochemical reaction by PAP method with the rabbit antiserum against vitellin, the vitellogenic oocytes and the hepatopancreas of mature female showed positive PAP reaction, but not in follicle cells and previtellogenic oocytes nf ovary, muscle of female and mature male hepatopancreas. Therefore, it showed that the hepatopancreas of mature female is the site of vitellogenic synthesis.

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Immunocytochemical Localization of Metallothionein in Gastric Adenocarcinoma (위암 조직내 Metallothionein의 면역 세포화학적 연구)

  • Yang, Seung-Ha;Shin, Kil-Sang;Kim, Wan-Jong
    • Applied Microscopy
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    • v.32 no.4
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    • pp.411-419
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    • 2002
  • Metallothionein (MT) is a family of ubiquitous, low molecular weight ($6,000{\sim}7,000D$), cysteine-rich ($30{\sim}35%$) inducible protein with a high affinity to metal ions and has no aromatic amino acids and histidine. Some of the known functions of MT include detoxification of heavy metals and alkylating agents and neutralization of free radicals. Also, this protein has been reported to involve in tumor pathophysiology and therapy resistance. MT expression may affect a number of cellular processes including gene expression, apoptosis, proliferation and differentiation. Many reports on the physiological and biochemical properties of MT have been published, but ultrastructural reports on the localization of MT in human gastric cancer tissues are extremely rare. The present study was undertaken to examine the ultrastructural features and the localization of MT within the gastric adenocarcinoma. Ultrastructures of gastric cancer cells were characterized by the high nuclear cytoplasmic ratio, the interdigitation between cells, the irregular nucleus containing much heterochromatin and the wide distribution of free ribosomes in the cytoplasm. Immunohistochemical reaction for MT was prominent in the gastric adenocarcinoma. And the immunogold labellings were more prominent within the nucleus than the cytoplasm. Particularly, immunogold particles were numerously seen at nulcleolus or nucleolar associated heterochromatin. These results suggest that MT expression by gastric cancer cells is associated with cell proliferative activity and is possibly synthesized in the cytoplasm, and then the protein is transported into the nucleus to participate in any transcriptional steps.

Immunohistochemical Diagnosis of Renal Pelvis Transitional Cell Carcinoma in a Dog (개의 신우 이행상피암종의 면역조직화학적 진단)

  • Yang, Hyoung-Seok;Kang, Sang-Chul;Kim, Jae-Hoon
    • Journal of Veterinary Clinics
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    • v.30 no.4
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    • pp.292-295
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    • 2013
  • A 9-year-old, male, Doberman pinscher dog with 5-month history of intermittent hematuria, vomiting and glucosuria was referred to local animal hospital. Abdominal ultrasonography showed an irregular and hyperechoic mass in the renal medulla of the enlarged left kidney. Grossly atrophied renal cortex and medulla and marked hydronephrosis were observed on the cut surface of kidney. A single, numerous papillary projected, pedunculated mass 4~5.5 cm in diameter was occupied in renal pelvis, and extended from pelvis to the inlet of ureter. Histopathologically, the mass had numerous papillary structures with arboriform pattern. These papillae were consisted of fibro-vascular stalks that were lined by multiple layers of neoplastic urothelium (transitional epithelium) with marked cellular atypia. Immnohistochemical (IHC) staining demonstrated that the neoplastic cells showed strong positive reactions for cytokeratin (CK) 7, CK 19, CK clone MNF116 and CK high molecular weight, but negative signals for CK 8 low molecular weight. Based on the gross findings, histopathology and CKs profile using IHC staining, this mass was diagnosed as renal pelvis transitional cell carcinoma in a dog.

The Significance of p53 Expression in Serum and Tissue from Patients with Lung Cancer (원발성 폐암환자의 혈청 및 조직에서의 p53단백 표현)

  • Chang, Jung-Hyun;Sung, Sun-Hee
    • Tuberculosis and Respiratory Diseases
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    • v.45 no.2
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    • pp.333-340
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    • 1998
  • Background: Lung cancer is the leading cause of cancer over the world. P53 alteration is by far the most common genetic defect in lung cancer. The mutation of p53 protein involves the loss of inhibitory function of p53 related tumor suppressor gene and resultant oncogenesis. The analysis of p53 alterations consists of immunohistochemical stain, PCR based assay, or serologic ELISA (enzyme-linked immunosorbent assay). Methods : Serum levels of p53 mutant protein were measured in 69 cases of lung cancer (adenocarcinoma n=29, epidermoid n=16, small cell n=13, large cell n=1, undifferentiated n=1, undetermined n=9) and 42 controls of respiratory disorders using ELISA. Immunohistochemical stain in tissue was performed using monoclonal antibody of p53 in lung cancer subjects. Results: Both serum p53s in nonsmall cell cancer ($0.28{\pm}0.44ng/ml$) and in small cell cancer ($0.20{\pm}0.14ng/ml$) were not different from controls ($0.34{\pm}0.20ng/ml$). Also there was no significant difference in serum p53 according to tumor stages. P53 immunohistochemical stain showed 50% positivity overall in lung cancer. There were no close correlation between serologic level and positivity of immunohistochemical stain. Conclusion: The serologic determination of p53 mutant protein is thought to have no diagnostic role in lung cancer. Immunohistochemical stain in lung cancer specimen shows 50% positivity.

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