• 대한두경부종양학회지
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• 제9권1호
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• pp.74-87
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• 1993

Immunohistochemical studies on S-100 protein and lactoferrin were carried out to evaluate the existence and distribution pattern of S-100 protein and lactoferrin positive cells in salivary gland tumors. The specimens used were 25 cases of pleomorphic adenoma, 2 cases of monomorphic adenoma, 2 cases of mucoepidermoid tumor, 2 cases of acinic cell tumor, 3 cases of adenoid cystic carcinoma and 2 cases of adenocarcinoma occured in parotid and submandibular salivary gland. ABC kits(Dako corp. Copenhagen. Denmark) for S-100 protein and lactoferrin were used. The results obtained were summarized as follows: In the normal salivary gland. positive immunoreaction for S-100 protein was observed in myoepithelial cells of acini and intercalated ducts. Positive immunoreaction for lactoferrin was observed in serous acinic cells, epithelial cells of intercalated ducts, and excretory material in the ductal lumina. In the pleomorphic and monomorphic adenomas. most of tumor cells were positive for S-100 protein, while luminal tumor cells in gland-like or duct-like structures were rarely positive for lactoferrin. In mucoepidermoid tumor, most of squamous cells and a few of intermediate cells were positive for S-100 protein, but all of tumor cells were negative for lactoferrin. In acinic cell tumor, most of tumor cells were positive for lactoferrin, but all of tumor cells were negative for S-100 protein. In adenoid cystic carcinoma, basaloid tumor cells in trabecular structure were focally positive for S-100 protein. and in adenocarcinoma, many of tumor cells were posivive for both S-100 protein and lactoferrin. Thus, according to the embryonic stage of the development of the tumor cell origin, it was possible to classify the salivary gland tumor as followings: mucoepidermoid carcinoma which originated from the earliest stage, acinic cell tumor which originated from the end stage. Between these two extremes, there were pleomorphic adenoma, adenoid cystic carcinoma and adenocarcinoma which originated in the middle stage of the development of .the salivary glands. Based on the above results, it can be stated that S-100 protein is demonstrated in tumor cells orginated from myoepithelial cells and lactoferrin in glandular differentiated tumor cells.

• IMMUNE NETWORK
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• 제2권3호
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• pp.175-181
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• 2002

Background: S100A6 is a calcium-binding protein overexpressed in several tumor cell lines including melanoma with high metastatic activity and involved in various cellular processes such as cell division and differentiation. To detect S100A6 protein in patient' samples (ex, blood or tissue), it is essential to produce a monoclonal antibody specific to the protein. Methods: First, cDNA coding for ORF region of human S100A6 gene was amplified and cloned into the expression vector for GST fusion protein. We have produced recombinant S100A6 protein and subsequently, monoclonal antibodies to the protein. The specificity of anti-S100A6 monoclonal antibody was confirmed using recombinant S100A recombinant proteins of other S100A family (GST-S100A1, GST-S100A2 and GST-S100A4) and the cell lysates of several human cell lines. Also, to identify the specific recognition site of the monoclonal antibody, we have performed the immunoblot analysis with serially deleted S100A6 recombinant proteins. Results: GST-S100A6 recombinant protein was induced and purified. And then S100A6 protein excluding GST protein was obtained and monoclonal antibody to the protein was produced. Monoclonal antibody (K02C12-1; patent number, 330311) has no cross-reaction to several other S100 family proteins. It appears that anti-S100A6 monoclonal antibody reacts with the region containing the amino acid sequence from 46 to 61 of S100A6 protein. Conclusion: These data suggest that anti-S100A6 monoclonal antibody produced can be very useful in development of diagnostic system for S100A6 protein.

• Molecular Medicine Reports
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• 제20권3호
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• pp.2476-2483
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• 2019

Atopic dermatitis (AD ) is an inflammatory skin disorder caused by immunological dysregulation and genetic factors. Whether the expression levels of cytokine and skin barrier protein were altered by S100 calcium binding protein A8 (S100A8) and S100A9 in human keratinocytic HaCaT cells was examined in the present study. Alterations of cytokine expression were examined by ELI SA following treatment with S100A8/9 and various signal protein-specific inhibitors. Activation of the mitogen activated protein kinase (MAPK) pathway and nuclear factor (NF)-κB was evaluated by using western blotting and an NF-κB activity test, respectively. The expression levels of interleukin (IL )-6, IL- 8 and monocyte chemoattractant protein-1 increased following treatment with S100A8 and S100A9, and the increase was significantly blocked by specific signaling pathway inhibitors, including toll-like receptor 4 inhibitor (TLR 4i), rottlerin, PD98059, SB203580 and BAY-11-7085. Extracellular signal-regulated kinase (ER K) and p38 MAPK pathways were activated in a time-dependent manner following treatment with S100A8 and S100A9. Phosphorylation of ER K and p38 MAPK were blocked by TLR 4i and rottlerin. S100A8 and S100A9 induced translocation of NF-κB in a time-dependent manner, and the activation of NF-κB was inhibited by TLR 4i, rottlerin, PD98059 and SB203580. In addition, S100A8 and S100A9 decreased the expression of skin barrier proteins, filaggrin and loricrin. These results may help to elucidate the pathogenic mechanisms of AD and develop clinical strategies for controlling AD.

• IMMUNE NETWORK
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• 제3권1호
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• pp.16-22
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• 2003

Background: The S100A2 gene, also known as S100L or CaN19, encodes a protein comprised of 99-amino acids, is a member of the calcium-binding proteins of EF-hand family. According to a recent study, this gene was over-expressed in several early and malignant carcinomas compared to normal tissues. To elucidate the role of S100A2 protein in the process during carcinogenesis, production of monoclonal antibody specific to the protein is essential. Methods: First, cDNA sequence coding for ORF region of human S100A2 gene was amplified and cloned into an expression vector to produce GST fusion protein. Recombinant S100A2 protein and subsequently, monoclonal antibody to the protein were produced. The specificity of anti-S100A2 monoclonal antibody was confirmed by immunoblot analysis of cross reactivity to other recombinant proteins of S100A family (GST-S100A1, GST-S100A4 and GST-S100A6). To confirm the relation of S100A2 to cervical carcinogenesis, S100A2 protein in early cervical carcinoma tissue was immunostained using the monoclonal antibody. Results: GST-S100A2 recombinant protein was purified by affinity chromatography and then fusion protein was cleaved and S100A2 protein was isolated. The monoclonal antibody (KK0723; Korean patent pending #2001-30294) to the protein was produced and the antibody did not react with other members of EF-hand family proteins such as S100A1, S100A4 and S100A6. Conclusion: These data suggest that anti-S100A2 monoclonal antibody produced in this study can be very useful for the early detection of cervical carcinoma and elucidation of mechanism during the early cervical carcinogenesis.

• 대한수의학회지
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• 제40권3호
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• pp.415-420
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• 2000

Distribution of S-100 protein-immunoreactive cells in the gastrointestinal tract of the catfish, Silurus asotus was investigated by PAP method. S-100 protein-immunoreactive cells were mainly observed just under the epithelium of the gastrointestinal tract. Immunoreactive cells were distributed numerously in the stomach and moderately in the middle part of the intestine, however, a few in the upper and lower part of the intestine.

• Journal of Korean Neurosurgical Society
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• 제39권4호
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• pp.271-276
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• 2006

Objective : Despite the recent progress that has been made in intracerebral monitoring, it is still difficult to quantify the exact extent of primary brain damage after severe head injury. In this work, we investigate the role of S-100B protein as a serum marker of brain damage after severe head injury. Methods : 21 patients with severe head injury [GCS score <9] were selected for this prospective study. A venous blood sample was taken as soon as possible after head injury and the serum concentration of S-100B protein was measured daily for five consecutive days. The serum level of S-100B protein was compared with the patients' outcome. The outcome was measured twice, at hospital discharge and after 6 months of follow-up using the Glasgow Outcome Scale[GOS]. Results : Those patients who died within two weeks [after head injury] had a significantly higher serum S-100B value than those who survived [median, 9.64ug/L versus 2.91ug/L]. Seven [78%] of the nine patients who died had a maximum S-100B value of 2ug/L or higher, while three [25%] of the twelve surviving patients showed a maximum S-100B protein value of more than 2ug/L [P<005]. Conclusion : These results indicate that S-100B protein appears to be the most reliable index for estimating the extent of brain damage.

• 한국양식학회지
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• 제8권4호
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• pp.343-354
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• 1995

순환여과식 사육수조에서 잉어(Cyprinus carpio) 치어를 사육하면서, 사료 단백질원인 혈분의 첨가 함량에 따라 총 5개 실험군을 3 반복으로 무작위 배치하고 6 주 동안 사육실험을 하였다. 실험사료의 단백질원은 동물성 $20\%$, 식물성 약 $75\%$를 사용하였고, 조단백질 $40\%$, 3,640 kcal/kg을 기준으로 실험실에서 제조하였다 : 사료 1 (100 FMP, control), $100\%$ fish meal protein : 사료 2 (25 BMP), $75\%$ fish meal $protein+25\%$ blood meal protein : 사료 3 (50 BMP), $50\%$ fish meal $protein+50\%$ blood meal protein ; 사료 4 (75 BMP), $25\%$ fish meal $protein+75\%$ blood meal protein ;사료 5 (100 BMP), $100\%$ blood meal protein. 6 주간의 주사육실험 결과, 혈분 첨가량이 증가할수록 증체량과 사료효율이 증가하였다. 대조군(100 FMP)에 비해 75 BMP와 100 BMP실험군의 증체량과 사료효율이 유의하게 높았다(P<0.05). 3주간의 교차확인실험에서도 100 FMP 대조군보다 100 BMP 실험군에서 높은 증체량과 사료효율을 나타내었다. (P<0.05). 사료의 유인성평가실험은 100 FMP와 100 BMP사료의 유인성을 측정하기 위해 수행되었다. 유인성평가 결과, 초기에는 100 BMP 실험군의 유인성이 100 FMP 대조군보다 낮았으나 2 주만에 큰 차이가 없게 되었다. 본 실험결과, 성장기 잉어 사료의 단백질원으로서 어분단백질을 혈분단백질로 $100\%$까지 대체 가능함을 알 수 있었다.

• Journal of Korean Neurosurgical Society
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• 제44권5호
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• pp.308-313
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• 2008

Objective: The serum S100 protein has been known to reflect the severity of neuronal damage. The purpose of this study was to assess the prognostic value of the serum S100 protein by Elecsys S100 immunoassay in patients with subarachnoid hemorrhage (SAH) and intracerebral hemorrhage (ICH) and to establish reference value for this new method. Methods: Serum S100 protein value was measured at admission, day 3 and 7 after bleeding in 42 consecutive patients (SAH : 20, ICH : 22) and 74 healthy controls, prospectively. Admission Glasgow coma scale (GCS) score, Hunt & Hess grade and Fisher grade for SAH, presence of intraventricular hemorrhage, ICH volume, and outcome at discharge were evaluated. Degrees of serum S100 elevation and their effect on outcomes were compared between two groups. Results: Median S100 levels in SAH and ICH groups were elevated at admission (0.092 versus $0.283{\mu}g/L$) and at day 3 (0.110 versus $0.099{\mu}g/L$) compared to healthy controls ($0.05{\mu}g/L;$ p<0001). At day 7, however, these levels were normalized in both groups. Time course of S100 level in SAH patient was relatively steady at least during the first 3 days, whereas in ICH patient it showed abrupt S100 surge on admission and then decreased rapidly during the next 7 days, suggesting severe brain damage at the time of bleeding. In ICH patient, S100 level on admission correlated well with GCS score (r=-0.859; p=0.0001) and ICH volume (r=0.663; p=0.001). A baseline S100 level more than $0.199{\mu}g/L$ predicted poor outcome with 92% sensitivity and 90% specificity. Logistic regression analyses showed Ln (S100) on admission as the only independent predictor of poor outcome (odd ratio 36.1; 95% CI, 1.98 to 656.3) Conclusion: Brain damage in ICH patient seems to develop immediately after bleeding, whereas in SAH patients it seems to be sustained for few days. Degree of brain damage is more severe in ICH compared to SAH group based on the S100 level. S100 level is considered an independent predictor of poor outcome in patient with spontaneous ICH, but not in SAH. Further study with large population is required to confirm this result.

• 생물정신의학
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• 제14권3호
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• pp.177-183
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• 2007

목 적: 성상세포(astrocyte)에서 생산되어 신경세포의 증식과분화에 관여하는 S100B 단백이 정신분열병의 진행과 증상론과 관련이 있다는 연구가 계속 진행되고 있다. 이에 정신분열병 환자와 정상대조군의 혈청 S100B 농도를 비교하고, 정신분열병 환자의 증상 양상과 S100B 농도와의 연관성을 연구하였다. 방 법: DSM-IV-TR 진단 기준에 따라 정신분열병으로 진단받은 환자 중 정신분열병 최초 발병 환자 혹은 최소 6개월 간 약물 치료를 하지 않은 정신분열병 환자 21명과 정상대조군 27명의 혈청 S100B 농도를 비교하였으며, 정신분열병 환자의 PANSS 전체점수와 양성증상점수, 음성 증상점수 등과 S100B의 혈청농도 간의 상관관계에 대해서 알아보았다. 결 과: 정신분열병 환자에서의 S100B 혈청농도($0.074{\pm}0.039$ ng/ml)와 정상대조군에서의 S100B 혈청 농도($0.072{\pm}0.030$ng/ml)에는 통계적인 차이는 없었다(p=0.925). 또한, 음성증상점수와 S100B 혈청농도(${\rho}$=0.410, p=0.065 ; 표 3)의 상관관계 및 양성증상점수와 S100B 혈청농도 (${\rho}$=-0.390, p=0.080 ; 표 3)의 상관관계는 통계적으로 유의하지 않았다. 결 론: 이번 연구에서 S100B 혈청농도와 정신분열병과의 관련성을 뚜렷하게 발견하기 어려웠다. 이러한 S100B의 역할과 연관성을 확인하기 위해서 연구대상의 확대와 CSF에서의 농도 측정, 장기적 추적 검사, 다른 관련 물질과의 연관성에 대한 추가적인 연구가 필요하다.

• 대한의생명과학회지
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• 제4권2호
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• pp.137-142
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• 1998

쥐 뇌에서 발현되는 S-100 beta 유전자의 다형현상을 조사하였다. Polymerase chain reaction을 위한 주형으로는 뇌에서 분리한 mRNA를 직접 역전사한 cDNA, 또는 rat brain cDNA library에서 분리한 phage DNA를 사용하였다. 증폭된 DNA 절편들은 크기가 기존에 보고되었던 것과 일치하였으나 DNA sequencing을 통한 세부적인 분석 결과 coding region 내에 염기변화 (CAT가 CAC로 변함)가 있음이 확인되었다. 그러나 이들은 모두 histidine을 결정하는 유전암호이기에 단백질의 1차구조에는 아무런 영향을 미치지 않는 다형현상으로 결론지어졌다. 본 연구는 S-100 beta 단백질에 그동안 알려지지 않았던 다형현상이 존재함을 시사하는 것으로서 S-100beta 효소 유전자의 전체적인 구조를 이해하기 위한 학문적 자료가 될 것으로 기대된다.