• Korean Journal of Head & Neck Oncology
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• v.9 no.1
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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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• v.2 no.3
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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.

• IMMUNE NETWORK
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• v.3 no.1
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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.

• Korean Journal of Veterinary Research
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• v.40 no.3
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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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• v.39 no.4
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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.

• Journal of Aquaculture
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• v.8 no.4
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• pp.343-354
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• 1995

A series of feeding experiments were conducted to study the possible utilization of blood meal as a dietary protein source in growing common carp, Cyprinus carpio. Diets were formulated on isonitrogenous and isocaloric basis of $40\%$ crude protein and 3,640 kcal/kg diet : diet 1 (100 FMP, control), $100\%$ fish meal Protein (FMP) : diet 2 (25 BMP), $75\%$ $FMP+25\%$ blood meal protein (BMP) : diet 3 (50 BMP), $50\%$ $FMP+50\%$ BMP : diet 4 (75 BMP), $25\%$ $FMP+75\%$ BMP : d;et 5 (100 BMP), $100\%$ BMP. As the dietary protein sources, $34.2\%$ of animal protein were supplied by FMP and/or BMP, and approximately $65.8\%$ of plant protein were used. In the first experiment, weight gain and feed efficiency were improved with increased level of blood meal protein in the diets. Weight gain and feed efficiency from fish fed diets 4 and S were significantly higher (P<0.05) than those from fish fed diets 1, 2 and 3. The second experiment was designed as a cross-over study to prove the first experiment's results. This cross-over study shows that weight gain from fish fed diet 5 is greater than that from fish fed diet 1. The third experiment was conducted to compare palatability between diet 1 (100 FMP) and 5 (100 BMP). The data from this palatability study indicated that the palatability of diet 5 was lower than that of diet 1 initially, however, the palatability of iiet 5 was improved and not worse than that of diet 1 within a week. Therefore, these findings may suggest that the fish meal can be replaced with blood meal completely in growing common carp diets.

• Journal of Korean Neurosurgical Society
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• v.44 no.5
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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.

• Korean Journal of Biological Psychiatry
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• v.14 no.3
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• pp.177-183
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• 2007

Objectives:Previous studies have suggested that S100B protein play an important role in the pathogenesis and progress of schizophrenia. In the present study, we evaluate the serum levels of S100B in the patients with schizophrenia, and compare them with those of healthy controls. Method:The serum S100B levels were measured by lectrochemiluminescence immunoassay in 21 schizophrenic patients (8 males, 13 females) and 27 normal controls(11 males, 16 females). The Positive and Negative Syndrome Scale(PANSS) was used to evaluate the symptoms of the patients with schizophrenia, and the correlation between PANSS subscale scores and serum S100B levels was examined. Results:No significant difference was found between the serum S100B levels of the schizophrenic patients($0.074{\pm}0.039$ng/ml) and those of the normal controls($0.072{\pm}0.030$ng/ml)(p=0.925). Correlationships between the high serum S100B level with high negative symptom scores(p=0.065) or with the low positive symptom scores(p=0.080) did not exist. Conclusion:The relation between serum S100B level and schizophrenia was not found in the present study. However, to confirm this result, further studies, such as measurement of S100 protein level in CSF, postmortem study, long-term follow-up study, and studies with other neurotrophic proteins are needed.

• Biomedical Science Letters
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• v.4 no.2
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• pp.137-142
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• 1998

We examined mRNAs, isolated from the rat brain, to ascertain if there is any polymorphism for S-100 beta protein gene. As templates for polymerase chain reaction (PCR) the reverse-transcribed cDNA from the rat brain or phage DNAs isolated from the rat brain cDNA libraries were used. Although PCR products turned out to be exactly same as the expected size based on the previously reported mRNA sequence a single base substitution (CAT to CAC) was identified at nucleotide level. This change was considered as polymorphism since it did not cause any change of the primary structure for S-100 beta protein. This result should facilitate the understanding of the overall structure of the gene for S-100 beta protein.

• Biomedical Science Letters
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• v.23 no.1
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• pp.44-47
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• 2017

S100A8 and S100A9 are associated with myeloid cell differentiation, chemotactic activities, adhesion of neutrophils, and apoptosis. In this study, we investigated the contribution of S100A8 and S100A9 to differentiation of the human eosinophilic leukemia cell line, EoL-1. S100A8 and S100A9 increased the number of vacuole per one cell and the protein expression of EPO and MBP. Rottlerin, an inhibitor of protein kinase C delta ($PKC{\delta}$), inhibited the EoL-1 cell differentiation induced by S100A8 and S100A9. These results suggest that S100A8 and S100A9 may regulate the differentiation of eosinophilic progenitors. Moreover, these findings may shed light on elucidation of eosinophil differentiation due to S100 proteins.