한국산 겨우살이(Viscum album coloratum)로부터 추출된 lectin의 돼지에 대한 독성 및 오제스키병 백신의 면역원성에 미치는 영향

여상건,Yeo, Sang-Geon 대한수의학회 2006 大韓獸醫學會誌 Vol.46 No.3

In the present study toxicity and immunostimulating activity of the lectin(KML-C), which was extracted from Korean mistletoe(Viscum album coloratum) were investigated in swine. To determine the toxicity, lectin was injected into thigh or cervical muscles of 4-week-old piglets(Landrace) and observed clinically and pathologically. For determination of the immnunostimulating activity, lectin($0.7{\mu}g/kg$ of body weight)-adjuvanted vaccine of Aujeszky's disease virus(ADV)(NYJ1-87) which was inactivated by 0.2% formalin was injected into the cervical muscle of antibody-negative piglets in the same age group. Subpopulation of the immune cells and serum neutralizing(SN) antibodies in the piglets were examined after vaccination, and resistance of the piglets against challenge by virulent NYJ1-87 was further examined. The results were also compared with those from piglets injected with aluminum hydroxide [$Al(OH)_3$]-adjuvanted vaccine of inactivated NYJ1-87 and NYJ1-87 vaccine without adjuvant, and the results are as follows. By injection of lectin with $30{\mu}g/kg$ of body weight to the thigh muscle, all of 12 piglets died after signs such as dyspnea, fever, systemic erythema and subcutaneous hemorrhages, and lesions pertaining to poisonous hepatitis and dysfunction of kidney were observed. By injection of lectin with $7{\mu}g/kg$ of body weight to the thigh muscle, all of 12 piglets showed signs such as edema and cutaneous hemorrhage in the injected area, lameness and depression, and lesions pertaining to poisonous hepatitis and dysfunction of kidney were observed. By injection of lectin with 1, 3 and $5{\mu}g/kg$ of body weight to the thigh muscle of each one piglet, signs such as congestion, induration and grayish coloration in the injected area, depression and inappetence were observed in all piglets. Toxic changes were also observed in the liver and kidney of piglets by lectin of 3 and $5{\mu}g$. By injection of lectin with 0.5 and $0.7{\mu}g/kg$ of body weight to the cervical muscle of each 9 piglets, all piglets were clinically normal and there were no significant changes in blood counts and chemistry values. Whereas, epithelial swelling and vacuolation of convoluted tubules were observed from one piglet injected with lectin of $0.7{\mu}g$, and necrosis and fibrosis of muscular fiber were observed in the muscle of one piglet injected with lectin of $0.5{\mu}g$. Only population of sIgM+ B lymphocytes increased among immune cells in all of 15 piglets immunized with lectin($0.7{\mu}g/kg$ of body weight)-adjuvanted vaccine, while compared to those in $Al(OH)_3$-adjuvanted vaccine and vaccine without adjuvant. No additional stimulation to the immune cells was recognized when lectin was added to $Al(OH)_3$-adjuvanted vaccine. In piglets immunized with lectin-adjuvanted vaccine, SN titers in reciprocal values for loge were 1.3-4.0 at 1-4 weeks after vaccination, which was similar to those with 1.0-3.3 by vaccine without adjuvant but lower than those with 2.0-5.7 by $Al(OH)_3$-adjuvanted vaccine. Also, no additional increase in the SN titers was recognized when lectin was added to $Al(OH)_3$-adjuvanted vaccine. Piglets immunized with lectin-adjuvanted vaccine were resistant to challenge by the virulent NYJ1-87 at 4 weeks after vaccination, and the SN titers reached to 5.0 one week after challenge, which was higher than those with 4.0 by vaccine without adjuvant but somewhat lower than those with 7.7 by $Al(OH)_3$-adjuvanted vaccine.

한국산 겨우살이(Viscum album coloratum)로부터 추출된 lectin의 닭에 대한 독성 및 뉴캐슬병 백신의 특이면역 증강 효과

여상건,Yeo, Sang-Geon 대한수의학회 2006 大韓獸醫學會誌 Vol.46 No.3

In order to search the availability of the lectin extracted from Korean mistletoe(Viscum album coloratum) as an adjuvant for the avian vaccines, attempts were made to determine toxicity of the lectin in chicks and its immunostimulating activity on the inactivated vaccines against Newcastle disease virus(NDV). For the determination of toxicity, the lectin was injected into the thigh muscle of SPF chicks(Charles River) of 1-week-old and observed hematologically and pathologically. For the determination of immunostimulating effects, lectin-adjuvanted, inactivated NDV vaccines were injected into the thigh muscle of SPF chicks in the same age group. Sera of the chicks were examined for the hemagglutination-inhibition(HI) antibodies induced, their HI titers and reaction to the NDV antigens. The data were further compared with those from aluminum hydroxide [$Al(OH)_3$]-adjuvanted vaccines and vaccines without adjuvant, and the results are as follows. There were no significant changes observed in the values of RBC, WBC, Hb, PCV, MCV, MCH, MCHC, AST, ALT, BUN, creatinine and total proteins in the chicks administered with lectin of 1.1, 2.2 and $22.2{\mu}g/kg$ body weight, which means the lectin has no effects on blood values and functions of liver and kidney. In histopathologic observation, no lesions were observed in the brain, heart, liver, lung, spleen, kidney, thymus and bursa of Fabricius of the chicks administered with lectin of 1.1, 2.2 and $22.2{\mu}g/kg$ body weight. There were inflammatory lesions, such as congestion, hemorrhage, edema, infiltration of macrophages and coagulation necrosis observed in the thigh muscle of chicks administered with lectin of $22.2{\mu}g/kg$ body weight, whereas no changes were observed in 1.1 and $22.2{\mu}g/kg$ lectin administered chicks. In chicks immunized with lectin($4.4{\mu}g/kg$ of body weight)-adjuvanted B1, LaSota and Ulster 2C vaccines, HI titers in reciprocal values for $log_2$ were 1.8-2.2 at 1 week after vaccination, which was similar with those of 1.5-2.9 by $Al(OH)_3$-adjuvanted vaccines. The HI titers by the lectin-adjuvanted vaccines reached to 3.9-5.3 at 4 weeks, whereas those by the $Al(OH)_3$-adjuvanted vaccines were more high as 7.3-9.3. Meanwhile, the immunostimulating effects of the lectin were recognized while compared to the HI titers with 2.4-3.7 in chicks immunized with vaccines without adjuvants at 4 weeks after vaccination. The chicks immunized with lectin-adjuvanted vaccines were enough to resist challenges by Kyojeongwon strain, a very virulent NDV at 4 weeks after vaccination as well as chicks immunized with $Al(OH)_3$-adjuvanted vaccines. The HI titers by the lectin-adjuvanted vaccines reached to high level as 8.7-10.3 as those with 8.2-9.6 by the $Al(OH)_3$-adjuvanted vaccines at 6 weeks after vaccination, which may be the booster effects by the challenge virus. Antibodies specific to the HN and F antigens of NDV were observed in the sera of both chicks immunized with lectin-adjuvanted vaccines and $Al(OH)_3$-adjuvanted vaccines.

대두 근류균의 리포 다당과 Lectin의 결합성

박우철,김진호,강상재 慶北大學校農業科學技術硏究所 1997 慶北大農學誌 Vol.15 No.-

근류균과 두과작물의 공생에서 숙주결합성을 조사하기 위하여 대두 종자 및 유근으로부터 분리한 lectin과 근류균의 표피다당과의 결합성을 확인한 결과는 다음과 같다. 팔달, 백운 및 황금으로부터 분리한 종자선을 형성하였다. 대두 종자 lectin및 뿌리 추출물은 R. japonicum및 B. japonicum과 결합하였고 R. viceae와는 결합 하지 않았으며 완두의 lectin은 R. viceae와 결합하였으나 R. japonicum및 B. japonicum과는 결합 하지 않았다. B. japonicum과 R. viceae로 부터 분리한 세포표피 다당의 겔 여과한 결과 두개의 분획으로 각각 나타났다. B. japonicum으로 부터 분리한 표피다당은 대두의 종자 lectin과 결합하였으나 R. viceae로 부터 분리한 표피다당은 대두 lectin과 결합하지 않았다. 이상의 결과로부터 근류균이 숙주세포와 결합할 때 숙주를 인식하는 초기 단계에서 lectin이 관여함을 추론할 수 있고 이것이 상호접종군을 형성하는데 매개역할을 하는 것으로 추정할 수 있었다. This study was carried out to research the biological characteristics among rhizobia and soybean seed and root lectins, and to obtain a basic imformation of host specificity in biological nitrogen symbiosis system. The results obtained were as follows; Purified seed lectin from soybean varieties of paldal, backwoon and hwangkeum formed immunoprecipitin lines with standard soybean seed lectin and the root lectins from soybean seedlings immunoelectrophoretically. Soybean seed and root lectins interacted with Rhizobium japonicum and Bradyrhizobium japonicum, but didn't interacted with Rhizobium, viceae, whereas pea lectin conjugated with R. viceae, but didn't bind with R. japonicum and B. japonicum. Lipopolysaccharides of B. japonicum and R. viceae were fractionated into LPS Ⅰand LPS Ⅱ on the sephadex G-50. Lipopolysaccharides from B. japonicum showed rhe binding activity both with soybean seed lectin and root lectin, but those from R. viceae didn't show it with soybean seed and root lectins.

대두-근류균의 공생에서 Lectin에 의한 결합특이성

김진호,박우철,강상재,Kim, Jin-Ho,Park, Woo-Churl,Kang, Sang-Jae 한국응용생명화학회 1997 Applied Biological Chemistry (Appl Biol Chem) Vol.44 No.4

근류균과 대두의 공생에서 숙주 결합성을 조사하기 위하여 대두종자로 부터 분리한 lectin과 뿌리추출물과의 동일성 여부를 조사한 결과는 다음과 같다. 탈지 대두분으로 부터 분리한 lectin은 크로마토그라피와 전기영동상 단일물질로 분리되었고 백운 및 팔달로 부터 분리한 lectin은 표준 lectin의 항체와 항원-항체 반응을 나타내어 동일한 물질이었다. 종자lectin 및 뿌리추출물 및 뿌리분비물에 대한 화학주성은 RCR 3407, KCTC 2422에서 뿌리분비물에 대한 주성이 가장 높았고 종자 lectin과 뿌리추출물은 비슷한 화학주성을 나타내었다. 대두의 유근으로 부터 분리한 뿌리추출물은 표준 lectin의 항체와 침강선을 형성하여 대두 종자 lectin과 동일한 물질임을 알수 있었으며 뿌리 분비물과는 침강선을 형성치 않았다. 대두와 상호접종군을 형성하는 RCR3407, KCTC2422 및 LPN-101은 대두의 종자 lectin 및 뿌리추출물과 결합하였으나 완두의 lectin과는 결합하지 않았고 대두와 근류형성을 하지않는 LPN-100은 대두의 lectin과 결합하지 않았다. This study was carried out to elucidate the biological characteristics of Rhizobia in biological nitrogen fixation system. The results of investigation were as follows; Polyacrylamide gel electrophoresis pattern of root lectin in the presence of SDS was ascertained electrophoretically and chromatographically. The purified root lectin formed immunoprecipitin line with anti lectin rabbit IgG. Root lectin, seed lectin and root exudate were tested for chemotactic ability. Chemotactic responses of RCR3407 and KCTC2422 toward root exudate were stronger than those of seed lectin and root lectin, but there didn't occur chemotactic responses of LPN100, not bound with seed lectin and that of LPN101, bound with seed lectin toward root exudate, root lectin and seed lectin. RCR3407, KCTC2422 and LPN-101, which nodulated with soybean, interacted with soybean lectin, but not with pea lectin. LPN-100, which was not nodulated with soybean, didn't interact with soybean lectin.

Saccharomyces cerevisae에서 한국산 겨우살이 유래 lectin A 및 B 유전자의 발현

최윤혁,김종배,양웅석,황철원 한국생명과학회 2004 생명과학회지 Vol.14 No.5

A study for expression of Korean Mistletoe (KM) lectin gene (A,B) in Saccharomyces cerevisiae was done using transforming system of yeast. In order to overexpress the genes efficiently in yeast, two lectin genes (A,B) were re-cloned and modified including Kozak translation initiation sequence using PCR amplification. The constructed plasmids containing modified lectin A and B genes were transformed to S. cerevisea INVSc (MAT G, his3 $\Delta$1, leu2, trpl-289, ura3-52). The transformed cells were identified by DNA sequencing with ABI3700 system and induced with 2% of galactose for recombinant KM lectin (rKM lectin) protein. The rKM lectin A and B proteins were determinated about 29kDa size of protein by SOS-P AGE and western blotting analysis. The expressed recombinant lectin was determinated 1.24∼1.75 $\mu\textrm{g}$ per 1 mg of cytosolic soluble protein by sandwich ELISA method. Moreover the lectin genes were expressed as maximum level at 36 h after galactose induction and lectin A gene was were repressed after 48 h. 본 연구는 한국산 겨우살이 lectin유전자 (A 및 B chain) 을 효모 (Saccharmyces cerevisiae) 에 형질 전환시키는 시스템을 사용한 것으로, 효모내 효과적인 lectin유전자 발현을 위하여 유전자 상에 Kozak translation initiation sequence를 PCR을 이용 삽입, 변형시켜 재 클로닝 하였다. 변형된 lectin A 및 B 유전자를 포함하는 재조합 플라스미드는 S. cerevisiae INVSc (MATa, his3 $\Delta$l, leu2, trpl-289, ura3-52) 에 형질전환 되었다. 형질전환된 효모는 ABI 3700 system을 이용한 DNA 염기서열 분석을 통해 확인되었고 재조합 한국산겨우살이 lectin 발현을 위해 2% galactose를 사용하여 유도발현되었다. 재조합 lectin A 및 B 단백질은 SDS-PACE 및 western blotting 분석을 수행한 결과 약 29kDa 크기로 확인되었다. 재조합 lectin은 세포내 가용성 단백질 1mg중 1.24∼l.75 $\mu\textrm{g}$ 수준으로 발현되어짐을 ELISA 분석을 통해 확인하였다. 한편 lectin 유전자는 galartose 유도발현 후 36시간이 되 었을 때 발현량이 최대가 되었으며 lectin A 유전자의 경우 48 시간 이후에는 발현이 억제되었다.

Analysis of EST and lectin expressions in hemocytes of Manila clams (<i>Ruditapes philippinarum</i>) (Bivalvia: Mollusca) infected with <i>Perkinsus olseni</i>

Kang, Yoon-Suk,Kim, Young-Mee,Park, Kyung-Il,Kim Cho, Somi,Choi, Kwang-Sik,Cho, Moonjae Elsevier 2006 Developmental and comparative immunology Vol.30 No.12

<P><B>Abstract</B></P><P>The hemocytes of invertebrates play key roles in both cellular and humoral immune reactions by phagocytosis or delivering immune factors such as lectin and anti-microbial peptides. Bacterial infection causes changes in components such as lectins, anti-bacterial peptides, and lysosomal enzymes of plasma or hemolymph in molluscs. Previously, we found that infection with the protozoan parasite, <I>Perkinsus,</I> increases lectin synthesis in hemocytes. In order to investigate the patterns of genes expressed in Manila clams (<I>Ruditapes philippinarum</I>) infected with the protozoan parasite <I>Perkinsus olseni</I>, we constructed a cDNA library and sequenced 1850 clones (expressed sequence tags). A total of 79 ESTs, were related to 29 functional immune genes such as C-type lectin, lysozyme, and cystatin B, in Manila clams. Lectins were the largest group of immune-function ESTs found in our Manila clams library. Among 7 lectin clones, two full length cDNAs of lectins were cloned. MCL-3, which is a simple C-type lectin composed of 151 amino acids, has a relatively short signal sequence of 17aa and single carbohydrate-recognition domain (CRD) of ∼130 residues. It is highly homologous to eel C-type lectin. The sequence of mc-sialic acid-binding lectin consists of 168 amino acid residues with molecular weight of 19.2 and shows high homology to sialic acid-binding lectin from the snail, <I>Cepaea hortensis</I>.</P><P>The expression of 7 different lectins in hemocytes was analyzed by RT-PCR using gene-specific primers. Hemocytes from <I>Perkinsus</I>-infected clam expressed different sets of lectins than with <I>Vibrio</I> infection. These results demonstrate that several lectins are involved in Manila clam innate immunity and different challenges induce expression of different lectins.</P>

Comparison of Biochemical Characterization of Korean and Chinese Mung Bean Lectin

Kwang Soo Roh(노광수) 한국생명과학회 2014 생명과학회지 Vol.24 No.6

한국산과 중국산 녹두 종자에서 0.15 M NaCl/0.1 M sodium phosphate buffer (pH7.0)에 의한 추출, (NH₄)₂SO₄ 침전, 최종적으로 Sephadex G-100을 이용한 affinity chromatography에 의해 lectin을 분리한 다음, 이들의 생화학적 특성을 조사, 비교하였다. 사람의 적혈구는 trypsin의 처리 유무와 상관없이 응집반응이 일어나지 않으며, 토끼의 적혈구에서는 trypsin을 처리한 경우에만 응집반응이 일어났다. 두 녹두 종자 lectin의 분자량은 SDS-PAGE를 통해 54 kDa와 28 kDa로 확인되었다. 한국산 녹두 종자 lectin의 최적 반응 온도는 60℃이며, 중국산 녹두 종자 lectin의 경우는 50℃로 나타났다. 종자 lectin이 열에 가장 안정한 온도는 한국산의 경우는 50℃이며, 중국산의 경우 40-50℃로 밝혀졌다. 한국산 녹두 종자 lectin은 pH 3.2에서 가장 높은 활성을 보였으며, 중국산 녹두 종자 lectin은 pH 6.2에서 가장 높은 활성을 보였다. 변성제를 처리했을 때, thiourea와 guanidine-HCl과는 혈액 응집이 일어나지 않아 변성작용이 일어남을 알 수 있었고, urea와는 혈액 응집이 일어나지 않아 변성작용이 일어나지 않음을 알 수 있었다. D-glucose외 6가지의 탄수화물에 대한 특이성이 나타나지 않았다. 또한 두 녹두 종자의 lectin은 Ca<SUP>2+</SUP>, Co<SUP>2+</SUP>, Cu<SUP>2+</SUP>, Fe<SUP>2+</SUP>, Mg<SUP>2+</SUP> 및 Mn<SUP>2+</SUP> 등의 금속이온에 대한 특이성이 없었다. The lectins were separated from Korean and Chinese mung bean seeds finally via chromatography using Sephadex G-100 and their biochemical features were studied and compared. They showed no hemagglutination with human red blood cells regardless of trypsin treatment and showed hemagglutination with only trypsin treated rabbit red blood cells. The molecular weights of two lectins were identified as 54 kDa and 28 kDa by SDS-PAGE. It was found that while the optimal reaction temperature of the lectin from Korean mung bean was 60℃, that of the lectin from Chinese mung bean seeds was 50℃. It was found also that the most thermal stable temperature of the seed lectin from Korean mung bean seeds was 50℃ and the lectin from Chinese mung bean was 40-50℃. The lectin from Korean mung bean seeds showed the highest activity at pH 3.2 and the lectin from Chinese mung bean showed the highest activity at pH 6.2. It was identified that when treating a denaturant, thiourea and guanidine-HCl resulted in no hemagglutination, so they induced denaturalization. It was identified also that there was no hemagglutination with urea, so it did not induced denaturalization. They showed no septicity to 6 types of carbohydrates including D-glucose. In addition, the lectins from the two mung bean seed had specificity to metal ions.

방울토마토 열매 locular fluid lectin의 항균성과 생화학적 특성

노광수(Kwang Soo Roh) 한국생물공학회 2010 KSBB Journal Vol.25 No.3

Lectin은 당 결합 단백질과 세포 응집 단백질로서, 식물 방어의 역할도 하는데 방울토마토 열매의 locular fluid에는 곰팡이로부터 식물의 보호 기능을 하는 것으로 생각되는 chitin 결합 lectin이 들어 있다. 이에 본 연구에서는 방울토마토의 locular fluid로부터 최종적으로 Sephadex G-200을 통과시켜 lectin을 분리한 다음, 이의 항균성과 분자량, 적혈구 응집력, 혈액특이성, 최적 온도, 열 안정성 및 최적 pH 등의 생화학적 특성을 연구하였다. 식물성 병원균인 4개의 균주 중 Cladosporium cucumerinum과 Monosporascus cannonballus에 대해서는 항균 활성을 나타내었으나, Fusarium oxysporum과 Rhizoctonia solani에 대해서는 항균 활성을 나타내지 않았다. SDS-PAGE의 결과, 2개의 band로 나타났으며, 이의 분자량을 표준 단백질을 이용 측정하여 87 kDa와 47 kDa로 계산되었다. 사람의 A, B, O, AB형의 혈액을 사용하여 각각의 혈구응집반응을 확인한 결과, A, B, O, AB형 모두에서 응집반응이 일어났으며, 이 중 B형 혈액에서 가장 높은 활성을 나타내었다. 분리된 방울토마토 locular fluid lectin의 최적 반응 온도는 30℃이며, 가장 높은 30℃ 를 포함하는 20-80℃ 범위에서 열 안정성을 보였고, 최적 pH는 7.0이다. Lectins are carbohydrate-binding and a cell-agglutinating proteins, and are concerted with a plants defence mechanism. In particular, chitin-binding lectins in locular fluid of cherry tomato fruit seemed to have a role in defending plants against fungi. The antifungal activity using lectin isolated from locular fluid of cherry tomato fruit was measured in the plant pathogen Cladosporium cucumerinum, Monosporascus cannonballus, Fusarium oxysporum, and Rhizoctonia solani. Amoung the four strains, a potent antifungal activity was detected in Cladosporium cucumerinum and Monosporascus cannonballus, not in Fusarium oxysporum, and Rhizoctonia solani. The molecular weight of this lectin isolated as double protein bands by SDS-PAGE was calculated to be 87 kDa and 47 kDa from the relative mobilities compared with those of reference molecular weight markers. The isolated lectin agglutinated human red blood cells (A, B, AB, O) treated with trypsin, and the most activity was found at B. The optimal temperature of isolated lectin was at 30℃. For the thermal stability, lectin was stable at 20-80℃. The optimal pH of this lectin was at 7.2, and showed complete loss below pH 9.0.

조피볼락, 용치놀래기, 송곳니베도라치 및 졸복 식도 점액세포의 복합당질에 대한 Lectin 조직화학

정길남,이응희,조기진,정권순,조운복 한국생명과학회 2004 생명과학회지 Vol.14 No.3

경골어류인 조피볼락, 용치놀래기, 송곳니베도라치 및 졸복 식도 점액세포의 복합당질 성상을 biotinylated lectin인 DBA, SBA, PNA, BSL-1, RCA-1, sWGA, UEA-1, LCA 및 Con A로 연구하였다. 조피볼락과 용치놀래기는 큰ㆍ중간 및 작은 점액세포가 섞여 있었고, 송곳니베도라치와 졸복은 중간 및 작은 점액세포들이 섞여 있었다. 식도 점액세포들의 lectin 결합양상도 어종에 따라 차이가 있었으며 조피볼락은 DBA, SBA, BSL-1, RCA-1 및 sWGA에, 용치 놀래기는 DBA, SBA, PNA 및 sWGA에, 송곳니베도라치는 SBA 및 sWGA에 각각 반응을 하였으며 졸복은 DBA, LCA 및 Con A를 제외한 모든 lectin에 반응하였다. 조피볼락의 모든 점액세포에는 DBA, SBA 및 sWGA가, 작은 점액세포에는 이 외에 BSL-1이 반응하였다. 용치놀래기의 큰 점액세포에서는 PNA가, 중간 점액세포에는 DBA, SBA 및 sWGA가, 작은 점액세포에는 DBA와 SBA가 반응하였다. 송곳니베도라치의 중간 점액세포에는 sWGA가, 작은 점액세포에는 SBA와 sWGA가 반응하였으며 졸복은 모든 점액세포에 SBA, PNA 및 RCA-1가, 중간 점액세포에는 이 외에 sWGA와 UEA-1이 반응하였다. 특히 조피볼락의 점액세포에서 DBA와 SBA의 양이 많고, 용치놀래기에서는 큰 점액세포에서 PNA 양이, 중간 및 작은 점액세포에서 SBA양이 많았으며, 졸복의 경우 중간 점액세포에서 SBA, PNA, sWGA 및 UEA-1의 양이, 작은 점액세포에서 RCA-1의 양이 많았다. This study attempts to investigate lectin binding patterns of the glycoconjugates of the esophageal mucous cells in four teleostean speceis, i. e., Sebastes schlegeli, Halichoeres poecilopterus, Bryzoichthys lysimus and Takifugu pardalis. To investigate glycoconjugates of esophageal mucous cells, nine biotinylated lectins (DBA, SBA, PNA, BSL-l, RCA-l, sWGA, UEA-l, LCA and ConA) were applied with ABC method. Esophageal mucous cells of Sebastes schlegeli and Halichoeres poecilopterus were mixed with large, medium sized and small mucous cells. But these cells of the other species only were mixed with medium sized and small mucous cells. The lectin binding pattern of esophageal mucous cells depends on the species; Sebastes schlegeli was stained with DBA, SBA, BSL-l, RCA-l and sWGA, Halichoeres poecilopterus with DBA, SBA, PNA and sWGA, Bryzoichthys lysimus with SBA and sWGA, Takifugu pardalis with all lectins except DBA, LCA and Con A, respectively. All the mucous cells of Sebastes schlegeli were stained with DBA, SBA and sWGA, while small mucous cells with BSL-l besides these lectins. In Halichoeres poecilopterus,l the large mucous cells reacted with PNA, medium sized mucous cells with DBA, SBA and sWGA, and small mucous cells with DBA and SBA, respectively. Medium sized mucous cells of Bryzoichthys lysimus were stained with sWGA, and small mucous cells with SBA and sWGA. In Takifugu pardalis, all mucous cells reacted with SBA, PNA and RCA-l, but medium sized mucous cells with sWGA and UEA-l besides these lectins. Especially DBA and SBA lectins showed a strong binding to all mucous cells of Sebastes schlegeli. In Halichoeres poecilopterus, PNA binding were notable in large mucous cells, and SBA binding in medium sized and small cells, respectively. However, SBA, PNA, sWGA and UEA-l lectins of Takifugu pardalis showed a strong binding to medium sized mucous cells, but RCA-l binding which small mucous cells were notable.

겨우살이 Lectin의 항당뇨 효과

장철수,노광수 대한의생명과학회 2000 Journal of biomedical laboratory sciences Vol.6 No.2

국문초록 : 겨우살이 (Viscum album)는 민간요법에서 여러 질환에 치료제로 쓰이고 있다. 이는 겨우살이가 가지고 있는 lectin의 약리작용에 의한 것으로 그 가능성을 알아보고자 겨우살이 lectin의 항당뇨 효과를 연구하였다. 이를 위해 streptozotocin으로 당뇨를 유발시킨 흰쥐에 국내 참나무류에 기생하는 겨우살이의 추출물과 정제된 lectin을 경구와 복강내에 투여하여 조사하였다. 추출물을 29일 동안 경구 투여시 혈당치가 36%까지 현저히 감소하였으나, 정제된 lectin을 경구 투여시 항당뇨 효과가 현저히 나타나지 않았다. 또한 정제된 lectin 0.4 mg/kg을 복강내에 주사시 당뇨군에서 2시간과 4시간에서 saline에 비해 혈당치가 각각 32%와 28% 감소하였으므로 lectin의 항당뇨 효과는 뚜렸하였다. We investigated anti-diabetic effect of the crude extracts and the lectin purified from the leaves of Viscum album collected in Mt. Duk Yu. The induction of diabetes mellitus was confirmed by the presence of statistically significant greater serum glucose levels in streptozotocin-treated rats compared with the untreated non-diabetic group. There are no significant differences in the serum glucose levels compared extracts and purified lectin to tap water in the non-diabetic group after administration through the oral cavity in 29 day. But for streptozotocin-induced diabetic rats the serum glucose level in extracts after administration through the oral cavity was strikely decreased to 36% than tap water in 29 day. Significantly lower glucose level was obtained at 2 hr and 4 hr after administration of purified lectin (0.4mg/kg) through the peritoneal cavity. These results provide an evidence that Viscum album lectin has an anti-diabetic effect pharmacologically.