Pub Date : 2001-11-17DOI: 10.1136/bmj.323.7322.1184
G L Sayer
{"title":"Nodular thyroid disease. Abnormal thyroid function may be positive discriminator for malignancy.","authors":"G L Sayer","doi":"10.1136/bmj.323.7322.1184","DOIUrl":"10.1136/bmj.323.7322.1184","url":null,"abstract":"","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"109 1","pages":"1184"},"PeriodicalIF":105.7,"publicationDate":"2001-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1121653/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82237284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Neurocan is a chondroitin sulfate proteoglycan of the lectican family and a component of the extracellular matrix of the central nervous system. It is mainly expressed during modeling and remodeling stages of this tissue. Neurocan can bind to various structural extracellular matrix components, such as hyaluronan, heparin, tenascin-C and tenascin-R, and the growth and mobility factors FGF-2, HB-GAM, and amphoterin. Neurocan can also interact with several cell surface molecules, such as N-CAM, L1/Ng-CAM, TAG-1/axonin-1, and an N-cadherin-binding N-acetyl-galactosamine-phosphoryl-transferase, and in vitro studies have shown that neurocan is able to modulate the cell-binding and neurite outgrowth promoting activites of these molecules. Current analysis of the molecular structures and substructures involved in homophilic and heterophilic interactions of these molecules and complementary loss-of-function mutations might shed some light on the roles played by neurocan and interacting molecules in the fine tuning of the nervous system.
{"title":"Neurocan: a brain chondroitin sulfate proteoglycan.","authors":"U Rauch, K Feng, X H Zhou","doi":"10.1007/PL00000822","DOIUrl":"10.1007/PL00000822","url":null,"abstract":"<p><p>Neurocan is a chondroitin sulfate proteoglycan of the lectican family and a component of the extracellular matrix of the central nervous system. It is mainly expressed during modeling and remodeling stages of this tissue. Neurocan can bind to various structural extracellular matrix components, such as hyaluronan, heparin, tenascin-C and tenascin-R, and the growth and mobility factors FGF-2, HB-GAM, and amphoterin. Neurocan can also interact with several cell surface molecules, such as N-CAM, L1/Ng-CAM, TAG-1/axonin-1, and an N-cadherin-binding N-acetyl-galactosamine-phosphoryl-transferase, and in vitro studies have shown that neurocan is able to modulate the cell-binding and neurite outgrowth promoting activites of these molecules. Current analysis of the molecular structures and substructures involved in homophilic and heterophilic interactions of these molecules and complementary loss-of-function mutations might shed some light on the roles played by neurocan and interacting molecules in the fine tuning of the nervous system.</p>","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"65 1","pages":"1842-56"},"PeriodicalIF":6.2,"publicationDate":"2001-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11337305/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82191209","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K Honjoh, H Shimizu, N Nagaishi, H Matsumoto, K Suga, T Miyamoto, M Iio, S Hatano
A cryoprotective protein, HIC6, was expressed transgenically in tobacco, a cold-sensitive plant, and the localization of the protein within the cell as well as freezing tolerance of the transgenic tobacco was investigated. For constitutive expression of HIC6 in tobacco, its corresponding gene was subcloned into pBI121. Through the transformation with pBI121/hiC6, fifteen transgenic tobacco lines were acquired, out of which twelve lines expressed the HIC6 protein. None of the transgenic tobacco lines, however, showed significant differences in freezing tolerance from the control plants (wild-type and transformed with pBI121) at -1, -3, and -4 degrees C, with the exception that their freezing temperature was -2 degrees C. In order to increase the accumulation level of HIC6, pBE2113 with a stronger promoter was used. Eight lines expressed the protein out of thirteen lines transformed with pBE2113/hiC6. The accumulation levels of the protein were clearly higher in the tobacco plants transformed with pBE2113/hiC6 than in those with pBI121/hiC6. The HIC6 protein seemed to be localized in mitochondria of the transgenic tobacco plants. Freezing-tolerance tests at -1 - -4 degrees C showed that the degree of electrolyte leakage was significantly lower in the plants with pBE2113/hiC6 than in the control plants. A leaf browning observation also showed that high accumulation of HIC6 significantly suppressed injury caused by freezing to the transgenic tobacco at -3 degrees C.
{"title":"Improvement of freezing tolerance in transgenic tobacco leaves by expressing the hiC6 gene.","authors":"K Honjoh, H Shimizu, N Nagaishi, H Matsumoto, K Suga, T Miyamoto, M Iio, S Hatano","doi":"10.1271/bbb.65.1796","DOIUrl":"10.1271/bbb.65.1796","url":null,"abstract":"<p><p>A cryoprotective protein, HIC6, was expressed transgenically in tobacco, a cold-sensitive plant, and the localization of the protein within the cell as well as freezing tolerance of the transgenic tobacco was investigated. For constitutive expression of HIC6 in tobacco, its corresponding gene was subcloned into pBI121. Through the transformation with pBI121/hiC6, fifteen transgenic tobacco lines were acquired, out of which twelve lines expressed the HIC6 protein. None of the transgenic tobacco lines, however, showed significant differences in freezing tolerance from the control plants (wild-type and transformed with pBI121) at -1, -3, and -4 degrees C, with the exception that their freezing temperature was -2 degrees C. In order to increase the accumulation level of HIC6, pBE2113 with a stronger promoter was used. Eight lines expressed the protein out of thirteen lines transformed with pBE2113/hiC6. The accumulation levels of the protein were clearly higher in the tobacco plants transformed with pBE2113/hiC6 than in those with pBI121/hiC6. The HIC6 protein seemed to be localized in mitochondria of the transgenic tobacco plants. Freezing-tolerance tests at -1 - -4 degrees C showed that the degree of electrolyte leakage was significantly lower in the plants with pBE2113/hiC6 than in the control plants. A leaf browning observation also showed that high accumulation of HIC6 significantly suppressed injury caused by freezing to the transgenic tobacco at -3 degrees C.</p>","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"98 1","pages":"1796-804"},"PeriodicalIF":1.6,"publicationDate":"2001-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1271/bbb.65.1796","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82226924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The Effects of Positive Mood on Memory.","authors":"Angela Y. Lee, B. Sternthal","doi":"10.1086/321943","DOIUrl":"https://doi.org/10.1086/321943","url":null,"abstract":"","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"1999-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60027918","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A polyclonal antibody directed against antigens on the surface of the germinated conidia of Erysiphe graminis f.sp. hordei E. M. Marchal was used to determine the presence and location of these antigens in host (barley) tissues from 4 to 96 h after inoculation. These studies were carried out using protein A-gold immunolabeling followed by quantitative analysis of labeling density in the nuclei, chloroplasts, vacuoles, and walls of the host cell. Four hours after inoculation the level of labeling detected in mesophyll cells of infected tissues (which are not penetrated by the fungus) was similar to that found in control healthy tissues. However, at 24 h and especially at 96 h after inoculation, the level of labeling in infected tissues was significantly higher than in the healthy tissues. This increase in labeling in infected tissues may be a result of synthesis of co-antigens by the plant as a response to infection, or it may indicate that fungal antigens enter the mesophyll cells very early in the infection process (4-24 h) around the time that penetration of the epidermal cell by the infection peg occurs.
一种针对禾本科erysiphhe graminis f.sp萌发分生孢子表面抗原的多克隆抗体。用hordei E. M. Marchal测定接种后4 ~ 96 h这些抗原在寄主(大麦)组织中的存在和位置。这些研究采用蛋白a -金免疫标记,然后定量分析宿主细胞细胞核、叶绿体、液泡和细胞壁中的标记密度。接种4小时后,在感染组织(未被真菌渗透)的叶肉细胞中检测到的标记水平与对照健康组织中的标记水平相似。然而,在接种后24 h,特别是96 h,感染组织中的标记水平明显高于健康组织。感染组织中标记的增加可能是植物对感染的反应合成共抗原的结果,也可能表明真菌抗原在感染过程的早期(4-24小时)进入叶肉细胞,大约在感染钉穿透表皮细胞的时候。
{"title":"Detection of Antigens of Powdery Mildew, Erysiphe graminis f.sp. Hordei, in Susceptible Plant Host Cells, Shortly After Inoculation and During the Early Stages of Infection","authors":"C. van Roestel, R. Smith, W. Mckeen, A. W. Day","doi":"10.1086/337907","DOIUrl":"https://doi.org/10.1086/337907","url":null,"abstract":"A polyclonal antibody directed against antigens on the surface of the germinated conidia of Erysiphe graminis f.sp. hordei E. M. Marchal was used to determine the presence and location of these antigens in host (barley) tissues from 4 to 96 h after inoculation. These studies were carried out using protein A-gold immunolabeling followed by quantitative analysis of labeling density in the nuclei, chloroplasts, vacuoles, and walls of the host cell. Four hours after inoculation the level of labeling detected in mesophyll cells of infected tissues (which are not penetrated by the fungus) was similar to that found in control healthy tissues. However, at 24 h and especially at 96 h after inoculation, the level of labeling in infected tissues was significantly higher than in the healthy tissues. This increase in labeling in infected tissues may be a result of synthesis of co-antigens by the plant as a response to infection, or it may indicate that fungal antigens enter the mesophyll cells very early in the infection process (4-24 h) around the time that penetration of the epidermal cell by the infection peg occurs.","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"152 1","pages":"460 - 467"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60238747","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The timing and morphological characteristics of the early stages in the establishment of Phoradendron macrophyllum (Viscaceae) on Salix laevigata were observed and quantified using clonal host material in greenhouse conditions. Observed stages were seed germination; holdfast formation; renewed greening of mistletoe tissue; swelling of the underlying host branch; aerial shoot formation; and development of the endophytic system. Aerial shoot formation was influenced by local moisture availability, but other stages in establishment were independent of water or nutrient sprays. When seeds of P. macrophyllum were placed on cuttings of Eucalyptus (a host susceptible to certain loranthaceous mistletoes, but not susceptible to Phoradendron), seed germination and hypocotyl swelling took place, but no further stages in holdfast formation occurred. A corky layer, or wound periderm, formed locally beneath the mistletoe seeds. When viscin alone from Phoradendron seeds was placed on Eucalyptus stems, wound periderm formation was also triggered.
{"title":"Establishment of the Mistletoe Phoradendron macrophyllum: Phenology of Early Stages and Host Compatibility Studies","authors":"J. Lichter, A. Berry","doi":"10.1086/337908","DOIUrl":"https://doi.org/10.1086/337908","url":null,"abstract":"The timing and morphological characteristics of the early stages in the establishment of Phoradendron macrophyllum (Viscaceae) on Salix laevigata were observed and quantified using clonal host material in greenhouse conditions. Observed stages were seed germination; holdfast formation; renewed greening of mistletoe tissue; swelling of the underlying host branch; aerial shoot formation; and development of the endophytic system. Aerial shoot formation was influenced by local moisture availability, but other stages in establishment were independent of water or nutrient sprays. When seeds of P. macrophyllum were placed on cuttings of Eucalyptus (a host susceptible to certain loranthaceous mistletoes, but not susceptible to Phoradendron), seed germination and hypocotyl swelling took place, but no further stages in holdfast formation occurred. A corky layer, or wound periderm, formed locally beneath the mistletoe seeds. When viscin alone from Phoradendron seeds was placed on Eucalyptus stems, wound periderm formation was also triggered.","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"152 1","pages":"468 - 475"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1086/337908","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60238757","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1991-12-01DOI: 10.1086/botanicalgazette.152.4.2995255
H. E. M. Stry, J. Waid
PhitM;n | The l tamics f decnapbic Pattq ning in Seied Plint S becies JON4 lllAN D. SU1 R j New ii W paper "A tefr shihg nd v approach . Thistook has brigh togethek plant ecolo migra ion, evolutiqn, a .d ghyQeography i: thoug at-stimulatir g wa 7."tBiocience "A rol nded 'hum4z' bio eorapuy, which shc the ca cnplexity of e su ect, theidistinctiven of es h migratiol 1 patt >rn, andflwhich as move I much of i he un: eal FbstrAction." A -Jou >1 Biogeogra $13.9c paper, 29Qpages j
{"title":"Back Matter","authors":"H. E. M. Stry, J. Waid","doi":"10.1086/botanicalgazette.152.4.2995255","DOIUrl":"https://doi.org/10.1086/botanicalgazette.152.4.2995255","url":null,"abstract":"PhitM;n | The l tamics f decnapbic Pattq ning in Seied Plint S becies JON4 lllAN D. SU1 R j New ii W paper \"A tefr shihg nd v approach . Thistook has brigh togethek plant ecolo migra ion, evolutiqn, a .d ghyQeography i: thoug at-stimulatir g wa 7.\"tBiocience \"A rol nded 'hum4z' bio eorapuy, which shc the ca cnplexity of e su ect, theidistinctiven of es h migratiol 1 patt >rn, andflwhich as move I much of i he un: eal FbstrAction.\" A -Jou >1 Biogeogra $13.9c paper, 29Qpages j","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"152 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1086/botanicalgazette.152.4.2995255","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60890600","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Hydnobolites cerebriformis is a widespread species of hypogeous ascomycetes found in both the United States and Europe. The ascomata are from 0.5 to 3.0 cm in diameter, with a thin cortical region surrounding clusters of globose to saccate asci arranged near veins within the medullary region. Because hymenial chambers were believed to lead to the surface of the ascomata, the genus was until recent years placed among Tuberaceae. The size, shape, and arrangement of asci and the pigmentation of ascospores, however, have led recent workers to place Hydnobolites in the Terfeziaceae. Cytological and ultrastructural features of asci, septa, and spore wall ontogeny in H. cerebriformis reveal a number of characters that link Hydnobolites to the traditional epigeous Pezizaceae. These include the presence of electron-dense, biconvex bands in septal pores of asci, dextrinoid and weak bluing reaction of asci in iodine, and a type of spore wall deposition similar to members of Pezizaceae.
{"title":"Ultrastructural Evidence for a Phylogenetic Linkage of the Truffle Genus Hydnobolites to the Pezizaceae (Pezizales, Ascomycetes)","authors":"J. Kimbrough, J. Gibson","doi":"10.1086/337902","DOIUrl":"https://doi.org/10.1086/337902","url":null,"abstract":"Hydnobolites cerebriformis is a widespread species of hypogeous ascomycetes found in both the United States and Europe. The ascomata are from 0.5 to 3.0 cm in diameter, with a thin cortical region surrounding clusters of globose to saccate asci arranged near veins within the medullary region. Because hymenial chambers were believed to lead to the surface of the ascomata, the genus was until recent years placed among Tuberaceae. The size, shape, and arrangement of asci and the pigmentation of ascospores, however, have led recent workers to place Hydnobolites in the Terfeziaceae. Cytological and ultrastructural features of asci, septa, and spore wall ontogeny in H. cerebriformis reveal a number of characters that link Hydnobolites to the traditional epigeous Pezizaceae. These include the presence of electron-dense, biconvex bands in septal pores of asci, dextrinoid and weak bluing reaction of asci in iodine, and a type of spore wall deposition similar to members of Pezizaceae.","PeriodicalId":9213,"journal":{"name":"Botanical Gazette","volume":"152 1","pages":"408 - 420"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60238227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}