Archives of histology and cytology最新文献

{"title":"Endothelin A receptor-like immunoreactivity on the basal infoldings of rat renal tubules and collecting ducts.","authors":"Toshiharu Yamamoto, H. Suzuki, Yukari Kubo, A. Matsumoto, H. Uemura","doi":"10.1679/AOHC.71.77","DOIUrl":"https://doi.org/10.1679/AOHC.71.77","url":null,"abstract":"We investigated the distribution of endothelin A (ET(A)) receptor-like immunoreactivity in the rat kidney using affinity-purified antibodies against amino acid residues 403-417 of the rat ET(A) receptor modified by the multiple antigen peptide complex system. Western blot analysis using the affinity-purified anti-ET(A) antibody detected bands of approximately 47.3 and 64.5 kDa in the rat kidney. By light microscopy, ET(A) receptor-like immunoreactivity was seen in the basal side of the renal tubules and collecting ducts. The most intense immunoreactivity was present in the distal renal tubules and inner medullary collecting ducts. In addition to the basal infoldings, immunoreactive puncta were scattered in the epithelial cells of the renal tubules and collecting ducts. Specimens prepared using the pre-embedding method were examined by electron microscopy, and some immunopositive signals were seen on the basal infodings of the renal tubules and collecting ducts. The lengths of immunopositive cytoplasmic membrane were far longer in the distal tubules and inner medullary collecting ducts than in the proximal tubules and outer medullary collecting ducts. Immunopositive signals were also sometimes observed in the thick portion of Henle's loop, but never in the thin portion. We have not previously detected immunopositive signals on the renal vascular systems with the antibody used here. These results suggest that endothelin acts on the basal infoldings through the ET(A) receptor, particularly in the distal tubules and inner medullary collecting ducts, although involvement of the ET(B) receptor cannot be excluded.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 2 1","pages":"77-87"},"PeriodicalIF":0.0,"publicationDate":"2008-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.71.77","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484372","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 serine racemase mRNA is expressed in both neurons and glial cells of the rat retina.","authors":"Naoko Takayasu, M. Yoshikawa, Mariko Watanabe, H. Tsukamoto, Toshiyasu Suzuki, Hiroyuki Kobayashi, S. Noda","doi":"10.1679/AOHC.71.123","DOIUrl":"https://doi.org/10.1679/AOHC.71.123","url":null,"abstract":"D-Serine, an endogenous and obligatory coagonist for the glycine site of the N-methyl-D-aspartate receptor in mammals, is synthesized from L-serine by serine racemase. Serine racemase and D-serine have long been believed to occur predominantly in astrocytes, according to immunohistochemical studies. Recent studies have demonstrated, however, that both the mRNA and protein levels of serine racemase are considerably higher in neurons than in astrocytes in primary cultures of the rat brain and that the mRNA level of serine racemase predominates in neurons of the adult rat brain. Here we report the application of in situ hybridization based on tyramide signal amplification for the detection of serine racemase mRNA in sections of the adult rat retina and optic nerve head. The localization of serine racemase mRNA could be demonstrated in ganglion cells, amacrine cells, bipolar cells, horizontal cells, and Müller cells of the retina as well as in the astrocytes of the optic nerve head and the lamina cribrosa. This is the first study to demonstrate the exact localization of serine racemase mRNA at the cellular or tissue level in the retina and the optic nerve head. These results suggest that both the neuron- and glia-derived D-serine could modulate neurotransmission via the glycine site of the N-methyl-D-aspartate receptors in the retina.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"26 1","pages":"123-9"},"PeriodicalIF":0.0,"publicationDate":"2008-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.71.123","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484258","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":"Inhibition of the terminal differentiation of odontoblasts and their transdifferentiation into osteoblasts in Runx2 transgenic mice.","authors":"T. Miyazaki, N. Kanatani, S. Rokutanda, C. Yoshida, S. Toyosawa, Reiko M. Nakamura, S. Takada, T. Komori","doi":"10.1679/AOHC.71.131","DOIUrl":"https://doi.org/10.1679/AOHC.71.131","url":null,"abstract":"Runx2 is an essential transcription factor for bone and tooth development whose function in odontoblast differentiation remains to be clarified. To pursue this issue, we examined tooth development in Runx2 transgenic mice under the control of Col1a1 promoter (Tg(Col1a1-Runx2) mice). Endogenous Runx2 protein was detected in the nuclei of preodontoblasts, immature odontoblasts, mesenchymal cells in the dental sac, and osteoblasts, while transgene expression was detected in odontoblasts and osteoblasts. Odontoblasts in Tg(Col1a1-Runx2) mice lost their columnar shape and dentin was deposited around the odontoblasts, which were cuboid or flat in shape. The dentin in Tg(Col1a1-Runx2) mice was thin and possessed lacunae that contained odontoblasts and bone canaliculi-like structures, while predentin and dentinal tubules were absent. We examined the expression of dentin matrix protein genes, Col1a1 and dentin sialophosphoprotein (DSPP), by in situ hybridization, and dentin matrix proteins, osteocalcin, osteopontin, and dentin matrix protein 1 (DMP1) as well as an intermediate filament, nestin, by immunohistochemistry to characterize odontoblasts in Tg(Col1a1-Runx2) mice. Results showed Col1a1 expression was down-regulated, DSPP expression was lost, and nestin expression was severely decreased in the odontoblasts of Tg(Col1a1-Runx2) mice. Further, the expressions of osteocalcin, osteopontin, and DMP1 were up-regulated in odontoblasts, although the up-regulation of osteocalcin expression was transient. These findings indicate that Runx2 inhibits the terminal differentiation of odontoblasts, and that Runx2 induces transdifferentiation of odontoblasts into osteoblasts forming a bone structure. Thus, Runx2 expression has to be down-regulated during odontoblast differentiation to acquire full odontoblast differentiation for dentinogenesis.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 2 1","pages":"131-46"},"PeriodicalIF":0.0,"publicationDate":"2008-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.71.131","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484317","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 modulation of collagen fibril assembly and its structure by decorin: an electron microscopic study.","authors":"Shunsuke Iwasaki,&nbsp;Yoshinao Hosaka,&nbsp;Tomohito Iwasaki,&nbsp;Katsuhiro Yamamoto,&nbsp;Aya Nagayasu,&nbsp;Hiromi Ueda,&nbsp;Yasuo Kokai,&nbsp;Kazushige Takehana","doi":"10.1679/aohc.71.37","DOIUrl":"https://doi.org/10.1679/aohc.71.37","url":null,"abstract":"<p><p>The present study was carried out to determine the effect of decorin in the process of collagen assembly. Collagen fibrils were obtained in vitro by aggregation from commercialized acid-soluble type I collagen with the addition of different concentrations of decorin (0-25 microg/ml). All specimens were observed by scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The distribution of collagen fibril diameters was also analyzed by TEM. In samples without or with low concentrations of decorin, highly porous collagen fiber networks were formed. On the other hand, dense networks were observed in samples treated with high concentrations of decorin. The influence of decorin secreted by cells on collagen fibrils was observed by SEM, and the fiber network elasticity was measured using a rheometer. SEM images showed that collagen fiber networks without fibroblasts were much looser than those cultured with normal fibroblasts. The networks cultured with the fibroblasts were composed of straight fibers with large diameters. On the other hand, collagen fiber networks cultured with siRNA-decorin-transfected (siDT) fibroblasts had loose, meandering fibers with small diameters. The elasticity of collagen fiber networks cultured with untransfected fibroblasts showed no significant difference over the 7-day incubation period. However, significantly lower elastic values were obtained for collagen fiber networks treated with siDT cells on days 3 and 7. In addition, after treatment with 5.0 or 25 microg/ml decorin, the l collagen fiber networks cultured with siDT cells exhibited an altered structure that showed a dense structure similar to that of the fiber networks cultured with untransfected fibroblasts. In conclusion, this in vitro study showed that decorin is a regulatory and architecturally small leucine-rich repeat proteoglycan in the process of collagen fibril assembly.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 1","pages":"37-44"},"PeriodicalIF":0.0,"publicationDate":"2008-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.71.37","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27530459","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":"Appearance of LFA-1 in the initial stage of synaptogenesis of developing hippocampal neurons.","authors":"Yoshihiro Wakabayashi,&nbsp;Atsushi Tsujimura,&nbsp;Ken-Ichi Matsuda,&nbsp;Norio Yoshimura,&nbsp;Mitsuhiro Kawata","doi":"10.1679/aohc.71.23","DOIUrl":"https://doi.org/10.1679/aohc.71.23","url":null,"abstract":"<p><p>In the present study, we found that leucocyte function-associated antigen-1 (LFA-1), and integrin (heterodimer complex of CD11a and CD18), which are abundant in immunological synapse, were expressed in developing hippocampal neurons. The expression of LFA-1 in hippocampal neurons was in the period of synaptogenesis, and synaptogenesis was inhibited by the blocking antibodies of anti-CD11a or anti-CD18 in vitro. Since it is known that LFA-1 has an important role in the immunological response, especially in immunological synapse, LFA-1 is considered to have an important role in neuronal synapse and is highly involved in synaptogenesis in the early developmental stage in vitro. In vivo, we also confirmed that CD18 was expressed in hippocampus in the early developmental stage. Telencephalin, which is a candidate for postsynaptic elements to contact LFA-1, was precisely opposed to CD18-positive structures in presynaptic elements, and telencephalin was considered to be involved in synaptogenesis. The present study showed that 17beta-estradiol of steroid hormones, which are well known to have various effects on hippocampal neurons, has a significant influence on the presynaptic expression of CD18 in synaptogenesis and inhibited synaptogenesis in the early developmental stage in vitro. These results suggest that LFA-1 plays some mechanisms in synaptic contacts and synaptogenesis of hippocampal neurons.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 1","pages":"23-36"},"PeriodicalIF":0.0,"publicationDate":"2008-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.71.23","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27530553","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":"Organization and developmental aspects of lymphatic vessels.","authors":"Osamu Ohtani,&nbsp;Yuko Ohtani","doi":"10.1679/aohc.71.1","DOIUrl":"https://doi.org/10.1679/aohc.71.1","url":null,"abstract":"<p><p>The lymphatic system plays important roles in maintaining tissue fluid homeostasis, immune surveillance of the body, and the taking up dietary fat and fat-soluble vitamins A, D, E and K. The lymphatic system is involved in many pathological conditions, including lymphedema, inflammatory diseases, and tumor dissemination. A clear understanding of the organization of the lymphatic vessels in normal conditions would be critically important to develop new treatments for diseases involving the lymphatic vascular system. Therefore, the present paper reviews the organization of the lymphatic vascular system of a variety of organs, including the thyroid gland, lung and pleura, small intestine, cecum and colon in the rat, the diaphragm in the rat, monkey, and human, Peyer's patches and the appendix in the rabbit, and human tonsils. Methods employed include scanning electron microscopy of lymphatic corrosion casts and tissues with or without treatment of alkali maceration technique, transmission electron microscopy of intact tissues, confocal microscopy in conjunction with immunohistochemistry to some lymphatic-specific markers (i.e., LYVE-1 and VEGFR-3), and light microscopy in conjunction with enzyme-histochemistry to 5'-nucleotidase. Some developmental aspects of the lymphatic vessels and lymphedema are also discussed.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 1","pages":"1-22"},"PeriodicalIF":0.0,"publicationDate":"2008-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.71.1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27530551","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 skeletal muscle vascular supply closely correlates with the muscle fiber surface area in the rat.","authors":"Emiko Ichinose,&nbsp;Tomoyuki Kurose,&nbsp;Daisuke Daitoku,&nbsp;Seiichi Kawamata","doi":"10.1679/aohc.71.45","DOIUrl":"https://doi.org/10.1679/aohc.71.45","url":null,"abstract":"<p><p>The skeletal muscle capillary supply (capillarity) dynamically changes in response to muscle conditions such as growth, atrophy, and hypertrophy. The capillary number-to-fiber ratio is reported to correlate closely with the muscle fiber cross sectional area. However, little information is available regarding the capillarity of neonatal and very young skeletal muscles. In this study, the vascular endothelium was reliably stained with an anti-PECAM-1 antibody, and relationships between the capillarity and muscle fiber parameters were analyzed. For assessment of the capillarity, we used the capillary length-to-fiber ratio, due to the presence of transversely running vessels. In young and adult rats, the capillary length-to-fiber ratio was proportional to both the muscle fiber cross sectional area and muscle fiber radius. However, when these data were analyzed together with data from neonatal and very young rats, the capillary length-to-fiber ratio correlated more closely with the muscle fiber radius than the muscle fiber cross sectional area in the tibialis anterior muscle. The capillary number-to-fiber ratio demonstrated results very similar to the capillary length-to-fiber ratio. During muscle atrophy after denervation, the number of capillaries was decreased in a non-apoptotic manner as revealed by electron microscopy, maintaining the close relationship between the parameters described above. In conclusion, capillarity was closely correlated with the muscle fiber radius (which represents the perimeter) during growth and atrophy. This indicates that the capillarity is linked to the muscle fiber surface area (which is determined by perimeter and section thickness), in agreement with the essential role of the cell membrane in the transport of materials by simple diffusion or active transport.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 1","pages":"45-57"},"PeriodicalIF":0.0,"publicationDate":"2008-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.71.45","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27530460","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":"Cell-type specific occurrence of apoptosis in taste buds of the rat circumvallate papilla.","authors":"Katsura Ueda,&nbsp;Yasuo Ichimori,&nbsp;Hitomi Maruyama,&nbsp;Yayoi Murakami,&nbsp;Masae Fujii,&nbsp;Shiho Honma,&nbsp;Satoshi Wakisaka","doi":"10.1679/aohc.71.59","DOIUrl":"https://doi.org/10.1679/aohc.71.59","url":null,"abstract":"<p><p>The present study employed immunohistochemistry for single-stranded DNA (ssDNA) to detect apoptotic cells in taste buds of the rat circumvallate papilla. Double-labeling of ssDNA and markers for each cell type - phospholipase C beta2 (PLCbeta2) and alpha-gustducin for type II cells, neural cell adhesion molecule (NCAM) for type III cells, and Jacalin for type IV cells - was also performed to reveal which types of cells die by apoptosis. We detected approximately 16.8% and 14.0% of ssDNA-immunoreactive nuclei among PLCbeta2-immunoreactive and alpha-gustducinimmunoreactive cells, respectively, but rarely found ssDNA-immunoreactive cells among NCAM-immunoreactive or Jacalin-labeled cells, indicating that type II cells die by apoptosis. We also applied double labeling of ssDNA and human blood group antigen H (AbH) - which mostly labels type I cells as well as other cell types - and found that approximately 78% of ssDNA-immunoreactive cells were labeled with AbH, indicating that apoptosis also occurs in type I cells. The present results revealed that apoptosis occurs in both type I cells (dark cells) and type II cells (light cells), suggesting that there are two major cell lineages (dark cell and light cell lineages) for the differentiation of taste bud cells. In summury, type IV cells differentiate into dark and light cells and type III cells differentiate to type II cells within the light cell line.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"71 1","pages":"59-67"},"PeriodicalIF":0.0,"publicationDate":"2008-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.71.59","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27530461","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":"Soluble EMMPRIN (extra-cellular matrix metalloproteinase inducer) stimulates the migration of HEp-2 human laryngeal carcinoma cells, accompanied by increased MMP-2 production in fibroblasts.","authors":"Kyoshi Hanata,&nbsp;Noriko Yamaguchi,&nbsp;Kiwamu Yoshikawa,&nbsp;Yoshihiro Mezaki,&nbsp;Mitsutaka Miura,&nbsp;Shinsuke Suzuki,&nbsp;Haruki Senoo,&nbsp;Kazuo Ishikawa","doi":"10.1679/aohc.70.267","DOIUrl":"https://doi.org/10.1679/aohc.70.267","url":null,"abstract":"<p><p>The basement membrane functions as a barrier against the invasion of cancer cells. It is therefore important to investigate the mechanism of basement membrane degradation by matrix metalloproteinases (MMPs). Previously, cancer cells were long considered to be the major source of MMPs; however, current evidence indicates that most MMPs in cancer tissue are produced by stromal rather than cancer cells. A glycoprotein highly expressed on the cancer-cell membrane, EMMPRIN (extra-cellular matrix metalloproteinase inducer), exhibits the potential role of the MMP inductor in stromal cells. Depending on the cell type, EMMPRIN can stimulate the production of MMP-1, MMP-2, and MMP-3. We here report that soluble full-length EMMPRIN is liberated from HEp-2 human laryngeal epidermoid carcinoma cells, probably via microvesicle shedding. Soluble EMMPRIN stimulates human fibroblasts to produce MMP-2, after which the augmented migration of HEp-2 cells occurs, as observed in an invasion chamber assay with separately cultured fibroblasts. An anti-EMMPRIN function-blocking antibody reduced MMP-2 activity in the conditioned medium and inhibited the migration of HEp-2; obviously, EMMPRIN activity contributes to cancer-cell migration. We postulate that soluble EMMPRIN probably triggers the promotion of cancer invasion in vivo.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"70 5","pages":"267-77"},"PeriodicalIF":0.0,"publicationDate":"2007-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.70.267","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27399273","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":"Existence of subtypes of gustducin-immunoreactive cells in the vallate taste bud of guinea pigs.","authors":"Yasuhiro Ohkubo,&nbsp;Hiroyuki Yokosuka,&nbsp;Masahiko Kumakura,&nbsp;Sumio Yoshie","doi":"10.1679/aohc.70.291","DOIUrl":"https://doi.org/10.1679/aohc.70.291","url":null,"abstract":"<p><p>Vallate taste buds in the guinea-pig tongue were immunohistochemically investigated with regard to the colocalization of gustducin with calbindin-D28K (=spot 35 protein) and type III inositol triphosphate receptor (IP(3)R-3) in order to characterize gustducin-immunoreactive cells. Individual taste bud cells ranged from totally immunopositive to totally immunonegative for these three molecules. Among the immunoreactive cells, gustducin-immunoreactive cells were divided into two cell populations: one immunopositive and the other immunonegative for calbindin-D28K. Applying our previous data to the present results, the former cells should belong to Type III cells designated by electron microscopy. This finding provides new evidence regarding the taste bud types of cells expressing gustducin in the guinea pig.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"70 5","pages":"291-6"},"PeriodicalIF":0.0,"publicationDate":"2007-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/aohc.70.291","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27399819","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}