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  • 1
    Publication Date: 2012-04-25
    Description:    Insights into the three-dimensional (3D) organization and function of intracellular structures at nanometer resolution, holds the key to our understanding of the molecular underpinnings of cellular structure−function. Besides this fundamental understanding of the cell at the molecular level, such insights hold great promise in identifying the disease processes by their altered molecular profiles, and help determine precise therapeutic treatments. To achieve this objective, previous studies have employed electron microscopy (EM) tomography with reasonable success. However, a major hurdle in the use of EM tomography is the tedious procedures involved in fixing, high-pressure freezing, staining, serial sectioning, imaging, and finally compiling the EM images to obtain a 3D profile of sub-cellular structures. In contrast, the resolution limit of EM tomography is several nanometers, as compared to just a single or even sub-nanometer using the atomic force microscope (AFM). Although AFM has been hugely successful in 3D imaging studies at nanometer resolution and in real time involving isolated live cellular and isolated organelles, it has had limited success in similar studies involving 3D imaging at nm resolution of intracellular structure–function in situ. In the current study, using both AFM and EM on aldehyde-fixed and semi-dry mouse pancreatic acinar cells, new insights on a number of intracellular structure–function relationships and interactions were achieved. Golgi complexes, some exhibiting vesicles in the process of budding were observed, and small vesicles were caught in the act of fusing with larger vesicles, possibly representing either secretory vesicle biogenesis or vesicle refilling following discharge, or both. These results demonstrate the power and scope of the combined engagement of EM and AFM imaging of fixed semi-dry cells, capable of providing a wealth of new information on cellular structure–function and interactions. Content Type Journal Article Category Original Paper Pages 1-16 DOI 10.1007/s00418-012-0948-x Authors Sunxi Wang, Department of Chemical Engineering and Materials Science, College of Engineering, Wayne State University, 5050 Anthony Wayne Drive, Detroit, MI 48202, USA Jin-Sook Lee, Department of Physiology, School of Medicine, Wayne State University, 540 E. Canfield, Detroit, MI 48201, USA Nicole Bishop, Department of Pathology, Microscopy Imaging Center, University of Vermont College of Medicine, Burlington, VT 05405, USA Aleksandar Jeremic, Department of Physiology, School of Medicine, Wayne State University, 540 E. Canfield, Detroit, MI 48201, USA Won Jin Cho, Department of Physiology, School of Medicine, Wayne State University, 540 E. Canfield, Detroit, MI 48201, USA Xuequn Chen, Department of Physiology, School of Medicine, Wayne State University, 540 E. Canfield, Detroit, MI 48201, USA Guangzhao Mao, Department of Chemical Engineering and Materials Science, College of Engineering, Wayne State University, 5050 Anthony Wayne Drive, Detroit, MI 48202, USA Douglas J. Taatjes, Department of Pathology, Microscopy Imaging Center, University of Vermont College of Medicine, Burlington, VT 05405, USA Bhanu P. Jena, Department of Chemical Engineering and Materials Science, College of Engineering, Wayne State University, 5050 Anthony Wayne Drive, Detroit, MI 48202, USA Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 2
    Publication Date: 2012-11-08
    Description:    Liprin α3 was reported for the first time using sperm proteomics. Present study reports its localization on sperm and immunochemical characterization. Liprin α3 is identified as a 133 kDa protein in testis and epididymal protein extracts. In testis, immunohistochemical localization was seen in pachytenes, diplotenes, round spermatids whereas it was localized in the epithelial cells and luminal sperm in all the three regions of epididymis. Protein was localized in acrosome of rat sperm, which was further confirmed by sequential treatment of sperm with hypertonic solution. In the spermatogenic cells the protein was found to be located in developing acrosome as evident by its co-localization with Golgi marker. Protein was found to be developmentally regulated. In silico analysis of Liprin α3 revealed presence of the estrogen responsive elements upstream to initiation site and its regulation by estrogen was experimentally validated using a tamoxifen treated rat model. Western blot analysis of epididymosomes showed the presence of Liprin α3, indicating its involvement in trafficking of vesicle. The protein expression was seen in both mouse and human sperm indicating conserved nature and a probable role in acrosome reaction. Content Type Journal Article Category Original Paper Pages 1-14 DOI 10.1007/s00418-012-1044-y Authors Chetanchandra S. Joshi, Department of Gamete Immunobiology, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012 India Amol R. Suryawanshi, Department of Gamete Immunobiology, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012 India Shagufta A. Khan, Department of Gamete Immunobiology, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012 India Nafisa H. Balasinor, Department of Neuroendocrinology, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012 India Vrinda V. Khole, Department of Gamete Immunobiology, National Institute for Research in Reproductive Health (ICMR), J. M. Street, Parel, Mumbai, 400012 India Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 3
    Publication Date: 2012-11-08
    Description:    Various cells types, including stem and progenitor cells, can exchange complex information via plasma membrane-derived vesicles, which can carry signals both in their limiting membrane and lumen. Astrocytes, traditionally regarded as mere supportive cells, play previously unrecognized functions in neuronal modulation and are capable of releasing signalling molecules of different functional significance. In the present study, we provide direct evidence that human fetal astrocytes in culture, expressing the same feature as immature and reactive astrocytes, release membrane vesicles larger than the microvesicles described up to now. We found that these large vesicles, ranging from 1–5 to 8 μm in diameter and expressing on their surface β 1-integrin proteins, contain mitochondria and lipid droplets together with ATP. We documented vesicle content with fluorescent-specific dyes and with the immunocytochemistry technique we confirmed that mitochondria and lipid droplets were co-localized in the same vesicle. Scanning electron microscopy and transmission electron microscopy confirmed that astrocytes shed from surface membrane vesicles of the same size as the ones detected by fluorescence microscopy. Our results report for the first time that cultured astrocytes, activated by repetitive stimulation of ATP released from neighboring cells, shed from their surface large membrane vesicles containing mitochondria and lipid droplets. Content Type Journal Article Category Original Paper Pages 1-11 DOI 10.1007/s00418-012-1045-x Authors Angela Maria Falchi, Department of Biomedical Sciences, University of Cagliari, Cittadella Universitaria Monserrato, 09042 Monserrato, CA, Italy Valeria Sogos, Department of Biomedical Sciences, University of Cagliari, Cittadella Universitaria Monserrato, 09042 Monserrato, CA, Italy Francesca Saba, Department of Biomedical Sciences, University of Cagliari, Cittadella Universitaria Monserrato, 09042 Monserrato, CA, Italy Monica Piras, Department of Biomedical Sciences, University of Cagliari, Cittadella Universitaria Monserrato, 09042 Monserrato, CA, Italy Terenzio Congiu, Department of Surgical and Morphological Sciences, University of Insubria, 21100 Varese, Italy Marco Piludu, Department of Biomedical Sciences, University of Cagliari, Cittadella Universitaria Monserrato, 09042 Monserrato, CA, Italy Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 4
    Publication Date: 2012-11-08
    Description:    The aim of this study was to examine the comparative localisations of fibrillin-1 and perlecan in the foetal human, wild-type C57BL/6 and HS-deficient hspg2 Δ 3−/ Δ 3− exon 3 null mouse intervertebral disc (IVD) using fluorescent laser scanning confocal microscopy. Fibrillin-1 fibrils were prominent components of the outer posterior and anterior annulus fibrosus (AF) of the foetal human IVD. Finer fibrillin-1 fibrils were evident in the inner AF where they displayed an arcade-type arrangement in the developing lamellae. Relatively short but distinct fibrillin-1 fibrils were evident in the central region of the IVD and presumptive cartilaginous endplate and defined the margins of the nuclear sheath in the developing nucleus pulposus (NP). Fibrillin-1 was also demonstrated in the AF of C57BL/6 wild-type mice but to a far lesser extent in the HS-deficient hspg2 Δ 3−/ Δ 3− exon 3 null mouse. This suggested that the HS chains of perlecan may have contributed to fibrillin-1 assembly or its deposition in the IVD. The cell–matrix interconnections provided by the fibrillin fibrils visualised in this study may facilitate communication between disc cells and their local biomechanical microenvironment in mechanosensory processes which regulate tissue homeostasis. The ability of fibrillin-1 to sequester TGF-β a well-known anabolic growth factor in the IVD also suggests potential roles in disc development and/or remodelling. Content Type Journal Article Category Original Paper Pages 1-11 DOI 10.1007/s00418-012-1041-1 Authors Anthony J. Hayes, Confocal Microscopy Unit, Cardiff School of Biosciences, Cardiff University, Cardiff, CF10 3US Wales, UK Susan M. Smith, Raymond Purves Bone and Joint Research Laboratories, Institute of Bone and Joint Research, The Kolling Institute of Medical Research, University of Sydney at The Royal North Shore Hospital, Level 10, Building B6, St. Leonards, NSW 2065, Australia James Melrose, Raymond Purves Bone and Joint Research Laboratories, Institute of Bone and Joint Research, The Kolling Institute of Medical Research, University of Sydney at The Royal North Shore Hospital, Level 10, Building B6, St. Leonards, NSW 2065, Australia Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 5
    Publication Date: 2012-09-25
    Description:    The extracellular matrix protein reelin controls radial migration and layer formation of cortical neurons, in part by modulation of cytoskeletal dynamics. A stabilizing effect of reelin on the actin cytoskeleton has been described recently. However, it is poorly understood how reelin modulates microtubule dynamics. Here, we provide evidence that reelin increases microtubule assembly. This effect is mediated, at least in part, by promoting microtubule plus end dynamics in processes of developing neurons. Thus, we treated primary neuronal cultures with nocodazole to disrupt microtubules. After nocodazole washout, we found microtubule reassembly to be accelerated in the presence of reelin. Moreover, we show that reelin treatment promoted the formation of microtubule plus end binding protein 3 (EB3) comets in developing dendrites, and that EB3 immunostaining in the developing wild-type neocortex is most intense in the reelin-rich marginal zone where leading processes of radially migrating neurons project to. This characteristic EB3 staining pattern was absent in reeler. Also reassembly of nocodazole-dispersed dendritic Golgi apparati, which are closely associated to microtubules, was accelerated by reelin treatment, though with a substantially slower time course when compared to microtubule reassembly. In support of our in vitro results, we found that the subcellular distribution of α-tubulin and acetylated tubulin in reeler cortical sections differed from wild-type and from mice lacking the very low density lipoprotein receptor (VLDLR), known to bind reelin. Taken together, our results suggest that reelin promotes microtubule assembly, at least in part, by increasing microtubule plus end dynamics. Content Type Journal Article Category Original Paper Pages 1-15 DOI 10.1007/s00418-012-1025-1 Authors Maurice Meseke, Institute of Neuroanatomy, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, Germany Ersin Cavus, Institute of Neuroanatomy, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, Germany Eckart Förster, Institute of Neuroanatomy, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, Germany Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 6
    Publication Date: 2012-09-25
    Description:    Isoform 1 of the sodium-vitamin C co-transporter (SVCT1) is expressed in the apical membrane of proximal tubule epithelial cells in adult human and mouse kidneys. This study is aimed at analyzing the expression and function of SVCTs during kidney development. RT-PCR and immunohistochemical analyses revealed that SVCT1 expression is increased progressively during postnatal kidney development. However, SVCT1 transcripts were barely detected, if not absent, in the embryonic kidney. Instead, the high-affinity transporter, isoform 2 (SVCT2), was strongly expressed in the developing kidney from E15; its expression decreased at postnatal stages. Immunohistochemical analyses showed a dynamic distribution of SVCT2 in epithelial cells during kidney development. In renal cortex tubular epithelial cells, intracellular distribution of SVCT2 was observed at E19 with distribution in the basolateral membrane at P1. In contrast, SVCT2 was localized to the apical and basolateral membranes between E17 and E19 in medullary kidney tubular cells but was distributed intracellularly at P1. In agreement with these findings, functional expression of SVCT2, but not SVCT1 was detected in human embryonic kidney-derived (HEK293) cells. In addition, kinetic analysis suggested that an ascorbate-dependent mechanism accounts for targeted SVCT2 expression in the developing kidney during medullary epithelial cell differentiation. However, during cortical tubular differentiation, SVCT1 was induced and localized to the apical membrane of tubular epithelial cells. SVCT2 showed a basolateral polarization only for the first days of postnatal life. These studies suggest that the uptake of vitamin C mediated by different SVCTs plays differential roles during the ontogeny of kidney tubular epithelial cells. Content Type Journal Article Category Original Paper Pages 1-15 DOI 10.1007/s00418-012-1027-z Authors Francisco Nualart, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Tamara Castro, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Marcela Low, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Juan Pablo Henríquez, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Karina Oyarce, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Pedro Cisternas, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Andrea García, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Alejandro J. Yáñez, Facultad de Ciencias Biológicas, Instituto de Bioquímica, Universidad Austral de Chile, Valdivia, Chile Romina Bertinat, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Viviana P. Montecinos, Departamento de Hematología-Oncología, Facultad de Medicina, Pontificia Universidad Católica de Chile, Santiago, Chile María Angeles García-Robles, Departamento de Biología Celular, Centro de Microscopía Avanzada CMA BIO-BIO, Universidad de Concepción, Concepción, Chile Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 7
    Publication Date: 2012-09-29
    Description:    Autophagy has been described as a cellular response to stressful stimuli like starvation. One of its primary functions is to recycle amino acids from degraded proteins for cellular survival under nutrient deprived conditions. Autophagy is characterized by double membrane cytosolic vesicles called autophagosomes and prolonged autophagy is known to result in autophagic (Type II) cell death. Beclin-1 is involved in the regulation of autophagy in mammalian cells. This study examined the potential impact of knockdown of Beclin-1 in an autophagic response in HT22 neurons challenged with amino acid starvation (AAS). AAS exposure induced light chain-3 (LC-3)-immunopositive and monodansylcadaverine (MDC) fluorescent dye-labeled autophagosome formation in cell bodies as early as 3 h post-AAS in wild type cells. Elevated levels of the autophagosome-targeting LC3-II were also observed following AAS. In addition, neuronal death induced by AAS in HT22-cells led to a moderate activation of caspase-3, a slight upregulation of AIF and did not alter the HtrA2 levels. Autophagy inhibition by a knockdown of Beclin-1 significantly reduced AAS-induced LC3-II increase, reduced accumulation of autophagosomes, and potentiated AAS-mediated neuronal death. Collectively, this study shows that the both apoptotic and autophagic machineries are inducible in cultured hippocampal HT22 neurons subjected to AAS. Our data further show that attenuation of autophagy by a knockdown of Beclin-1 enhanced neurons susceptibility to proapoptotic signals induced by AAS and underlines that autophagy is per se a protective than a deleterious mechanism. Content Type Journal Article Category Original Paper Pages 1-10 DOI 10.1007/s00418-012-1013-5 Authors M. Kim, Dr. Senckenbergische Anatomie, Institute of Cellular and Molecular Anatomy, Wolfgang Goethe-University, Anatomie III, Universitätsklinikum, Theodor-Stern-Kai 7, 60590 Frankfurt/Main, Germany J. Fekadu, Dr. Senckenbergische Anatomie, Institute of Cellular and Molecular Anatomy, Wolfgang Goethe-University, Anatomie III, Universitätsklinikum, Theodor-Stern-Kai 7, 60590 Frankfurt/Main, Germany E. Maronde, Dr. Senckenbergische Anatomie, Institute of Cellular and Molecular Anatomy, Wolfgang Goethe-University, Anatomie III, Universitätsklinikum, Theodor-Stern-Kai 7, 60590 Frankfurt/Main, Germany A. Rami, Dr. Senckenbergische Anatomie, Institute of Cellular and Molecular Anatomy, Wolfgang Goethe-University, Anatomie III, Universitätsklinikum, Theodor-Stern-Kai 7, 60590 Frankfurt/Main, Germany Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 8
    Publication Date: 2012-10-01
    Description:    Odontogenesis consists of a series of consecutive tooth morphogenesis stages, in which apoptosis is involved to eliminate the unnecessary cells. Autophagy, a lysosome or endosome-mediated self-degradation process, is indicated to participate in embryogenesis and tissue morphogenesis associated with apoptosis. This study hypothesized that autophagy may be involved and associated with apoptosis in odontogenesis. The transcripts of autophagy-related genes (Atg5, Atg7, and Atg12) were positively detected in tooth germs at embryonic day (E) 14.5 and postnatal day (P) 5.5 by quantitative real-time PCR. The protein expression of Atg5–Atg12 conjugate and lipidation of LC3 (microtubule-associated protein 1 light chain 3, autophagic marker) were revealed in the developing tooth germs by western blot. Meanwhile, LC3 was immunolocalized in the enamel organ and dental papilla at embryonic stages (E13.5–E18.5), especially stage E14.5 cervical loop and the PEK that facing the mesenchyme. At postnatal stages (P1.5–P15.5), besides the dental epithelium cells, LC3 was detected in the differentiating and differentiated odontoblasts, dental follicle cells, and Hertwig’s epithelium root sheath cells. Moreover, double-immunofluorescence analysis revealed the partial colocalization of LC3 and TUNEL signal in the E14.5 PEK that facing the mesenchyme, the E16.5 stratum intermedium and outer enamel epithelium, the P5.5 stratum intermedium and stellate reticulum. Nevertheless, LC3 was also found in non-apoptotic cells. Furthermore, the transmission electron microscopic images revealed the presence of autophagy, as well as the partial colocalization of autophagic vacuoles and apoptotic nuclei during tooth development. Our findings imply the developmental appearance of autophagy and its partial colocalization with apoptosis during odontogenesis. Content Type Journal Article Category Original Paper Pages 1-10 DOI 10.1007/s00418-012-1016-2 Authors Jing-wen Yang, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Ling-xin Zhu, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Guo-hua Yuan, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Yang-xi Chen, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Li Zhang, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Lu Zhang, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Zhi Chen, The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei-MOST), Key Laboratory of Oral Biomedicine, Ministry of Education, School and Hospital of Stomatology, Wuhan University, 237 Luoyu Road, Wuhan, 430079 China Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 9
    Publication Date: 2012-10-01
    Description:    Galnt3 belongs to the GalNAc transferase gene family involved in the initiation of mucin-type O-glycosylation. Male Galnt3 -deficient ( Galnt3 −/− ) mice were infertile, as previously reported by Ichikawa et al. ( 2009 ). To investigate the involvement of Galnt3 in spermatogenesis, we examined the differentiation of germ cells in Galnt3 −/− mice. Galnt3 mRNA was most highly expressed in testis, and Galnt3 protein was localized in the cis-medial parts of the Golgi stacks of spermatocytes and spermatids in the seminiferous tubules. Spermatozoa in Galnt3 −/− mice were rare and immotile, and most of them had deformed round heads. They exhibited abnormal acrosome and disturbed mitochondria arrangement in the flagella. At the cap phase, proacrosomal vesicles of various sizes, which had not coalesced to form a single acrosomal vesicle, were attached to the nucleus in Galnt3 −/− mice. TUNEL-positive cells were increased in the seminiferous tubules. The binding of VVA lectin, which recognizes the Tn antigen (GalNAc- O -Ser/Thr), in the acrosomal regions of spermatids and spermatozoa in Galnt3 −/− mice was drastically reduced. Equatorin is a N , O -sialoglycoprotein localized in the acrosomal membrane and is suggested to be involved in sperm–egg interaction. Immunohistochemical and Western blot analyses showed a drastic reduction in the reactivity with MN9 antibody, which recognizes the O -glycosylated moiety of equatorin and inhibits sperm–egg interaction. These findings indicate that deficiency of Galnt3 results in a severe reduction of mucin-type O -glycans in spermatids and causes impaired acrosome formation, leading to oligoasthenoteratozoospermia, and suggest that Galnt3 may also be involved in the process of fertilization through the O-glycosylation of equatorin. Content Type Journal Article Category Original Paper Pages 1-16 DOI 10.1007/s00418-012-1031-3 Authors Toshihiro Miyazaki, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Masako Mori, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Carolina A. Yoshida, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Chizuru Ito, Department of Anatomy and Developmental Biology, Chiba University Graduate School of Medicine, Chiba, Japan Kenji Yamatoya, Department of Anatomy and Developmental Biology, Chiba University Graduate School of Medicine, Chiba, Japan Takeshi Moriishi, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Yosuke Kawai, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Hisato Komori, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Tetsuya Kawane, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Shin-ichi Izumi, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Kiyotaka Toshimori, Department of Anatomy and Developmental Biology, Chiba University Graduate School of Medicine, Chiba, Japan Toshihisa Komori, Department of Cell Biology, Unit of Basic Medical Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki, 852-8588 Japan Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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  • 10
    Publication Date: 2012-10-13
    Description:    While tryptophan hydroxylase-2 ( Tph2 ) null mutant ( Tph2 −/− ) mice are completely deficient in brain serotonin (5-HT) synthesis, the formation of serotonergic neurons and pathfinding of their projections are not impaired. However, 5-HT deficiency, during development and in the adult, might affect morphological and functional parameters of other neural systems. To assess the influence of 5-HT deficiency on γ-amino butyric acid (GABA) systems, we carried out measurements of GABA concentrations in limbic brain regions of adult male wildtype ( wt ), heterozygous ( Tph2 +/− ) and Tph2 −/− mice. In addition, unbiased stereological estimation of GABAergic interneuron numbers and density was performed in subregions of amygdala and hippocampus. Amygdala and prefrontal cortex displayed significantly increased and decreased GABA concentrations, respectively, exclusively in Tph2 +/− mice while no changes were detected between Tph2 −/− and wt mice. In contrast, in the hippocampus, increased GABA concentrations were found in Tph2 −/− mice. While total cell density in the anterior basolateral amygdala did not differ between genotypes, the number and density of the GABAergic interneurons were significantly decreased in Tph2 −/− mice, with the group of parvalbumin (PV)-immunoreactive (ir) interneurons contributing somewhat less to the decrease than that of non-PV-ir GABAergic interneurons. Major morphological changes were also absent in the dorsal hippocampus, and only a trend toward reduced density of PV-ir cells was observed in the CA3 region of Tph2 −/− mice. Our findings are the first to document that life-long reduction or complete lack of brain 5-HT transmission causes differential changes of GABA systems in limbic regions which are key players in emotional learning and memory processes. The changes likely reflect a combination of developmental alterations and functional adaptations of emotion circuits to balance the lack of 5-HT, and may underlie altered emotional behavior in 5-HT-deficient mice. Taken together, our findings provide further insight into the mechanisms how life-long 5-HT deficiency impacts the pathogenesis of anxiety- and fear-related disorders. Content Type Journal Article Category Original Paper Pages 1-15 DOI 10.1007/s00418-012-1029-x Authors Jonas Waider, Laboratory of Translational Neuroscience, Division of Molecular Psychiatry, Department of Psychiatry, Psychosomatics, and Psychotherapy, University of Wuerzburg, Fuechsleinstrasse 15, 97080 Wuerzburg, Germany Florian Proft, Laboratory of Translational Neuroscience, Division of Molecular Psychiatry, Department of Psychiatry, Psychosomatics, and Psychotherapy, University of Wuerzburg, Fuechsleinstrasse 15, 97080 Wuerzburg, Germany Georg Langlhofer, Laboratory of Translational Neuroscience, Division of Molecular Psychiatry, Department of Psychiatry, Psychosomatics, and Psychotherapy, University of Wuerzburg, Fuechsleinstrasse 15, 97080 Wuerzburg, Germany Esther Asan, Institute of Anatomy and Cell Biology, University of Wuerzburg, Koellikerstr. 6, 97070 Wuerzburg, Germany Klaus-Peter Lesch, Laboratory of Translational Neuroscience, Division of Molecular Psychiatry, Department of Psychiatry, Psychosomatics, and Psychotherapy, University of Wuerzburg, Fuechsleinstrasse 15, 97080 Wuerzburg, Germany Lise Gutknecht, Laboratory of Translational Neuroscience, Division of Molecular Psychiatry, Department of Psychiatry, Psychosomatics, and Psychotherapy, University of Wuerzburg, Fuechsleinstrasse 15, 97080 Wuerzburg, Germany Journal Histochemistry and Cell Biology Online ISSN 1432-119X Print ISSN 0948-6143
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