Shoko Kawashima, Sachiko Miyamoto-Kikuta, T. Ezaki, Takahiro Okamoto
{"title":"Immunohistochemical characterization of interstitial cells of Cajal (ICC) in the mouse intestine using whole mount preparations – with particular reference to their density, morphological features, and network patterns","authors":"Shoko Kawashima, Sachiko Miyamoto-Kikuta, T. Ezaki, Takahiro Okamoto","doi":"10.1679/aohc.80.1","DOIUrl":"https://doi.org/10.1679/aohc.80.1","url":null,"abstract":"","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2020-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44932099","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}
Kinue Shimizu, Megumi Sano, Aoi Kita, N. Sawai, A. Iizuka-Kogo, H. Kogo, T. Aoki, K. Takata, T. Matsuzaki
Aquaporin-2 (AQP2) is a water channel protein that is trafficked between intracellular vesicles and the plasma membrane of kidney collecting duct cells upon vasopressin stimulation. Vasopressin changes the phosphorylation states of the AQP2 C-terminal serines (Sers), Ser256, Ser261, Ser264, and Ser269, in rats and mice, which is thought to play a role in controlling trafficking. Here, we focused on Ser269. We developed a specific antibody to Ser269-phosphorylated AQP2. Using immunofluorescence microscopy, we examined its localization in the rat kidney following injection of vasopressin and a vasopressin type 2 receptor-specific antagonist (OPC-31260). Ser269-phosphorylated AQP2 was almost undetectable in the water-loaded rat kidney, but was detected intracellularly soon after vasopressin injection, and then highly accumulated on the apical membrane of connecting tubule and collecting duct principal cells. In addition to the apical membrane, Ser269phosphorylated AQP2 was also detected on the basolateral membrane of connecting tubule cells and inner medullary collecting duct principal cells. OPC-31260 injection following vasopressin stimulation caused internalization of AQP2, a pool of which was phosphorylated at Ser269. These results suggest that 1) AQP2 is phosphorylated at Ser269 intracellularly upon vasopressin stimulation and is rapidly trafficked to the plasma membrane, and 2) AQP2 can be internalized from the plasma membrane even if it remains phosphorylated at Ser269.
{"title":"Phosphorylation and dephosphorylation of aquaporin-2 at serine 269 and its subcellular distribution during vasopressin-induced exocytosis and subsequent endocytosis in the rat kidney","authors":"Kinue Shimizu, Megumi Sano, Aoi Kita, N. Sawai, A. Iizuka-Kogo, H. Kogo, T. Aoki, K. Takata, T. Matsuzaki","doi":"10.1679/AOHC.77.25","DOIUrl":"https://doi.org/10.1679/AOHC.77.25","url":null,"abstract":"Aquaporin-2 (AQP2) is a water channel protein that is trafficked between intracellular vesicles and the plasma membrane of kidney collecting duct cells upon vasopressin stimulation. Vasopressin changes the phosphorylation states of the AQP2 C-terminal serines (Sers), Ser256, Ser261, Ser264, and Ser269, in rats and mice, which is thought to play a role in controlling trafficking. Here, we focused on Ser269. We developed a specific antibody to Ser269-phosphorylated AQP2. Using immunofluorescence microscopy, we examined its localization in the rat kidney following injection of vasopressin and a vasopressin type 2 receptor-specific antagonist (OPC-31260). Ser269-phosphorylated AQP2 was almost undetectable in the water-loaded rat kidney, but was detected intracellularly soon after vasopressin injection, and then highly accumulated on the apical membrane of connecting tubule and collecting duct principal cells. In addition to the apical membrane, Ser269phosphorylated AQP2 was also detected on the basolateral membrane of connecting tubule cells and inner medullary collecting duct principal cells. OPC-31260 injection following vasopressin stimulation caused internalization of AQP2, a pool of which was phosphorylated at Ser269. These results suggest that 1) AQP2 is phosphorylated at Ser269 intracellularly upon vasopressin stimulation and is rapidly trafficked to the plasma membrane, and 2) AQP2 can be internalized from the plasma membrane even if it remains phosphorylated at Ser269.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"77 1","pages":"25-38"},"PeriodicalIF":0.0,"publicationDate":"2017-10-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45234387","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}
Summary. Neonatal hypoxic/ischemic (H/I) brain injury causes neurological impairment, including cognitive and motor dysfunction as well as seizures. Patterns of H/I injury-induced neuron death using rodent models are considered to be similar to the cases in human H/I encephalopathy. The participation of autophagy in neuron death has been a common feature in neonatal rodent models of H/I brain injury and human H/I encephalopathy when examined by immunochemical approaches for MAP1-LC3. This tendency has also been confirmed in neuronal tissue-specific Atg7 conditional knockout mice. However, while the current rat H/I model that is used for analyzing autophagy results in global damage to the ipsilateral hemisphere, it does not entirely reflect the neuropathological changes that appear in the neonatal mouse H/I model, in which the hippocampus is selectively damaged. The present study established a neonatal rat model of H/I injury with a milder ischemic insult, in which autophagy was involved in the hippocampal CA1 region after H/I injury when examined by electron microscopy, and by immunohistochemical and biochemical analyses of LC3.
{"title":"Induction of Autophagy in the Hippocampus after Hypoxic Ischemic Injury to Neonatal Rats","authors":"M. Koike, Ai Kawahara, M. Shibata, Y. Uchiyama","doi":"10.1679/AOHC.77.13","DOIUrl":"https://doi.org/10.1679/AOHC.77.13","url":null,"abstract":"Summary. Neonatal hypoxic/ischemic (H/I) brain injury causes neurological impairment, including cognitive and motor dysfunction as well as seizures. Patterns of H/I injury-induced neuron death using rodent models are considered to be similar to the cases in human H/I encephalopathy. The participation of autophagy in neuron death has been a common feature in neonatal rodent models of H/I brain injury and human H/I encephalopathy when examined by immunochemical approaches for MAP1-LC3. This tendency has also been confirmed in neuronal tissue-specific Atg7 conditional knockout mice. However, while the current rat H/I model that is used for analyzing autophagy results in global damage to the ipsilateral hemisphere, it does not entirely reflect the neuropathological changes that appear in the neonatal mouse H/I model, in which the hippocampus is selectively damaged. The present study established a neonatal rat model of H/I injury with a milder ischemic insult, in which autophagy was involved in the hippocampal CA1 region after H/I injury when examined by electron microscopy, and by immunohistochemical and biochemical analyses of LC3.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"77 1","pages":"13-23"},"PeriodicalIF":0.0,"publicationDate":"2017-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.77.13","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43845886","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}
In Xenopus laevis Daudin the anlage of the carotid labyrinth, a baroand chemoreceptor, appears in early premetamorphosis (NF stage 53) as a swelling of the third aortic arch at the point where the common carotid artery gives off the external carotid artery. A conspicuous accumulation of melanocytes preceeds the formation of the labyrinth maze which starts to grow at the end of metamorphic climax (NF stage 64) and continues so through juvenile age. In adult animals the carotid labyrinth displays a spherical to ovoid shape, has an average length of 1.4 mm, a width of about 0.8 mm and a height of about 0.4 mm. The maze vessels form by sprouting angiogenesis from the common carotid artery and the internal carotid artery. Scanning electron microscopy of vascular corrosion casts reveals that size, overall shape, surface morphology and vascular patterns of the carotid labyrinth vary greatly between individuals, whereby intussusceptive microvascular growth (= nonsprouting angiogenesis) and its facets model and contribute to the maturation of the labyrinth’s final vascular patterns.
{"title":"Vascular architecture of the carotid labyrinth in larval and adult Xenopus laevis – Histomorphology and scanning electron microscopy of vascular corrosion casts","authors":"C. Deutschmann, B. Minnich, A. Lametschwandtner","doi":"10.1679/AOHC.77.1","DOIUrl":"https://doi.org/10.1679/AOHC.77.1","url":null,"abstract":"In Xenopus laevis Daudin the anlage of the carotid labyrinth, a baroand chemoreceptor, appears in early premetamorphosis (NF stage 53) as a swelling of the third aortic arch at the point where the common carotid artery gives off the external carotid artery. A conspicuous accumulation of melanocytes preceeds the formation of the labyrinth maze which starts to grow at the end of metamorphic climax (NF stage 64) and continues so through juvenile age. In adult animals the carotid labyrinth displays a spherical to ovoid shape, has an average length of 1.4 mm, a width of about 0.8 mm and a height of about 0.4 mm. The maze vessels form by sprouting angiogenesis from the common carotid artery and the internal carotid artery. Scanning electron microscopy of vascular corrosion casts reveals that size, overall shape, surface morphology and vascular patterns of the carotid labyrinth vary greatly between individuals, whereby intussusceptive microvascular growth (= nonsprouting angiogenesis) and its facets model and contribute to the maturation of the labyrinth’s final vascular patterns.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"77 1","pages":"1-11"},"PeriodicalIF":0.0,"publicationDate":"2017-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43686896","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}
M. Zhou, R. Suzuki, A. Ishizawa, O. Tanaka, Y. Yasuoka, Yoshinori Kanatsu, K. Kawahara, H. Abe
ATP-sensitive K (KATP) channel subunits Kir6.1, Kir6.2, SUR1, SUR2A, and SUR2B in the rat pituitary gland were first investigated by RT-PCR assay and immunohistochemical staining. The results of RTPCR analysis showed that the rat pituitary gland expressed the five KATP channel subunits mentioned above. Immunohistochemical staining showed that these KATP channel subunits were widely localized in the anterior lobe, intermediate lobe, and posterior lobe at different intensities. Immunofluorescence double and triple staining showed that these KATP channel subunits colocalized with cells containing adrenocorticotropic hormone (ACTH) in the anterior lobe of the pituitary gland. Interestingly, neither Kir6.1 nor Kir6.2 colocalized with cells containing prolactin (PRL), follicular stimulating hormone (FSH), and growth hormone (GH). These results suggest that ACTH cells contain four types of KATP channels: Kir6.1/SUR2A, Kir6.2/SUR2A, Kir6.1/ SUR2B, and Kir6.2/SUR2B. KATP channels may play some important roles in ACTH cells in the pituitary gland. The different compositions of KATP channel subunits in corticotrophs but not in the PRL, FSH, and GH cells might be due to the different metabolic situations of these cells.
{"title":"Localization of ATP-sensitive K + channel subunits in rat pituitary gland","authors":"M. Zhou, R. Suzuki, A. Ishizawa, O. Tanaka, Y. Yasuoka, Yoshinori Kanatsu, K. Kawahara, H. Abe","doi":"10.1679/AOHC.76.53","DOIUrl":"https://doi.org/10.1679/AOHC.76.53","url":null,"abstract":"ATP-sensitive K (KATP) channel subunits Kir6.1, Kir6.2, SUR1, SUR2A, and SUR2B in the rat pituitary gland were first investigated by RT-PCR assay and immunohistochemical staining. The results of RTPCR analysis showed that the rat pituitary gland expressed the five KATP channel subunits mentioned above. Immunohistochemical staining showed that these KATP channel subunits were widely localized in the anterior lobe, intermediate lobe, and posterior lobe at different intensities. Immunofluorescence double and triple staining showed that these KATP channel subunits colocalized with cells containing adrenocorticotropic hormone (ACTH) in the anterior lobe of the pituitary gland. Interestingly, neither Kir6.1 nor Kir6.2 colocalized with cells containing prolactin (PRL), follicular stimulating hormone (FSH), and growth hormone (GH). These results suggest that ACTH cells contain four types of KATP channels: Kir6.1/SUR2A, Kir6.2/SUR2A, Kir6.1/ SUR2B, and Kir6.2/SUR2B. KATP channels may play some important roles in ACTH cells in the pituitary gland. The different compositions of KATP channel subunits in corticotrophs but not in the PRL, FSH, and GH cells might be due to the different metabolic situations of these cells.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"33 1","pages":"53-66"},"PeriodicalIF":0.0,"publicationDate":"2016-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.76.53","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484343","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 : 2016-05-21Epub Date: 2015-11-11DOI: 10.1016/S0140-6736(15)00755-2
Hellen Gelband, Rengaswamy Sankaranarayanan, Cindy L Gauvreau, Susan Horton, Benjamin O Anderson, Freddie Bray, James Cleary, Anna J Dare, Lynette Denny, Mary K Gospodarowicz, Sumit Gupta, Scott C Howard, David A Jaffray, Felicia Knaul, Carol Levin, Linda Rabeneck, Preetha Rajaraman, Terrence Sullivan, Edward L Trimble, Prabhat Jha
Investments in cancer control--prevention, detection, diagnosis, surgery, other treatment, and palliative care--are increasingly needed in low-income and particularly in middle-income countries, where most of the world's cancer deaths occur without treatment or palliation. To help countries expand locally appropriate services, Cancer (the third volume of nine in Disease Control Priorities, 3rd edition) developed an essential package of potentially cost-effective measures for countries to consider and adapt. Interventions included in the package are: prevention of tobacco-related cancer and virus-related liver and cervical cancers; diagnosis and treatment of early breast cancer, cervical cancer, and selected childhood cancers; and widespread availability of palliative care, including opioids. These interventions would cost an additional US$20 billion per year worldwide, constituting 3% of total public spending on health in low-income and middle-income countries. With implementation of an appropriately tailored package, most countries could substantially reduce suffering and premature death from cancer before 2030, with even greater improvements in later decades.
{"title":"Costs, affordability, and feasibility of an essential package of cancer control interventions in low-income and middle-income countries: key messages from Disease Control Priorities, 3rd edition.","authors":"Hellen Gelband, Rengaswamy Sankaranarayanan, Cindy L Gauvreau, Susan Horton, Benjamin O Anderson, Freddie Bray, James Cleary, Anna J Dare, Lynette Denny, Mary K Gospodarowicz, Sumit Gupta, Scott C Howard, David A Jaffray, Felicia Knaul, Carol Levin, Linda Rabeneck, Preetha Rajaraman, Terrence Sullivan, Edward L Trimble, Prabhat Jha","doi":"10.1016/S0140-6736(15)00755-2","DOIUrl":"10.1016/S0140-6736(15)00755-2","url":null,"abstract":"<p><p>Investments in cancer control--prevention, detection, diagnosis, surgery, other treatment, and palliative care--are increasingly needed in low-income and particularly in middle-income countries, where most of the world's cancer deaths occur without treatment or palliation. To help countries expand locally appropriate services, Cancer (the third volume of nine in Disease Control Priorities, 3rd edition) developed an essential package of potentially cost-effective measures for countries to consider and adapt. Interventions included in the package are: prevention of tobacco-related cancer and virus-related liver and cervical cancers; diagnosis and treatment of early breast cancer, cervical cancer, and selected childhood cancers; and widespread availability of palliative care, including opioids. These interventions would cost an additional US$20 billion per year worldwide, constituting 3% of total public spending on health in low-income and middle-income countries. With implementation of an appropriately tailored package, most countries could substantially reduce suffering and premature death from cancer before 2030, with even greater improvements in later decades.</p>","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"4 1","pages":"2133-2144"},"PeriodicalIF":0.0,"publicationDate":"2016-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89473884","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 microvascularization of the pancreas of larval and adult South African Clawed Toads Xenopus laevis, was studied by scanning electron microscopy of vascular corrosion casts and light microscopy of paraplast embedded Goldner-stained serial tissue sections. We showed that branches of left and right gastric artery, hepatic artery and anterior intestinal artery, namely anterior pancreatic, anterior middle pancreatic, posterior middle pancreatic and caudal pancreatic arteries supply and pancreatic veins drain the adult pancreas into hepatic portal vein, anterior and middle gastric vein, gastroduodenal vein, and anterior duodenal vein. In premetamorphosis the pancreas showed a dense but immature vascular bed with signs of ongoing sprouting and non-sprouting angiogenesis (=intussusceptive microvascular growth; IMG). During metamorphic climax the pancreas shrinked dramatically paralleled by vascular regression. The larval pancreas had an underdeveloped ductal system which in the course of pancreas remodeling during metamorphic climax developed into a complex ductal system. In adult Xenopus laevis the pancreas showed intralobular islets of Langerhans only and an insuloacinar portal vessel system as described sofar in reptiles, birds and mammals. Islets in Xenopus located superficially and within deeper regions and emitted both insulo-acinar portal vessels and insulo-venous efferent vessels. Intrainsular microvascular patterns found suggest that in Xenopus islets blood flows first to β-cells and subsequently to the other endocrine cells present in the endocrine pancreas.
{"title":"Microvascularization of the Pancreas in Larval and Adult Xenopus laevis – Histomorphology and Scanning Electron Microscopy of Vascular Corrosion Casts","authors":"J. Höpner, A. Lametschwandtner","doi":"10.1679/AOHC.76.35","DOIUrl":"https://doi.org/10.1679/AOHC.76.35","url":null,"abstract":"The microvascularization of the pancreas of larval and adult South African Clawed Toads Xenopus laevis, was studied by scanning electron microscopy of vascular corrosion casts and light microscopy of paraplast embedded Goldner-stained serial tissue sections. We showed that branches of left and right gastric artery, hepatic artery and anterior intestinal artery, namely anterior pancreatic, anterior middle pancreatic, posterior middle pancreatic and caudal pancreatic arteries supply and pancreatic veins drain the adult pancreas into hepatic portal vein, anterior and middle gastric vein, gastroduodenal vein, and anterior duodenal vein. In premetamorphosis the pancreas showed a dense but immature vascular bed with signs of ongoing sprouting and non-sprouting angiogenesis (=intussusceptive microvascular growth; IMG). During metamorphic climax the pancreas shrinked dramatically paralleled by vascular regression. The larval pancreas had an underdeveloped ductal system which in the course of pancreas remodeling during metamorphic climax developed into a complex ductal system. In adult Xenopus laevis the pancreas showed intralobular islets of Langerhans only and an insuloacinar portal vessel system as described sofar in reptiles, birds and mammals. Islets in Xenopus located superficially and within deeper regions and emitted both insulo-acinar portal vessels and insulo-venous efferent vessels. Intrainsular microvascular patterns found suggest that in Xenopus islets blood flows first to β-cells and subsequently to the other endocrine cells present in the endocrine pancreas.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"76 1","pages":"35-52"},"PeriodicalIF":0.0,"publicationDate":"2016-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.76.35","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484209","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}
Summary. The pancreas comprises exocrine and endocrine portions, the latter of which is a glucose-responsive tissue that secretes hormones in response to serum glucose levels. One pathway implicated in the regulatory mechanism of this gland is the phosphoinositide (PI) cycle, which generates second messengers. Diacylglycerol (DG), the major second messenger in the PI signaling cascade, is catalyzed by the diacylglycerol kinase (DGK) family. We previously described characteristic expression and localization patterns of DGKs in various organs under pathophysiological conditions. Nevertheless, little is known about the characteristics and morphological aspects of this enzyme family in the pancreas. This study was conducted to investigate the pancreas, specifically the expression and localization of the DGK family. RT-PCR analysis reveals that DGKζ is the major isozyme in the pancreas. Additionally, we show that DGKζ is expressed in pancreatic islet cells, but not in the exocrine cells. It localizes predominantly to the nuclei of α-, β-, and δ-cells. We found further that DGKζ translocates from the nucleus to the cytoplasm in β-cells in response to a β-cell-selective toxin streptozotocin (STZ) and that it disappears over time. These findings will substantiate and extend our understanding of the functional roles of DGKζ in pancreatic islet cells.
{"title":"Localization of diacylglycerol kinase ζ in rat pancreatic islet cells under normal and streptozotocin-induced stress conditions","authors":"Y. Hozumi, T. Nakano, Toshiaki Tanaka, K. Goto","doi":"10.1679/AOHC.76.23","DOIUrl":"https://doi.org/10.1679/AOHC.76.23","url":null,"abstract":"Summary. The pancreas comprises exocrine and endocrine portions, the latter of which is a glucose-responsive tissue that secretes hormones in response to serum glucose levels. One pathway implicated in the regulatory mechanism of this gland is the phosphoinositide (PI) cycle, which generates second messengers. Diacylglycerol (DG), the major second messenger in the PI signaling cascade, is catalyzed by the diacylglycerol kinase (DGK) family. We previously described characteristic expression and localization patterns of DGKs in various organs under pathophysiological conditions. Nevertheless, little is known about the characteristics and morphological aspects of this enzyme family in the pancreas. This study was conducted to investigate the pancreas, specifically the expression and localization of the DGK family. RT-PCR analysis reveals that DGKζ is the major isozyme in the pancreas. Additionally, we show that DGKζ is expressed in pancreatic islet cells, but not in the exocrine cells. It localizes predominantly to the nuclei of α-, β-, and δ-cells. We found further that DGKζ translocates from the nucleus to the cytoplasm in β-cells in response to a β-cell-selective toxin streptozotocin (STZ) and that it disappears over time. These findings will substantiate and extend our understanding of the functional roles of DGKζ in pancreatic islet cells.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"76 1","pages":"23-33"},"PeriodicalIF":0.0,"publicationDate":"2016-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.76.23","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484197","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}
Masaru Sasaki, Y. Sawanobori, Toshiya Tanaka, Hiashi Ueta, Y. Kitazawa, Sachiko Kikuta, T. Issekutz, K. Matsuno
Summary. Although salivary glands are one of the target organs in graft-versus host disease (GVHD), mechanism of disease-related tissue injury has been poorly understood. To investigate it, we employed rat GVHD model including irradiation and donor cell transfer. Immunostaining revealed that submandibular and parotid, but not sublingual glands showed acinar reduction whereas ducts were almost intact. Ductal area of sublingual glands was significantly smaller than those of submandibular and parotid glands. Ductal epithelial cells upregulated expression of class II major histocompatibility complex antigens overtime. This expression preceded donor cell infiltration. Donor cell infiltration was preferentially found in ductal area at the early phase of the disease. While ductal epithelial cells exhibited upregulated mRNA expression of Th1-type chemokines, infiltrating donor cells exhibited their receptors CXCR3 and CCR5. These results suggest ductal epithelial cells have a pivotal role in the progression of GVHD.
{"title":"Pivotal role of duct epithelia in salivary gland GVHD","authors":"Masaru Sasaki, Y. Sawanobori, Toshiya Tanaka, Hiashi Ueta, Y. Kitazawa, Sachiko Kikuta, T. Issekutz, K. Matsuno","doi":"10.1679/AOHC.76.9","DOIUrl":"https://doi.org/10.1679/AOHC.76.9","url":null,"abstract":"Summary. Although salivary glands are one of the target organs in graft-versus host disease (GVHD), mechanism of disease-related tissue injury has been poorly understood. To investigate it, we employed rat GVHD model including irradiation and donor cell transfer. Immunostaining revealed that submandibular and parotid, but not sublingual glands showed acinar reduction whereas ducts were almost intact. Ductal area of sublingual glands was significantly smaller than those of submandibular and parotid glands. Ductal epithelial cells upregulated expression of class II major histocompatibility complex antigens overtime. This expression preceded donor cell infiltration. Donor cell infiltration was preferentially found in ductal area at the early phase of the disease. While ductal epithelial cells exhibited upregulated mRNA expression of Th1-type chemokines, infiltrating donor cells exhibited their receptors CXCR3 and CCR5. These results suggest ductal epithelial cells have a pivotal role in the progression of GVHD.","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"76 1","pages":"9-21"},"PeriodicalIF":0.0,"publicationDate":"2016-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.76.9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484350","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}
M. Shibata, M. Koike, S. Kusumi, Noboru Sato, Y. Uchiyama
amino terminal amino acid sequence of the peptidase was x-Ala-Pro-x-Leu-Pro-Gly-Ser-Thr-Ser-Ala-Thr-x-x-Ser, where x indicates undetectable amino acid residues, and the antiserum against the peptidase was immunopositive for the brush border of a renal proximal tubule and the small intestine, and the surface membrane of bile canaliculi. These results indicate that the unknown peptidase that hydrolyzed AAF-MCA is the soluble form of aminopeptidase N/CD13, and caution is required when using AAF-MCA as a substrate for tripeptidyl peptidase assays. Summary. L-Alanyl-L-alanyl-L-phenylalanine 4-methyl-coumaryl-7-amide (AAF-MCA) is one of the classic substrates for use with tripeptidyl peptidases (TPP-I and TPP-II). We have previously clarified the tissue distribution of TPP-I in detail and noted that the protein expression of TPP-I is often incompatible with its enzyme activity. Herein, we describe the unknown peptidase, which could effectively hydrolyze AAF-MCA, in the rat kidney. The peptidase was purified after four chromatography steps, and its enzyme characteristics were elucidated. The peptidase activity was inhibited by amastatin, bestatin, and o-phenanthroline and was also inhibited by zinc and copper ions. The substrate specificity for several monoamino acidic-MCAs revealed that the peptidase had an affinity for alanyl-MCA. The
肽酶氨基末端氨基酸序列为x- ala - pro -x- leu - pro - gly - ser - thr - ser - ala - thr -x-x- ser，其中x表示未检测到氨基酸残基，抗血清对肾近端小管、小肠刷状缘和胆管表面膜均呈免疫阳性。这些结果表明，水解AAF-MCA的未知肽酶是氨基肽酶N/CD13的可溶性形式，使用AAF-MCA作为三肽基肽酶测定的底物时需要谨慎。总结。l-丙烯酰- l-丙烯酰- l-苯丙氨酸4-甲基-香豆醇-7-酰胺(AAF-MCA)是三肽基肽酶(TPP-I和TPP-II)的经典底物之一。我们之前已经详细阐明了tpp - 1的组织分布，并指出tpp - 1的蛋白表达往往与其酶活性不相容。在此，我们描述了一种未知的肽酶，它可以有效地水解大鼠肾脏中的AAF-MCA。经四层析纯化该肽酶，并对其酶学特性进行了分析。肽酶活性受阿马伐他汀、百司他汀和邻菲罗啉的抑制，锌离子和铜离子也有抑制作用。对几种单氨基酸- mca的底物特异性表明该肽酶对丙烯酰- mca具有亲和力。的
{"title":"A specific tripeptidyl substrate for tripeptidyl peptidase activity is effectively hydrolyzed by alanyl aminopeptidase/aminopeptidase N/CD13 in the rat kidney","authors":"M. Shibata, M. Koike, S. Kusumi, Noboru Sato, Y. Uchiyama","doi":"10.1679/AOHC.76.1","DOIUrl":"https://doi.org/10.1679/AOHC.76.1","url":null,"abstract":"amino terminal amino acid sequence of the peptidase was x-Ala-Pro-x-Leu-Pro-Gly-Ser-Thr-Ser-Ala-Thr-x-x-Ser, where x indicates undetectable amino acid residues, and the antiserum against the peptidase was immunopositive for the brush border of a renal proximal tubule and the small intestine, and the surface membrane of bile canaliculi. These results indicate that the unknown peptidase that hydrolyzed AAF-MCA is the soluble form of aminopeptidase N/CD13, and caution is required when using AAF-MCA as a substrate for tripeptidyl peptidase assays. Summary. L-Alanyl-L-alanyl-L-phenylalanine 4-methyl-coumaryl-7-amide (AAF-MCA) is one of the classic substrates for use with tripeptidyl peptidases (TPP-I and TPP-II). We have previously clarified the tissue distribution of TPP-I in detail and noted that the protein expression of TPP-I is often incompatible with its enzyme activity. Herein, we describe the unknown peptidase, which could effectively hydrolyze AAF-MCA, in the rat kidney. The peptidase was purified after four chromatography steps, and its enzyme characteristics were elucidated. The peptidase activity was inhibited by amastatin, bestatin, and o-phenanthroline and was also inhibited by zinc and copper ions. The substrate specificity for several monoamino acidic-MCAs revealed that the peptidase had an affinity for alanyl-MCA. The","PeriodicalId":8307,"journal":{"name":"Archives of histology and cytology","volume":"76 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2016-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1679/AOHC.76.1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"67484159","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}
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