The aim of the present paper was to check for the presence of cerebrovascular dystroglycan in vertebrates,because dystroglycan,which is localized in the vascular astroglial end-feet,has a pivotal function in glio-vasc...The aim of the present paper was to check for the presence of cerebrovascular dystroglycan in vertebrates,because dystroglycan,which is localized in the vascular astroglial end-feet,has a pivotal function in glio-vascular connections.In mammalian brains,the immunoreactivity ofβ-dystroglycan subunit delineates the vessels.The results of the present study demonstrate similar patterns in other vertebrates,except for anurans and the teleost groups Ostariophysi and Euteleostei.In this study,we investigated 1 or 2 representative species of the main groups of Chondrichthyes,teleost and non-teleost ray-finned fishes,urodeles,anurans,and reptiles.We also investigated 5 mammalian and 3 bird species.Animals were obtained from breeders or fishermen.The presence ofβ-dystroglycan was investigated immunohistochemically in free-floating sections.Pre-embedding electron microscopical immunohistochemistry on Heterodontus japonicus shark brains demonstrated that in Elasmobranchii,β-dystroglycan is also localized in the perivascular glial end-feet despite the different construction of their blood-brain barrier.The results indicated that the cerebrovascularβ-dystroglycan immunoreactivity disappeared separately in anurans,and in teleosts,in the latter group before its division to Ostariophysi and Euteleostei.Immunohistochemistry in muscles and western blots from brain homogenates,however,detected the presence ofβ-dystroglycan,even in anurans and all teleosts.A possible explanation is that in the glial end-feet,β-dystroglycan is masked in these animals,or disappeared during adaptation to the freshwater habitat.展开更多
The blood-brain barrier is a unique property of central nervous system blood vessels that protects sensitive central nervous system cells from potentially harmful blood components.The mechanistic basis of this barrier...The blood-brain barrier is a unique property of central nervous system blood vessels that protects sensitive central nervous system cells from potentially harmful blood components.The mechanistic basis of this barrier is found at multiple levels,including the adherens and tight junction proteins that tightly bind adjacent endothelial cells and the influence of neighboring pericytes,microglia,and astrocyte endfeet.In addition,extracellular matrix components of the vascular basement membrane play a critical role in establishing and maintaining blood-brain barrier integrity,not only by providing an adhesive substrate for blood-brain barrier cells to adhere to,but also by providing guidance cues that strongly influence vascular cell behavior.The extracellular matrix protein laminin is one of the most abundant components of the basement membrane,and several lines of evidence suggest that it plays a key role in directing blood-brain barrier behavior.In this review,we describe the basic structure of laminin and its receptors,the expression patterns of these molecules in central nervous system blood vessels and how they are altered in disease states,and most importantly,how genetic deletion of different laminin isoforms or their receptors reveals the contribution of these molecules to blood-brain barrier function and integrity.Finally,we discuss some of the important unanswered questions in the field and provide a“to-do”list of some of the critical outstanding experiments.展开更多
Myosin XVIIIA, or MYO18A, is a unique PDZ domain-containing unconventional myosin and is evolutionarily conserved from Drosophila to vertebrates. Although there is evidence indicating its expression in the somites, wh...Myosin XVIIIA, or MYO18A, is a unique PDZ domain-containing unconventional myosin and is evolutionarily conserved from Drosophila to vertebrates. Although there is evidence indicating its expression in the somites, whether it regulates muscle function re- mains unclear. We show that the two zebrafish myo18a genes （myo18aa and myo18ab） are predominantly expressed at somite borders during early developmental stages. Knockdown of these genes or overexpression of the MYO18A PDZ domain disrupts myofiber integrity, induces myofiber lesions, and compromises the localization of dystrophin, ^-dystroglycan （^-DG） and laminin at the myotome boundaries. Cell transplantation experiments indicate that myo18a morphant myoblasts fail to form elongated myofibers in the myotomes of wild-type embryos, which can be rescued by the full-length MYO18A protein. These results suggest that MYO18A likely functions in the adhesion process that maintains the stable attachment of myofibers to ECM （extracellular matrix） and muscle integrity during early development.展开更多
文摘The aim of the present paper was to check for the presence of cerebrovascular dystroglycan in vertebrates,because dystroglycan,which is localized in the vascular astroglial end-feet,has a pivotal function in glio-vascular connections.In mammalian brains,the immunoreactivity ofβ-dystroglycan subunit delineates the vessels.The results of the present study demonstrate similar patterns in other vertebrates,except for anurans and the teleost groups Ostariophysi and Euteleostei.In this study,we investigated 1 or 2 representative species of the main groups of Chondrichthyes,teleost and non-teleost ray-finned fishes,urodeles,anurans,and reptiles.We also investigated 5 mammalian and 3 bird species.Animals were obtained from breeders or fishermen.The presence ofβ-dystroglycan was investigated immunohistochemically in free-floating sections.Pre-embedding electron microscopical immunohistochemistry on Heterodontus japonicus shark brains demonstrated that in Elasmobranchii,β-dystroglycan is also localized in the perivascular glial end-feet despite the different construction of their blood-brain barrier.The results indicated that the cerebrovascularβ-dystroglycan immunoreactivity disappeared separately in anurans,and in teleosts,in the latter group before its division to Ostariophysi and Euteleostei.Immunohistochemistry in muscles and western blots from brain homogenates,however,detected the presence ofβ-dystroglycan,even in anurans and all teleosts.A possible explanation is that in the glial end-feet,β-dystroglycan is masked in these animals,or disappeared during adaptation to the freshwater habitat.
文摘The blood-brain barrier is a unique property of central nervous system blood vessels that protects sensitive central nervous system cells from potentially harmful blood components.The mechanistic basis of this barrier is found at multiple levels,including the adherens and tight junction proteins that tightly bind adjacent endothelial cells and the influence of neighboring pericytes,microglia,and astrocyte endfeet.In addition,extracellular matrix components of the vascular basement membrane play a critical role in establishing and maintaining blood-brain barrier integrity,not only by providing an adhesive substrate for blood-brain barrier cells to adhere to,but also by providing guidance cues that strongly influence vascular cell behavior.The extracellular matrix protein laminin is one of the most abundant components of the basement membrane,and several lines of evidence suggest that it plays a key role in directing blood-brain barrier behavior.In this review,we describe the basic structure of laminin and its receptors,the expression patterns of these molecules in central nervous system blood vessels and how they are altered in disease states,and most importantly,how genetic deletion of different laminin isoforms or their receptors reveals the contribution of these molecules to blood-brain barrier function and integrity.Finally,we discuss some of the important unanswered questions in the field and provide a“to-do”list of some of the critical outstanding experiments.
基金supported by the grants from the National Science Foundation of China (No. 31271556)Association Francaise contre les Myopathies (AFM)the Agence Nationale de la Recherche (ANR-09-BLAN-0262-03) in France
文摘Myosin XVIIIA, or MYO18A, is a unique PDZ domain-containing unconventional myosin and is evolutionarily conserved from Drosophila to vertebrates. Although there is evidence indicating its expression in the somites, whether it regulates muscle function re- mains unclear. We show that the two zebrafish myo18a genes （myo18aa and myo18ab） are predominantly expressed at somite borders during early developmental stages. Knockdown of these genes or overexpression of the MYO18A PDZ domain disrupts myofiber integrity, induces myofiber lesions, and compromises the localization of dystrophin, ^-dystroglycan （^-DG） and laminin at the myotome boundaries. Cell transplantation experiments indicate that myo18a morphant myoblasts fail to form elongated myofibers in the myotomes of wild-type embryos, which can be rescued by the full-length MYO18A protein. These results suggest that MYO18A likely functions in the adhesion process that maintains the stable attachment of myofibers to ECM （extracellular matrix） and muscle integrity during early development.
