scholarly journals Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation

1994 ◽  
Vol 124 (1) ◽  
pp. 149-160 ◽  
Author(s):  
CS Stipp ◽  
ED Litwack ◽  
AD Lander
Keyword(s):  
Nervous System ◽  
Heparan Sulfate ◽  
Developmental Stages ◽  
Core Protein ◽  
Adherent Cells ◽  
Attachment Sites ◽  
Developing Neurons ◽  
Developing Rat ◽  
Developing Nervous System

Heparan sulfate proteoglycans (HSPGs) are found on the surface of all adherent cells and participate in the binding of growth factors, extracellular matrix glycoproteins, cell adhesion molecules, and proteases and antiproteases. We report here the cloning and pattern of expression of cerebroglycan, a glycosylphosphatidylinositol (GPI)-anchored HSPG that is found in the developing rat brain (previously referred to as HSPG M13; Herndon, M. E., and A. D. Lander. 1990. Neuron. 4:949-961). The cerebroglycan core protein has a predicted molecular mass of 58.6 kD and five potential heparan sulfate attachment sites. Together with glypican (David, G., V. Lories, B. Decock, P. Marynen, J.-J. Cassiman, and H. Van den Berghe. 1990. J. Cell Biol. 111:3165-3176), it defines a family of integral membrane HSPGs characterized by GPI linkage and conserved structural motifs, including a pattern of 14 cysteine residues that is absolutely conserved. Unlike other known integral membrane HSPGs, including glypican and members of the syndecan family of transmembrane proteoglycans, cerebroglycan is expressed in only one tissue: the nervous system. In situ hybridization experiments at several developmental stages strongly suggest that cerebroglycan message is widely and transiently expressed by immature neurons, appearing around the time of final mitosis and disappearing after cell migration and axon outgrowth have been completed. These results suggest that cerebroglycan may fulfill a function related to the motile behaviors of developing neurons.

NeuroM, a neural helix-loop-helix transcription factor, defines a new transition stage in neurogenesis

Development ◽  
1997 ◽  
Vol 124 (17) ◽  
pp. 3263-3272 ◽  
Author(s):  
T. Roztocil ◽  
L. Matter-Sadzinski ◽  
C. Alliod ◽  
M. Ballivet ◽  
J.M. Matter
Keyword(s):  
Nervous System ◽  
Transcription Factor ◽  
Mitotic Cycle ◽  
Ventricular Zone ◽  
Helix Loop Helix ◽  
E Box ◽  
Genes Encoding ◽  
Developing Nervous System

Genes encoding transcription factors of the helix-loop-helix family are essential for the development of the nervous system in Drosophila and vertebrates. Screens of an embryonic chick neural cDNA library have yielded NeuroM, a novel neural-specific helix-loop-helix transcription factor related to the Drosophila proneural gene atonal. The NeuroM protein most closely resembles the vertebrate NeuroD and Nex1/MATH2 factors, and is capable of transactivating an E-box promoter in vivo. In situ hybridization studies have been conducted, in conjunction with pulse-labeling of S-phase nuclei, to compare NeuroM to NeuroD expression in the developing nervous system. In spinal cord and optic tectum, NeuroM expression precedes that of NeuroD. It is transient and restricted to cells lining the ventricular zone that have ceased proliferating but have not yet begun to migrate into the outer layers. In retina, NeuroM is also transiently expressed in cells as they withdraw from the mitotic cycle, but persists in horizontal and bipolar neurons until full differentiation, assuming an expression pattern exactly complementary to NeuroD. In the peripheral nervous system, NeuroM expression closely follows cell proliferation, suggesting that it intervenes at a similar developmental juncture in all parts of the nervous system. We propose that availability of the NeuroM helix-loop-helix factor defines a new stage in neurogenesis, at the transition between undifferentiated, premigratory and differentiating, migratory neural precursors.

scholarly journals Neurotrophin, p75, and Trk Signaling Module in the Developing Nervous System of the Marine AnnelidPlatynereis dumerilii

2016 ◽  
Vol 2016 ◽  
pp. 1-12 ◽  
Author(s):  
Antonella Lauri ◽  
Paola Bertucci ◽  
Detlev Arendt
Keyword(s):  
Nervous System ◽  
Neuronal Development ◽  
Neural Circuit ◽  
Circuit Development ◽  
Circuit Formation ◽  
Neurotrophic Signaling ◽  
High Degree ◽  
Developing Nervous System

In vertebrates, neurotrophic signaling plays an important role in neuronal development, neural circuit formation, and neuronal plasticity, but its evolutionary origin remains obscure. We found and validated nucleotide sequences encoding putative neurotrophic ligands (neurotrophin, NT) and receptors (Trk and p75) in two annelids,Platynereis dumerilii(Errantia) andCapitella teleta(Sedentaria, for which some sequences were found recently by Wilson, 2009). Predicted protein sequences and structures ofPlatynereisneurotrophic molecules reveal a high degree of conservation with the vertebrate counterparts; some amino acids signatures present in the annelid Trk sequences are absent in the basal chordate amphioxus, reflecting secondary loss in the cephalochordate lineage. In addition, expression analysis of NT, Trk, and p75 duringPlatynereisdevelopment by whole-mount mRNAin situhybridization supports a role of these molecules in nervous system and circuit development. These annelid data corroborate the hypothesis that the neurotrophic signaling and its involvement in shaping neural networks predate the protostome-deuterostome split and were present in bilaterian ancestors.

Distribution of acetylcholinesterase activity during the development of cysticercoids of Hymenolepis diminuta (Cestoda)

2006 ◽  
Vol 51 (2) ◽  
Author(s):  
Tadeusz Moczoń ◽  
Agnieszka Świetlikowska
Keyword(s):  
Nervous System ◽  
Developmental Stages ◽  
Acetylcholinesterase Activity ◽  
Hymenolepis Diminuta ◽  
Internal Wall ◽  
Early Developmental Stages ◽  
Early Developmental ◽  
Late Stages ◽  
Cyst Cavity ◽  
Developing Nervous System

AbstractThe distribution of acetylcholinesterase (AChE) in oncospheres and developing cysticercoids of Hymenolepis diminuta was examined. The enzyme was localized in the nervous system and in some non-nerve cells of these larvae. In oncospheres AChE was detected in hook muscles and in the binucleated medullar center that is known to enclose two neurons. At early developmental stages of the cysticercoids the enzyme was localized in the post-oncospheral hook muscles and in subtegumental muscle fibers of the cercomer. At medium and late stages of development the activity of AChE was detected in the developing nervous system and in two and, subsequently, in four populations of cells, which gradually spread over the whole internal wall of the cyst, thus forming a thin multilayer AChE-positive lining of the cyst cavity. Following withdrawal of the scolex the lining separates the parenchyma of the turned neck from the cyst tissues and remains AChE-positive during the whole life of the parasite, i.e. up to the death of the infected host. The role played by non-neural AChE associated with the cyst cavity lining is unknown, but seems to regulate both the transport of nutrients and minerals into the scolex and waste substances in the opposite direction.

Molecular analysis of heparan sulfate biosynthetic enzyme machinery and characterization of heparan sulfate structure in Nematostella vectensis

2009 ◽  
Vol 419 (3) ◽  
pp. 585-593 ◽  
Author(s):  
Almir Feta ◽  
Anh-Tri Do ◽  
Fabian Rentzsch ◽  
Ulrich Technau ◽  
Marion Kusche-Gullberg
Keyword(s):  
Heparan Sulfate ◽  
Developmental Stages ◽  
Structural Complexity ◽  
Sea Anemone ◽  
The Body ◽  
Nematostella Vectensis ◽  
Last Common Ancestor ◽  
Protein Ligands ◽  
Enzyme Families

HS (heparan sulfate) proteoglycans are key regulators of vital processes in the body. HS chains with distinct sequences bind to various protein ligands, such as growth factors and morphogens, and thereby function as important regulators of protein gradient formation and signal transduction. HS is synthesized through the concerted action of many different ER (endoplasmic reticulum) and Golgi-resident enzymes. In higher organisms, many of these enzymes occur in multiple isoforms that differ in substrate specificity and spatial and temporal expression. In order to investigate how the structural complexity of HS has evolved, in the present study we focused on the starlet sea anemone (Nematostella vectensis), which belongs to the Anthozoa, which are considered to have retained many ancestral features. Members of all of the enzyme families involved in the generation and modification of HS were identified in Nematostella. Our results show that the enzymes are highly conserved throughout evolution, but the number of isoforms varies. Furthermore, the HS polymerases [Ext (exostosin) enzymes Ext1, Ext2 and Ext-like3] represent distinct subgroups, indicating that these three genes have already been present in the last common ancestor of Cnidaria and Bilateria. In situ hybridization showed up-regulation of certain enzymes in specific areas of the embryo at different developmental stages. The specific mRNA expression pattern of particular HS enzymes implies that they may play a specific role in HS modifications during larval development. Finally, biochemical analysis of Nematostella HS demonstrates that the sea anemone synthesizes a polysaccharide with a unique structure.

scholarly journals Drosophila laminin: sequence of B2 subunit and expression of all three subunits during embryogenesis.

1989 ◽  
Vol 109 (5) ◽  
pp. 2441-2453 ◽  
Author(s):  
D J Montell ◽  
C S Goodman
Keyword(s):  
Nervous System ◽  
In Situ Hybridization ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Drosophila Embryogenesis ◽  
Substrate Adhesion ◽  
Genes Encoding ◽  
Developing Nervous System

In a previous study, we described the cloning of the genes encoding the three subunits of Drosophila laminin, a substrate adhesion molecule, and the cDNA sequence of the B1 subunit (Montell and Goodman, 1988). This analysis revealed the similarity of Drosophila laminin with the mouse and human complexes in subunit composition, domain structure, and amino acid sequence. In this paper, we report the deduced amino acid sequence of the B2 subunit. We then describe the expression and tissue distribution of the three subunits of laminin during Drosophila embryogenesis using both in situ hybridization and immunolocalization techniques, with particular emphasis on its expression in and around the developing nervous system.

scholarly journals In situ immunodetection of activated caspase-3 in apoptotic neurons in the developing nervous system

1998 ◽  
Vol 5 (12) ◽  
pp. 1004-1016 ◽  
Author(s):  
Anu Srinivasan ◽  
Kevin A Roth ◽  
Robert O Sayers ◽  
Kenneth S Shindler ◽  
Angela M Wong ◽  
...  
Keyword(s):  
Nervous System ◽  
Caspase 3 ◽  
Developing Nervous System

Expression of decorin mRNA in the nervous system of rat.

1993 ◽  
Vol 41 (9) ◽  
pp. 1383-1391 ◽  
Author(s):  
C O Hanemann ◽  
G Kuhn ◽  
A Lie ◽  
C Gillen ◽  
F Bosse ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
In Situ Hybridization ◽  
Amino Acid ◽  
Sciatic Nerve ◽  
Peripheral Nerve ◽  
Core Protein ◽  
Molecular Layer ◽  
Northern Blotting

A rat cDNA clone (pCD67) isolated from a cDNA library of regenerating sciatic nerve by differential hybridization screening revealed 75% homology on the nucleic acid level and 81% homology (including conservative amino acid changes) to the deduced amino acid sequence of the core protein of human dermatan/chondroitin sulfate proteoglycan decorin (PGII, PG40, PG-S2). Two transcripts of 1.3 and 1.75 KB very similar in size to the two decorin mRNA species previously identified in connective tissue were detected by Northern blotting in both normal and injured sciatic nerve and in the mature and embryonic rat brain. The steady-state level of the decorin 1.3 KB mRNA was very much higher in peripheral nerve than in the central nervous system or in other non-neural tissues (skeletal muscle, heart, colon, kidney). In situ hybridization experiments indicated that decorin mRNA is expressed by Schwann cells and vascular cells in peripheral nerve. In the spinal cord the ventral horn motor neurons and other neurons in gray matter showed specific hybridization signals. Furthermore, in situ hybridization indicated decorin expression in Purkinje neurons and cells of the molecular layer in cerebellum, and in neurons of the primary olfactory cortex and brainstem (pons). Our data clearly demonstrate decorin mRNA expression in distinct neural cell populations, suggesting yet unknown functions of this proteoglycan in the peripheral and central nervous system.

A chicken achaete-scute homolog (CASH-1) is expressed in a temporally and spatially discrete manner in the developing nervous system

Development ◽  
1994 ◽  
Vol 120 (4) ◽  
pp. 769-783 ◽  
Author(s):  
C.L. Jasoni ◽  
M.B. Walker ◽  
M.D. Morris ◽  
T.A. Reh
Keyword(s):  
Nervous System ◽  
Amino Acid ◽  
Progenitor Cell ◽  
Sequence Similarity ◽  
Basic Helix Loop Helix ◽  
Helix Loop Helix ◽  
Neuronal Progenitor ◽  
Discrete Manner ◽  
Developing Nervous System

We have identified a basic helix-loop-helix encoding cDNA from embryonic chicken retina which shares sequence similarity with the achaete-scute family of genes of Drosophila. The deduced amino acid sequence of this chicken achaete-scute homolog (CASH-1) is identical, over the region encoding the basic helix-loop-helix domain, to the recently identified mammalian achaete-scute homolog (MASH-1) and to the Xenopus homolog (XASH1), and 70% identical, over the same region, to Drosophila achaete-scute complex members. The expression of CASH-1 is restricted to subsets of neuronal progenitor cells in the developing chicken nervous system, similar in distribution to that reported for MASH-1 and XASH1. In addition, in situ localization in the retina reveals a dynamic character of expression of the gene in a particular region of the CNS, and suggests that the expression of CASH-1 may be important in defining a particular stage in the progenitor cell necessary for the differentiation of particular neuronal phenotypes.

scholarly journals Molecular cloning of syndecan, an integral membrane proteoglycan.

1989 ◽  
Vol 108 (4) ◽  
pp. 1547-1556 ◽  
Author(s):  
S Saunders ◽  
M Jalkanen ◽  
S O'Farrell ◽  
M Bernfield
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Transmembrane Domain ◽  
Core Protein ◽  
Extracellular Domain ◽  
Cdna Clones ◽  
Type I ◽  
Attachment Sites ◽  
Sequence Characteristics

We describe cDNA clones for a cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. The cDNA encodes a unique core protein of 32,868 D that contains several structural features consistent with its role as a glycosamino-glycan-containing matrix anchor. The sequence shows discrete cytoplasmic, transmembrane, and NH2-terminal extracellular domains, indicating that the molecule is a type I integral membrane protein. The cytoplasmic domain is small and similar in size but not in sequence to that of the beta-chain of various integrins. The extracellular domain contains a single dibasic sequence adjacent to the extracellular face of the transmembrane domain, potentially serving as the protease-susceptible site involved in release of this domain from the cell surface. The extracellular domain contains two distinct types of putative glycosaminoglycan attachment sites; one type shows sequence characteristics of the sites previously described for chondroitin sulfate attachment (Bourdon, M. A., T. Krusius, S. Campbell, N. B. Schwartz, and E. Ruoslahti. 1987. Proc. Natl. Acad. Sci. USA. 84:3194-3198), but the other type has newly identified sequence characteristics that potentially correspond to heparan sulfate attachment sites. The single N-linked sugar recognition sequence is within the putative chondroitin sulfate attachment sequence, suggesting asparagine glycosylation as a mechanism for regulating chondroitin sulfate chain addition. Both 5' and 3' regions of this cDNA have sequences substantially identical to analogous regions of the human insulin receptor cDNA: a 99-bp region spanning the 5' untranslated and initial coding sequences is 67% identical and a 35-bp region in the 3' untranslated region is 81% identical in sequence. mRNA expression is tissue specific; various epithelial tissues show the same two sizes of mRNA (2.6 and 3.4 kb); in the same relative abundance (3:1), the cerebrum shows a single 4.5-kb mRNA. This core protein cDNA describes a new class of molecule, an integral membrane proteoglycan, that we propose to name syndecan (from the Greek syndein, to bind together).

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