Class I and class II ganglion cells of rabbit retina: A structural basis for X and Y (brisk) cells

2004 ◽  
Vol 478 (4) ◽  
pp. 323-346 ◽  
Author(s):  
Edward V. Famiglietti
Keyword(s):  
Ganglion Cells ◽  
Class Ii ◽  
Class I ◽  
Structural Basis ◽  
Rabbit Retina

scholarly journals Purification and Crystallization Reveal Two Types of Interactions of the Fusion Protein Homotrimer of Semliki Forest Virus

2004 ◽  
Vol 78 (7) ◽  
pp. 3514-3523 ◽  
Author(s):  
Don L. Gibbons ◽  
Brigid Reilly ◽  
Anna Ahn ◽  
Marie-Christine Vaney ◽  
Armelle Vigouroux ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Fusion Proteins ◽  
Semliki Forest Virus ◽  
Three Dimensional ◽  
Class Ii ◽  
Class I ◽  
Structural Basis ◽  
Viral Fusion ◽  
Purification Method ◽  
Viral Fusion Proteins

ABSTRACT The fusion proteins of the alphaviruses and flaviviruses have a similar native structure and convert to a highly stable homotrimer conformation during the fusion of the viral and target membranes. The properties of the alpha- and flavivirus fusion proteins distinguish them from the class I viral fusion proteins, such as influenza virus hemagglutinin, and establish them as the first members of the class II fusion proteins. Understanding how this new class carries out membrane fusion will require analysis of the structural basis for both the interaction of the protein subunits within the homotrimer and their interaction with the viral and target membranes. To this end we report a purification method for the E1 ectodomain homotrimer from the alphavirus Semliki Forest virus. The purified protein is trimeric, detergent soluble, retains the characteristic stability of the starting homotrimer, and is free of lipid and other contaminants. In contrast to the postfusion structures that have been determined for the class I proteins, the E1 homotrimer contains the fusion peptide region responsible for interaction with target membranes. This E1 trimer preparation is an excellent candidate for structural studies of the class II viral fusion proteins, and we report conditions that generate three-dimensional crystals suitable for analysis by X-ray diffraction. Determination of the structure will provide our first high-resolution views of both the low-pH-induced trimeric conformation and the target membrane-interacting region of the alphavirus fusion protein.

A structural basis for omnidirectional connections between starburst amacrine cells and directionally selective ganglion cells in rabbit retina, with associated bipolar cells

2002 ◽  
Vol 19 (2) ◽  
pp. 145-162 ◽  
Author(s):  
E.V. FAMIGLIETTI
Keyword(s):  
Ganglion Cells ◽  
Dendritic Tree ◽  
Amacrine Cells ◽  
Dendritic Morphology ◽  
Bipolar Cells ◽  
Structural Basis ◽  
Rabbit Retina ◽  
Low Velocity ◽  
Accessory Optic System ◽  
Starburst Amacrine Cells

Directionally selective (DS) ganglion cells of rabbit retina are of two principal types. ON DS ganglion cells prefer low velocity in one of three directions of movement and project axons to the accessory optic system (AOS), whereas ON–OFF DS ganglion cells prefer higher velocity in one of four directions and project to tectum and thalamus. Each has a distinct, recognizable dendritic morphology, based upon the correlation of form, physiology, and central projections. In previous Golgi studies, ON and ON–OFF DS cells were found to be partly co-stratified, and ON–OFF DS cells were found to co-stratify with starburst amacrine (SA) cells, the cholinergic amacrine cells of the retina, which also contain elevated levels of GABA. SA cells are radially symmetrical, have synaptic boutons in a distal annular zone of its dendritic tree, are presynaptic primarily to ganglion cell dendrites, co-stratify with ON–OFF DS ganglion cells, and contain the neurotransmitters shown pharmacologically to be involved in DS responses. For these reasons, SA cells are thought to play a role in the DS mechanism. Several models of this mechanism have utilized SA cell dendritic geometry in a centrifugal, radial format to impose directional inputs on DS ganglion cells.

scholarly journals The fidelity of the translation of the genetic code.

2001 ◽  
Vol 48 (2) ◽  
pp. 323-335 ◽  
Author(s):  
R Sankaranarayanan ◽  
D Moras
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Genetic Code ◽  
Structural Information ◽  
Class Ii ◽  
Zinc Ion ◽  
Trna Synthetase ◽  
Class I ◽  
Structural Basis ◽  
Clear Understanding

Aminoacyl-tRNA synthetases play a central role in maintaining accuracy during the translation of the genetic code. To achieve this challenging task they have to discriminate against amino acids that are very closely related not only in structure but also in chemical nature. A 'double-sieve' editing model was proposed in the late seventies to explain how two closely related amino acids may be discriminated. However, a clear understanding of this mechanism required structural information on synthetases that are faced with such a problem of amino acid discrimination. The first structural basis for the editing model came recently from the crystal structure of isoleucyl-tRNA synthetase, a class I synthetase, which has to discriminate against valine. The structure showed the presence of two catalytic sites in the same enzyme, one for activation, a coarse sieve which binds both isoleucine and valine, and another for editing, a fine sieve which binds only valine and rejects isoleucine. Another structure of the enzyme in complex with tRNA showed that the tRNA is responsible for the translocation of the misactivated amino-acid substrate from the catalytic site to the editing site. These studies were mainly focused on class I synthetases and the situation was not clear about how class II enzymes discriminate against similar amino acids. The recent structural and enzymatic studies on threonyl-tRNA synthetase, a class II enzyme, reveal how this challenging task is achieved by using a unique zinc ion in the active site as well as by employing a separate domain for specific editing activity. These studies led us to propose a model which emphasizes the mirror symmetrical approach of the two classes of enzymes and highlights that tRNA is the key player in the evolution of these class of enzymes.

scholarly journals The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding, transport, and peptide occupancy.

1994 ◽  
Vol 180 (3) ◽  
pp. 1107-1113 ◽  
Author(s):  
P Romagnoli ◽  
R N Germain
Keyword(s):  
Major Histocompatibility Complex ◽  
Mhc Class Ii ◽  
Peptide Binding ◽  
Class Ii ◽  
Class I ◽  
Structural Basis ◽  
Invariant Chain ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Mhc Class Ii Molecules

Invariant chain (Ii) contributes in a number of distinct ways to the proper functioning of major histocompatibility complex (MHC) class II molecules. These include promoting effective association and folding of newly synthesized MHC class II alpha and beta subunits, increasing transit of assembled heterodimers out of the endoplasmic reticulum (ER), inhibiting class II peptide binding, and facilitating class II movement to or accumulation in endosomes/lysosomes. Although the cytoplasmic tail of Ii makes a key contribution to the endocytic localization of class II, the relationship between the structure of Ii and its other diverse functions remains unknown. We show here that two thirds of the lumenal segment of Ii can be eliminated without affecting its contributions to the secretory pathway events of class II folding, ER to Golgi transport, or inhibition of peptide binding. These same experiments reveal that a short (25 residue) contiguous internal segment of Ii (the CLIP region), frequently found associated with purified MHC class II molecules, is critical for all three functions. Together with other recent findings, these results raise the possibility that the contributions of Ii to the early postsynthetic behavior of class II may depend on its interaction with the class II binding site. This would be consistent with the intracellular behavior of unoccupied MHC class I and class II molecules as incompletely folded proteins and imply a related structural basis for the similar contributions of Ii to class II and of short peptides to class I assembly and transport.

Electron microscopy analysis of degenerating pancreatic ß cells in transgenic mice expressing the MHC Class I antigen Dd

1990 ◽  
Vol 48 (3) ◽  
pp. 548-549
Author(s):  
T. A. Stewart ◽  
D. Liggitt ◽  
S. Pitts ◽  
L. Martin ◽  
M. Siegel ◽  
...  
Keyword(s):  
Type I Diabetes ◽  
Disease Process ◽  
Class Ii ◽  
Class I ◽  
Type I ◽  
Aberrant Expression ◽  
Mhc Molecules ◽  
Endogenous Insulin ◽  
Class Ii Mhc ◽  
Ifn Γ

Insulin-dependant (Type I) diabetes mellitus (IDDM) is a metabolic disorder resulting from the lack of endogenous insulin secretion. The disease is thought to result from the autoimmune mediated destruction of the insulin producing ß cells within the islets of Langerhans. The disease process is probably triggered by environmental agents, e.g. virus or chemical toxins on a background of genetic susceptibility associated with particular alleles within the major histocompatiblity complex (MHC). The relation between IDDM and the MHC locus has been reinforced by the demonstration of both class I and class II MHC proteins on the surface of ß cells from newly diagnosed patients as well as mounting evidence that IDDM has an autoimmune pathogenesis. In 1984, a series of observations were used to advance a hypothesis, in which it was suggested that aberrant expression of class II MHC molecules, perhaps induced by gamma-interferon (IFN γ) could present self antigens and initiate an autoimmune disease. We have tested some aspects of this model and demonstrated that expression of IFN γ by pancreatic ß cells can initiate an inflammatory destruction of both the islets and pancreas and does lead to IDDM.

Pictish Horse Carvings

1991 ◽  
Vol 17 (1) ◽  
pp. 53-62
Author(s):  
Irene Hughson
Keyword(s):  
Class Ii ◽  
Class I ◽  
Early Historic Period ◽  
High Quality ◽  
Historic Period ◽  
Agricultural Economy ◽  
Different Types ◽  
Early Historic

Summary This paper examines the horse carvings to be found on Class I and Class II Pictish sculptured stones and considers their reliability as evidence of the sort of horses and ponies that would have existed in the Early Historic Period. An attempt is made to show that the availability in Britain of good sized, high quality riding horses during that period is not inconsistent with what is known of the development and distribution of different types of horses in pre-hislory. The importance of horses and ponies in Early Historic societies is stressed and inferences drawn about the agricultural economy that could support horses and the skilled specialists required to look after them.

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