The Experts below are selected from a list of 12978 Experts worldwide ranked by ideXlab platform
Enrique Rodriguezboulan - One of the best experts on this subject based on the ideXlab platform.
-
identification of the retinal pigment epithelium protein ret pe2 as ce 9 ox 47 a member of the Immunoglobulin Superfamily
Investigative Ophthalmology & Visual Science, 1997Co-Authors: Silvia C Finnemann, Alan D Marmorstein, James M Neill, Enrique RodriguezboulanAbstract:Purpose. To identify the retinal pigment epithelium (RPE) surface antigen recognized by the monoclonal antibody RET-PE2. Methods. A lambda bacteriophage complementary DNA (cDNA) expression library, representing the rat RPE cell line RPE-J, was constructed and screened with the RET-PE2 monoclonal antibody. Transient transfections of the RET-PE2 cDNA, immunofluorescence stainings of tissue sections or cultured cells, and Western blot analyses of tissue and cell detergent extracts served to prove that the protein resulting from expression of the cDNA is the RET-PE2 antigen. Results. Three independent cDNAs were cloned that shared overlapping sequences. Sequence alignment with EMBL database entries revealed identity to the published cDNA of CE-9/OX-47, a member of the Immunoglobulin Superfamily. One of the clones encoded the entire open reading frame of CE-9. The expression pattern of the RET-PE2 antigen matched that of CE-9, which is widely expressed. Chinese hamster ovary cells transiently transfected with the RET-PE2 cDNA produced a membrane-localized protein that was recognized by RET-PE2 and CE-9 antibodies. Conclusions. The antibody RET-PE2 recognizes the CE-9/OX-47 gene product, a transmembrane protein of the Immunoglobulin Superfamily. Contrary to results reported earlier, RET-PE2 immunoreactivity is widely distributed among different rat tissues-kidney, liver, and testis. In epithelia other than the adult RPE, it is confined to the basolateral plasma membrane. Its apical polarization in the RPE of adult rats supports earlier findings that some proteins that are basolateral in other epithelia exhibit reversed polarity in the RPE.
-
identification of the retinal pigment epithelium protein ret pe2 as ce 9 ox 47 a member of the Immunoglobulin Superfamily
Investigative Ophthalmology & Visual Science, 1997Co-Authors: Silvia C Finnemann, Alan D Marmorstein, James M Neill, Enrique RodriguezboulanAbstract:Purpose. To identify the retinal pigment epithelium (RPE) surface antigen recognized by the monoclonal antibody RET-PE2. Methods. A lambda bacteriophage complementary DNA (cDNA) expression library, representing the rat RPE cell line RPE-J, was constructed and screened with the RET-PE2 monoclonal antibody. Transient transfections of the RET-PE2 cDNA, immunofluorescence stainings of tissue sections or cultured cells, and Western blot analyses of tissue and cell detergent extracts served to prove that the protein resulting from expression of the cDNA is the RET-PE2 antigen. Results. Three independent cDNAs were cloned that shared overlapping sequences. Sequence alignment with EMBL database entries revealed identity to the published cDNA of CE-9/OX-47, a member of the Immunoglobulin Superfamily. One of the clones encoded the entire open reading frame of CE-9. The expression pattern of the RET-PE2 antigen matched that of CE-9, which is widely expressed. Chinese hamster ovary cells transiently transfected with the RET-PE2 cDNA produced a membrane-localized protein that was recognized by RET-PE2 and CE-9 antibodies. Conclusions. The antibody RET-PE2 recognizes the CE-9/OX-47 gene product, a transmembrane protein of the Immunoglobulin Superfamily. Contrary to results reported earlier, RET-PE2 immunoreactivity is widely distributed among different rat tissues-kidney, liver, and testis. In epithelia other than the adult RPE, it is confined to the basolateral plasma membrane. Its apical polarization in the RPE of adult rats supports earlier findings that some proteins that are basolateral in other epithelia exhibit reversed polarity in the RPE.
Cyrus Chothia - One of the best experts on this subject based on the ideXlab platform.
-
The Immunoglobulin Superfamily in Drosophila melanogaster and Caenorhabditis elegans and the evolution of complexity.
Development (Cambridge England), 2003Co-Authors: Christine Vogel, Sarah A. Teichmann, Cyrus ChothiaAbstract:Drosophila melanogaster is an arthropod with a much more complex anatomy and physiology than the nematode Caenorhabditis elegans. We investigated one of the protein superfamilies in the two organisms that plays a major role in development and function of cell-cell communication: the Immunoglobulin Superfamily (IgSF). Using hidden Markov models, we identified 142 IgSF proteins in Drosophila and 80 in C. elegans. Of these, 58 and 22, respectively, have been previously identified by experiments. On the basis of homology and the structural characterisation of the proteins, we can suggest probable types of function for most of the novel proteins. Though overall Drosophila has fewer genes than C. elegans, it has many more IgSF cell-surface and secreted proteins. Half the IgSF proteins in C. elegans and three quarters of those in Drosophila have evolved subsequent to the divergence of the two organisms. These results suggest that the expansion of this protein Superfamily is one of the factors that have contributed to the formation of the more complex physiological features that are found in Drosophila.
-
Immunoglobulin Superfamily proteins in Caenorhabditis elegans.
Journal of molecular biology, 2000Co-Authors: Sarah A. Teichmann, Cyrus ChothiaAbstract:The predicted proteins of the genome of Caenorhabditis elegans were analysed by various sequence comparison methods to identify the repertoire of proteins that are members of the Immunoglobulin Superfamily (IgSF). The IgSF is one of the largest families of protein domain in this genome and likely to be one of the major families in other multicellular eukaryotes too. This is because members of the Superfamily are involved in a variety of functions including cell-cell recognition, cell-surface receptors, muscle structure and, in higher organisms, the immune system. Sixty-four proteins with 488 I set IgSF domains were identified largely by using Hidden Markov models. The domain architectures of the protein products of these 64 genes are described. Twenty-one of these had been characterised previously. We show that another 25 are related to proteins of known function. The C. elegans IgSF proteins can be classified into five broad categories: muscle proteins, protein kinases and phosphatases, three categories of proteins involved in the development of the nervous system, leucine-rich repeat containing proteins and proteins without homologues of known function, of which there are 18. The 19 proteins involved in nervous system development that are not kinases or phosphatases are homologues of neuroglian, axonin, NCAM, wrapper, klingon, ICCR and nephrin or belong to the recently identified zig gene family. Out of the set of 64 genes, 22 are on the X chromosome. This study should be seen as an initial description of the IgSF repertoire in C. elegans, because the current gene definitions may contain a number of errors, especially in the case of long sequences, and there may be IgSF genes that have not yet been detected. However, the proteins described here do provide an overview of the bulk of the repertoire of Immunoglobulin Superfamily members in C. elegans, a framework for refinement and extension of the repertoire as gene and protein definitions improve, and the basis for investigations of their function and for comparisons with the repertoires of other organisms.
-
Structure and Stability of an Immunoglobulin Superfamily Domain from Twitchin, a Muscle Protein of the Nematode Caenorhabditis elegans
Journal of molecular biology, 1996Co-Authors: Sun Fong, Cyrus Chothia, Stefan J. Hamill, Mark R. Proctor, Stefan M.v. Freund, Guy M. Benian, Mark Bycroft, Jane ClarkeAbstract:The NMR solution structure of an Immunoglobulin Superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the Immunoglobulin Superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of Immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant.
-
Members of the Immunoglobulin Superfamily in bacteria.
Protein science : a publication of the Protein Society, 1996Co-Authors: Alex Bateman, Sean R. Eddy, Cyrus ChothiaAbstract:We report a prediction that two prokaryotic proteins contain Immunoglobulin Superfamily domains. Immunoglobulin-like folds have been identified previously in prokaryotic proteins, but these share no recognizable sequence similarity with eukaryotic Immunoglobulin Superfamily (IgSF) folds, and may be the result of the physics and chemistry of proteins favoring certain common folds. In contrast, the prokaryotic proteins identified have sequences whose match to the Immunoglobulin Superfamily can be detected by hidden Markov modeling, BLASTP matches, key residue analysis, and secondary structure predictions. We propose that these prokaryotic Immunoglobulin-like domains are almost certain to be related by divergence from a common ancestor to eukaryotic Immunoglobulin Superfamily domains.
-
Many of the Immunoglobulin Superfamily Domains in Cell Adhesion Molecules and Surface Receptors Belong to a New Structural Set Which is close to That Containing Variable Domains
Journal of molecular biology, 1994Co-Authors: Yahouda Harpaz, Cyrus ChothiaAbstract:On the basis of similarities in sequence and structure, the protein domains that form the Immunoglobulin Superfamily have been divided into three sets: one with variable-like domains, the V set, and two with different variants of the constant-like domains, the C1 and C2 sets. Examination of a muscle member of the Immunoglobulin Superfamily, telokin, shows that its structure is closely related to those of the variable domains found in antibodies, CD2, CD4 and CD8. However, it also contains structural features that, previously, have only been found in constant domains. Telokin represents a new structural set in the Superfamily which we call the I set. Using the structures of telokin, and variable domains from antibodies, CD4 and CD8, we constructed a profile that describes the sequence characteristics of the structural core common to those proteins. This sequence profile makes a good match to the sequences of many of the Immunoglobulin Superfamily domains that form the cell adhesion molecules and surface receptors. This match implies that these domains also have structures that belong to the I set.
Melitta Schachner - One of the best experts on this subject based on the ideXlab platform.
-
Neural Cell Adhesion Molecules of the Immunoglobulin Superfamily Regulate Synapse Formation, Maintenance, and Function
Trends in neurosciences, 2017Co-Authors: Vladimir Sytnyk, Iryna Leshchyns'ka, Melitta SchachnerAbstract:Immunoglobulin Superfamily adhesion molecules are among the most abundant proteins in vertebrate and invertebrate nervous systems. Prominent family members are the neural cell adhesion molecules NCAM and L1, which were the first to be shown to be essential not only in development but also in synaptic function and as key regulators of synapse formation, synaptic activity, plasticity, and synaptic vesicle recycling at distinct developmental and activity stages. In addition to interacting with each other, adhesion molecules interact with ion channels and cytokine and neurotransmitter receptors. Mutations in their genes are linked to neurological disorders associated with abnormal development and synaptic functioning. This review presents an overview of recent studies on these molecules and their crucial impact on neurological disorders.
-
The Injured and Regenerating Nervous System: Immunoglobulin Superfamily Members as Key Players
The Neuroscientist : a review journal bringing neurobiology neurology and psychiatry, 2011Co-Authors: Andrey Irintchev, Melitta SchachnerAbstract:Understanding restricted functional recovery and designing efficient treatments to alleviate dysfunction after injury of the nervous system remain major challenges in neuroscience and medicine. Numerous molecules of potential significance in neural repair have been identified in vitro, but only few of these have proved to be of major importance in vivo up to now. Among the molecules involved in regeneration are several members of the Immunoglobulin Superfamily, most notably the neural cell adhesion molecules L1, its close homologue CHL1, and NCAM and, in particular, its polysialic acid glycan moiety. Sufficient evidence is now available to justify the statement that these molecules are major players not only in nervous system development but also in the adult during neural repair and synaptic plasticity. Importantly, insights into the functions of these molecules in promoting or inhibiting functional recovery have allowed the design and assessment of therapeutic approaches in animal models of central nerv...
-
neural recognition molecules of the Immunoglobulin Superfamily signaling transducers of axon guidance and neuronal migration
Nature Neuroscience, 2007Co-Authors: Patricia F Maness, Melitta SchachnerAbstract:Recognition molecules of the Immunoglobulin Superfamily have important roles in neuronal interactions during ontogeny, including migration, survival, axon guidance and synaptic targeting. Their downstream signal transduction events specify whether a cell changes its place of residence or projects axons and dendrites to targets in the brain, allowing the construction of a dynamic neural network. A wealth of recent discoveries shows that cell adhesion molecules interact with attractant and repellent guidance receptors to control growth cone and cell motility in a coordinate fashion. We focus on the best-studied subclasses, the neural cell adhesion molecule NCAM and the L1 family of adhesion molecules, which share important structural and functional features. We have chosen these paradigmatic molecules and their interactions with other recognition molecules as instructive for elucidating the mechanisms by which other recognition molecules may guide cell interactions during development or modify their function as a result of injury, learning and memory.
Silvia C Finnemann - One of the best experts on this subject based on the ideXlab platform.
-
identification of the retinal pigment epithelium protein ret pe2 as ce 9 ox 47 a member of the Immunoglobulin Superfamily
Investigative Ophthalmology & Visual Science, 1997Co-Authors: Silvia C Finnemann, Alan D Marmorstein, James M Neill, Enrique RodriguezboulanAbstract:Purpose. To identify the retinal pigment epithelium (RPE) surface antigen recognized by the monoclonal antibody RET-PE2. Methods. A lambda bacteriophage complementary DNA (cDNA) expression library, representing the rat RPE cell line RPE-J, was constructed and screened with the RET-PE2 monoclonal antibody. Transient transfections of the RET-PE2 cDNA, immunofluorescence stainings of tissue sections or cultured cells, and Western blot analyses of tissue and cell detergent extracts served to prove that the protein resulting from expression of the cDNA is the RET-PE2 antigen. Results. Three independent cDNAs were cloned that shared overlapping sequences. Sequence alignment with EMBL database entries revealed identity to the published cDNA of CE-9/OX-47, a member of the Immunoglobulin Superfamily. One of the clones encoded the entire open reading frame of CE-9. The expression pattern of the RET-PE2 antigen matched that of CE-9, which is widely expressed. Chinese hamster ovary cells transiently transfected with the RET-PE2 cDNA produced a membrane-localized protein that was recognized by RET-PE2 and CE-9 antibodies. Conclusions. The antibody RET-PE2 recognizes the CE-9/OX-47 gene product, a transmembrane protein of the Immunoglobulin Superfamily. Contrary to results reported earlier, RET-PE2 immunoreactivity is widely distributed among different rat tissues-kidney, liver, and testis. In epithelia other than the adult RPE, it is confined to the basolateral plasma membrane. Its apical polarization in the RPE of adult rats supports earlier findings that some proteins that are basolateral in other epithelia exhibit reversed polarity in the RPE.
-
identification of the retinal pigment epithelium protein ret pe2 as ce 9 ox 47 a member of the Immunoglobulin Superfamily
Investigative Ophthalmology & Visual Science, 1997Co-Authors: Silvia C Finnemann, Alan D Marmorstein, James M Neill, Enrique RodriguezboulanAbstract:Purpose. To identify the retinal pigment epithelium (RPE) surface antigen recognized by the monoclonal antibody RET-PE2. Methods. A lambda bacteriophage complementary DNA (cDNA) expression library, representing the rat RPE cell line RPE-J, was constructed and screened with the RET-PE2 monoclonal antibody. Transient transfections of the RET-PE2 cDNA, immunofluorescence stainings of tissue sections or cultured cells, and Western blot analyses of tissue and cell detergent extracts served to prove that the protein resulting from expression of the cDNA is the RET-PE2 antigen. Results. Three independent cDNAs were cloned that shared overlapping sequences. Sequence alignment with EMBL database entries revealed identity to the published cDNA of CE-9/OX-47, a member of the Immunoglobulin Superfamily. One of the clones encoded the entire open reading frame of CE-9. The expression pattern of the RET-PE2 antigen matched that of CE-9, which is widely expressed. Chinese hamster ovary cells transiently transfected with the RET-PE2 cDNA produced a membrane-localized protein that was recognized by RET-PE2 and CE-9 antibodies. Conclusions. The antibody RET-PE2 recognizes the CE-9/OX-47 gene product, a transmembrane protein of the Immunoglobulin Superfamily. Contrary to results reported earlier, RET-PE2 immunoreactivity is widely distributed among different rat tissues-kidney, liver, and testis. In epithelia other than the adult RPE, it is confined to the basolateral plasma membrane. Its apical polarization in the RPE of adult rats supports earlier findings that some proteins that are basolateral in other epithelia exhibit reversed polarity in the RPE.
Alan D Marmorstein - One of the best experts on this subject based on the ideXlab platform.
-
identification of the retinal pigment epithelium protein ret pe2 as ce 9 ox 47 a member of the Immunoglobulin Superfamily
Investigative Ophthalmology & Visual Science, 1997Co-Authors: Silvia C Finnemann, Alan D Marmorstein, James M Neill, Enrique RodriguezboulanAbstract:Purpose. To identify the retinal pigment epithelium (RPE) surface antigen recognized by the monoclonal antibody RET-PE2. Methods. A lambda bacteriophage complementary DNA (cDNA) expression library, representing the rat RPE cell line RPE-J, was constructed and screened with the RET-PE2 monoclonal antibody. Transient transfections of the RET-PE2 cDNA, immunofluorescence stainings of tissue sections or cultured cells, and Western blot analyses of tissue and cell detergent extracts served to prove that the protein resulting from expression of the cDNA is the RET-PE2 antigen. Results. Three independent cDNAs were cloned that shared overlapping sequences. Sequence alignment with EMBL database entries revealed identity to the published cDNA of CE-9/OX-47, a member of the Immunoglobulin Superfamily. One of the clones encoded the entire open reading frame of CE-9. The expression pattern of the RET-PE2 antigen matched that of CE-9, which is widely expressed. Chinese hamster ovary cells transiently transfected with the RET-PE2 cDNA produced a membrane-localized protein that was recognized by RET-PE2 and CE-9 antibodies. Conclusions. The antibody RET-PE2 recognizes the CE-9/OX-47 gene product, a transmembrane protein of the Immunoglobulin Superfamily. Contrary to results reported earlier, RET-PE2 immunoreactivity is widely distributed among different rat tissues-kidney, liver, and testis. In epithelia other than the adult RPE, it is confined to the basolateral plasma membrane. Its apical polarization in the RPE of adult rats supports earlier findings that some proteins that are basolateral in other epithelia exhibit reversed polarity in the RPE.
-
identification of the retinal pigment epithelium protein ret pe2 as ce 9 ox 47 a member of the Immunoglobulin Superfamily
Investigative Ophthalmology & Visual Science, 1997Co-Authors: Silvia C Finnemann, Alan D Marmorstein, James M Neill, Enrique RodriguezboulanAbstract:Purpose. To identify the retinal pigment epithelium (RPE) surface antigen recognized by the monoclonal antibody RET-PE2. Methods. A lambda bacteriophage complementary DNA (cDNA) expression library, representing the rat RPE cell line RPE-J, was constructed and screened with the RET-PE2 monoclonal antibody. Transient transfections of the RET-PE2 cDNA, immunofluorescence stainings of tissue sections or cultured cells, and Western blot analyses of tissue and cell detergent extracts served to prove that the protein resulting from expression of the cDNA is the RET-PE2 antigen. Results. Three independent cDNAs were cloned that shared overlapping sequences. Sequence alignment with EMBL database entries revealed identity to the published cDNA of CE-9/OX-47, a member of the Immunoglobulin Superfamily. One of the clones encoded the entire open reading frame of CE-9. The expression pattern of the RET-PE2 antigen matched that of CE-9, which is widely expressed. Chinese hamster ovary cells transiently transfected with the RET-PE2 cDNA produced a membrane-localized protein that was recognized by RET-PE2 and CE-9 antibodies. Conclusions. The antibody RET-PE2 recognizes the CE-9/OX-47 gene product, a transmembrane protein of the Immunoglobulin Superfamily. Contrary to results reported earlier, RET-PE2 immunoreactivity is widely distributed among different rat tissues-kidney, liver, and testis. In epithelia other than the adult RPE, it is confined to the basolateral plasma membrane. Its apical polarization in the RPE of adult rats supports earlier findings that some proteins that are basolateral in other epithelia exhibit reversed polarity in the RPE.
