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Relevant bibliographies by topics / Expression human fibronectin IIICS mRNA

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Academic literature on the topic 'Expression human fibronectin IIICS mRNA'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Expression human fibronectin IIICS mRNA"

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Hershberger, R. P., and L. A. Culp. "Cell-type-specific expression of alternatively spliced human fibronectin IIICS mRNAs." Molecular and Cellular Biology 10, no. 2 (1990): 662–71. http://dx.doi.org/10.1128/mcb.10.2.662.

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Fibronectin polypeptide diversity is generated to a large extent by alternative splicing of the fibronectin primary transcript at three sites: two extra domain exons encoding extra structural repeats and a region of nonhomologous sequence termed the type-III connecting segment (IIICS). A novel double primer extension assay was developed to identify and quantify simultaneously each of the five human IIICS mRNA splicing variants. Expression of the five IIICS variants was analyzed in a variety of human normal and tumor cell types as well as in human liver. Differences in IIICS expression patterns

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Hershberger, R. P., and L. A. Culp. "Cell-type-specific expression of alternatively spliced human fibronectin IIICS mRNAs." Molecular and Cellular Biology 10, no. 2 (1990): 662–71. http://dx.doi.org/10.1128/mcb.10.2.662-671.1990.

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Fibronectin polypeptide diversity is generated to a large extent by alternative splicing of the fibronectin primary transcript at three sites: two extra domain exons encoding extra structural repeats and a region of nonhomologous sequence termed the type-III connecting segment (IIICS). A novel double primer extension assay was developed to identify and quantify simultaneously each of the five human IIICS mRNA splicing variants. Expression of the five IIICS variants was analyzed in a variety of human normal and tumor cell types as well as in human liver. Differences in IIICS expression patterns

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Castellani, P., A. Siri, C. Rosellini, E. Infusini, L. Borsi, and L. Zardi. "Transformed human cells release different fibronectin variants than do normal cells." Journal of Cell Biology 103, no. 5 (1986): 1671–77. http://dx.doi.org/10.1083/jcb.103.5.1671.

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Fibronectin molecules are dimers composed of subunits whose primary structures may differ. This is due to alternative splicing in at least two regions (ED and IIICS) of the pre-mRNA. Using two monoclonal antibodies specific for two different epitopes of domain 5 (high affinity for heparin), we have quantitatively analyzed the expression of the IIICS sequence in human fibronectins from different sources. The results demonstrated that the percentage of fibronectin subunits containing the IIICS is higher in fibronectins from tumor-derived or simian virus 40-transformed human cells than in fibrone

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Mardon, H. J., and G. Sebastio. "Regulation of alternative splicing in the IIICS region of human fibronectin pre-mRNA encoding cell binding sites CS1 and CS5." Journal of Cell Science 103, no. 2 (1992): 423–33. http://dx.doi.org/10.1242/jcs.103.2.423.

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The cell binding sites CS1 and CS5 in the IIICS region of human fibronectin (FN) mediate the adhesion of specific cell types by interacting with the integrin alpha 4 beta 1. IIICS pre-mRNA is alternatively spliced via the use of three alternative splice acceptor sites and one alternative splice donor site. These alternative splicing pathways can potentially give rise to variant FN molecules which are CS1+,CS5+; CS1+,CS5-; CS1-,CS5+ or CS1-,CS5-. Here we show that selection of the acceptor site which incorporates mRNA encoding CS1 and CS5 is more frequent in foetal tissues compared to adult liv

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Humphries, M. J., S. K. Akiyama, A. Komoriya, K. Olden, and K. M. Yamada. "Neurite extension of chicken peripheral nervous system neurons on fibronectin: relative importance of specific adhesion sites in the central cell-binding domain and the alternatively spliced type III connecting segment." Journal of Cell Biology 106, no. 4 (1988): 1289–97. http://dx.doi.org/10.1083/jcb.106.4.1289.

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Fibronectin contains at least two domains that support cell adhesion. One is the central cell-binding domain that is recognized by a variety of cell types, including fibroblasts. The second, originally identified by its ability to support melanoma cell adhesion, is located in the alternatively spliced type III connecting segment (IIICS). Using specific adhesive ligands and inhibitory probes, we have examined the role of each of these domains in fibronectin-mediated neurite extension of neurons from chick embryo dorsal root and sympathetic ganglia. In studies using explanted ganglia, both fl3,

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Rosi, E., J. D. Beckmann, P. Pladsen, S. I. Rennard, and D. J. Romberger. "Modulation of human bronchial epithelial cell IIICS fibronectin mRNA in vitro." European Respiratory Journal 9, no. 3 (1996): 549–55. http://dx.doi.org/10.1183/09031936.96.09030549.

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De Candia, L. M., and R. J. Rodgers. "Characterization of the expression of the alternative splicing of the ED-A, ED-B and V regions of fibronectin mRNA in bovine ovarian follicles and corpora lutea." Reproduction, Fertility and Development 11, no. 6 (1999): 367. http://dx.doi.org/10.1071/rd99087.

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Fibronectin is an extracellular matrix glycoprotein. Alternative splicing of fibronectin mRNA within three specific regions, the extra domains (ED) A and B and the variable (V) or IIICS region, result in the production of different isoforms of fibronectin. These isoforms differentially regulate tissue developmental processes, such as those occurring during follicular and luteal development. The specific isoforms of fibronectin present in follicles and corpora lutea have not been identified. To identify these, primers for reverse transcription polymerase chain reaction (RT-PCR) were designed to

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Moursi, A. M., C. H. Damsky, J. Lull, et al. "Fibronectin regulates calvarial osteoblast differentiation." Journal of Cell Science 109, no. 6 (1996): 1369–80. http://dx.doi.org/10.1242/jcs.109.6.1369.

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The secretion of fibronectin by differentiating osteoblasts and its accumulation at sites of osteogenesis suggest that fibronectin participates in bone formation. To test this directly, we determined whether fibronectin-cell interactions regulate progressive differentiation of cultured fetal rat calvarial osteoblasts. Spatial distributions of alpha 5 integrin subunit, fibronectin, osteopontin (bone sialoprotein I) and osteocalcin (bone Gla-protein) were similar in fetal rat calvaria and mineralized, bone-like nodules formed by cultured osteoblasts. Addition of anti-fibronectin antibodies to cu

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de Groot, C. J., V. A. Chao, J. M. Roberts, and R. N. Taylor. "Human endothelial cell morphology and autacoid expression." American Journal of Physiology-Heart and Circulatory Physiology 268, no. 4 (1995): H1613—H1620. http://dx.doi.org/10.1152/ajpheart.1995.268.4.h1613.

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Human umbilical vein endothelial (HUVE) cells plated on plastic or gelatin-coated dishes grow as a “cobblestone” monolayer. By contrast, endothelial cells cultured on a complex matrix (e.g., Matrigel) form three-dimensional, capillary-like structures. In the current study, we verified the capillary phenotype of the latter structures and asked whether the morphological changes induced by extracellular matrix also affect human endothelial gene expression and function in vitro. Concentrations of cellular fibronectin, prostacyclin, and endothelin-1 were measured in the conditioned media by enzyme-

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Venu, Vivek Krishna Pulakazhi, Patrizia Uboldi, Ashish Dhyani, et al. "Fibronectin extra domain A stabilises atherosclerotic plaques in apolipoprotein E and in LDL-receptor-deficient mice." Thrombosis and Haemostasis 114, no. 07 (2015): 186–97. http://dx.doi.org/10.1160/th14-09-0790.

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SummaryThe primary transcript of fibronectin undergoes alternative splicing in the cassette-type EDA and EDB exons and in the IIICs segment to generate different protein isoforms. Human carotid atherosclerotic plaques with a more stable phenotype are enriched with EDA containing fibronectin (FN-EDA). The aim of this study was to investigate the role of EDA containing fibronectin during atherogenesis. Mice constitutively expressing or lacking the EDA domain of fibronectin (EDA+/+ or EDA-/-) were crossed with ApoE-/- or LDL-R-/- mice and fed with a western type diet for 12 weeks. Lack of FN-EDA

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Dissertations / Theses on the topic "Expression human fibronectin IIICS mRNA"

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Hershberger, Richard Paul. "Regulation of expression of alternatively-spliced human fibronectin IIICS mRNA variants." Case Western Reserve University School of Graduate Studies / OhioLINK, 1991. http://rave.ohiolink.edu/etdc/view?acc_num=case1055863527.

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Conference papers on the topic "Expression human fibronectin IIICS mRNA"

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Uzan, G., A. Lajmanovich, M. H. Prandini, Ph Frachet, A. Duperray, and G. Marguerie. "MOLECULAR CLONING OF PLATELET GPIIb FROM HEL CELLS AND HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643960.

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Platelet GP IIb-IIIa is an heterodimer which functions as a receptor for fibrinogen, fibronectin and Von Willebrand factor and is implicated in platelet adhesive reactions. To study the structure function relationship of this glycoprotein, a recombinant DNA approach was initiated. cDNA expression libraries were constructed in » gtll vector, from erythro-leukemia cells (HEL) and megakaryocytes mRNA. The human megakaryocytes were isolated from patients with chronic myeloid leukemia. The HEL library was initially screened with polyclonal antibodies anti GPIIb IIIa. One clone, λIIbI, containing a

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Marquerie, G., A. Duperray, G. Uzan, and R. Berthier. "BIOSYNTHETIC PATHWAYS OF THE PLATELET FIBRINOGEN RECEPTOR IN HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642954.

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Interaction between cells and between cells and extracellular matrices are critical for a number of biological processes, including organ development, cell differenciation, cell motility, and the inimune' response. These interactions are mediated by a family of adhesion receptors that recognize short sequences such as Arg-Gly-Asp (RGD). These receptors share similar structural properties. They are heterodimers composed of a and B subunits and sometime express common epitopes. This suggests that the structural and functional relationship of these receptors may result from the transcription of r

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LOFTUS, J. C., E. F. Plow, A. L. Frelinger III, M. A. Smith, S. D’ouza, and M. H. Ginsberg. "LOCALIZATION AND CHEMICAL SYNTHESIS OF A DIVALENT CATION REGULATED EPITOPE IN PLATELET MEMBRANE GPIIb." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643959.

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Platelet membrane glycoprotein (GP)IIb-IIIa is a component of a common adhesive protein receptor for fibrinogen, fibronectin, and von Willebrand factor. A monoclonal antibody, PMI-1, defines a divalent cation dependent regulation of the surface orientation of the heavy chain of GPIIb. Exposure of the PMI-1 epitope inversely correlates with the capacity of platelets to bind fibrinogen and aggregate. We have now localized and chemically synthesized this epitope. A 1.1 Kb cDNA clone which directs the synthesis of a fusion protein which bears the PMI-1 epitope was isolated from a lambda gt 11 expr

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