Cat3, a third gene locus coding for a tissue-specific catalase in maize: Genetics, intracellular location, and some biochemical properties

1980 ◽  
Vol 179 (1) ◽  
pp. 33-41 ◽  
Author(s):  
John G. Scandalios ◽  
Wu-Fu Tong ◽  
Demetrios G. Roupakias
Keyword(s):  
Gene Locus ◽  
Biochemical Properties ◽  
Intracellular Location ◽  
Tissue Specific ◽  
Maize Genetics

scholarly journals Multiple tissue-specific elements control the apolipoprotein E/C-I gene locus in transgenic mice

1991 ◽  
Vol 266 (14) ◽  
pp. 8651-8654 ◽  
Author(s):  
W.S. Simonet ◽  
N. Bucay ◽  
R.E. Pitas ◽  
S.J. Lauer ◽  
J.M. Taylor
Keyword(s):  
Transgenic Mice ◽  
Apolipoprotein E ◽  
Gene Locus ◽  
Tissue Specific ◽  
I Gene

scholarly journals Predictable activation of tissue-specific expression from a single gene locus using the pOp/LhG4 transactivation system in Arabidopsis

2004 ◽  
Vol 3 (1) ◽  
pp. 91-101 ◽  
Author(s):  
Célia Baroux ◽  
Robert Blanvillain ◽  
Hazel Betts ◽  
Henri Batoko ◽  
Judith Craft ◽  
...  
Keyword(s):  
Gene Locus ◽  
Single Gene ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression

Identification of distal regulatory regions in the human αIIb gene locus necessary for consistent, high-level megakaryocyte expression

Blood ◽  
2002 ◽  
Vol 100 (10) ◽  
pp. 3588-3596 ◽  
Author(s):  
Michael A. Thornton ◽  
Chunyan Zhang ◽  
Maria A. Kowalska ◽  
Mortimer Poncz
Keyword(s):  
Gene Locus ◽  
Tissue Specificity ◽  
Mrna Level ◽  
Regulatory Elements ◽  
Proximal Promoter ◽  
Regulatory Regions ◽  
Platelet Surface ◽  
Tissue Specific ◽  
Intergenic Regions ◽  
High Level

The αIIb/β3-integrin receptor is present at high levels only in megakaryocytes and platelets. Its presence on platelets is critical for hemostasis. The tissue-specific nature of this receptor's expression is secondary to the restricted expression of αIIb, and studies of the αIIb proximal promoter have served as a model of a megakaryocyte-specific promoter. We have examined the αIIb gene locus for distal regulatory elements. Sequence comparison between the human (h) and murine (m) αIIb loci revealed high levels of conservation at intergenic regions both 5′ and 3′ to the αIIb gene. Additionally, deoxyribonuclease (DNase) I sensitivity mapping defined tissue-specific hypersensitive (HS) sites that coincide, in part, with these conserved regions. Transgenic mice containing various lengths of the hαIIb gene locus, which included or excluded the various conserved/HS regions, demonstrated that the proximal promoter was sufficient for tissue specificity, but that a region 2.5 to 7.1 kb upstream of the hαIIb gene was necessary for consistent expression. Another region 2.2 to 7.4 kb downstream of the gene enhanced expression 1000-fold and led to levels of hαIIb mRNA that were about 30% of the native mαIIb mRNA level. These constructs also resulted in detectable hαIIb/mβ3 on the platelet surface. This work not only confirms the importance of the proximal promoter of the αIIb gene for tissue specificity, but also characterizes the distal organization of the αIIb gene locus and provides an initial localization of 2 important regulatory regions needed for the expression of the αIIb gene at high levels during megakaryopoiesis.

scholarly journals Septin functions in organ system physiology and pathology

2014 ◽  
Vol 395 (2) ◽  
pp. 123-141 ◽  
Author(s):  
Lee Dolat ◽  
Qicong Hu ◽  
Elias T. Spiliotis
Keyword(s):  
Biochemical Properties ◽  
Organ System ◽  
Protein Isoforms ◽  
Biological Functions ◽  
Tissue Specific ◽  
Gtp Binding ◽  
Organ Systems ◽  
System Physiology ◽  
And Function ◽  
Made In

Abstract Human septins comprise a family of 13 genes that encode for >30 protein isoforms with ubiquitous and tissue-specific expressions. Septins are GTP-binding proteins that assemble into higher-order oligomers and filamentous polymers, which associate with cell membranes and the cytoskeleton. In the last decade, much progress has been made in understanding the biochemical properties and cell biological functions of septins. In parallel, a growing number of studies show that septins play important roles for the development and physiology of specific tissues and organs. Here, we review the expression and function of septins in the cardiovascular, immune, nervous, urinary, digestive, respiratory, endocrine, reproductive, and integumentary organ systems. Furthermore, we discuss how the tissue-specific functions of septins relate to the pathology of human diseases that arise from aberrations in septin expression.

scholarly journals Neuronal protein NP185 in avian and murine cerebellum: expression during development and evidence for its presence in nerve endings.

1991 ◽  
Vol 39 (11) ◽  
pp. 1461-1470 ◽  
Author(s):  
D G Perry ◽  
V Hanson ◽  
M L Benuck ◽  
S Puszkin
Keyword(s):  
Monoclonal Antibody ◽  
Neural Tissue ◽  
Specific Protein ◽  
Biochemical Properties ◽  
Coated Vesicles ◽  
Nerve Endings ◽  
Tissue Specific ◽  
Neuronal Protein ◽  
Mature Neurons

The neuronal protein NP185 is a neural tissue-specific protein isolated from clathrin-coated vesicles in brain. Using 8G8, a monoclonal antibody (MAb) characterized in our laboratory, we studied the expression and distribution of neuronal protein NP185 in developing avian cerebellum and in mature murine cerebellum. Furthermore, we compared these parameters to that of synapse-specific neuronal protein, synaptophysin, and an axon-specific (i.e., non-synaptic) neuronal protein, neurofilament NF68. We found that NP185 expression temporally and spatially corresponds to avian cerebellar synaptogenesis. In addition, NP185 distribution parallels synaptophysin distribution throughout development, while differing from that of either unassembled or filamentous forms of NF68. The evidence also suggests that embryonic NP185 expression coincides with synaptogenesis, and that NP185 remains concentrated in the terminal boutons of mature neurons. The synapse specificity of NP185 and the recent biochemical properties reported for this protein support the postulate that this molecule may trigger synaptic events and distinguish structurally and functionally active synapses.

scholarly journals Modification of isolation methods and physico-biochemical properties of preparations of fungal oxidoreductases

2020 ◽  
Vol 11 (2) ◽  
pp. 310-314
Author(s):  
O. V. Fedotov ◽  
Z. L. Usikova
Keyword(s):  
Amino Acids ◽  
Lentinula Edodes ◽  
Gel Filtration ◽  
Amino Acid Content ◽  
Toxicity Testing ◽  
Culture Fluid ◽  
Biochemical Properties ◽  
Individual Characteristics ◽  
Intracellular Location ◽  
Enzyme Preparations

The results of the modification of methods for producing enzymatic preparations (EP) of peroxidases and catalases of extra- and intracellular finding from fungal cultures are presented. Strains of Flammulina velutipes F-vv, Lentinula edodes 523 and Pleurotus ostreatus P-01 were used as producers of oxidoreductases. The producers were cultured in glucose-peptone medium, modified for each strain. Protein fractionation was carried out by leaching with ammonium sulfate at a saturation of 40–70% for peroxidases and 80% for catalases. The obtained solutions of protein fractions were additionally subjected to purification by dialysis, gel filtration on Molselect G-50 and G-75 granules, and also freeze drying. The yield of enzymatic preparations per unit mass of mycelium and the volume of culture fluid were calculated. The individual characteristics of EP – enzymatic activity, the mass percentage of protein and associated amino acids, the ratio of the latter in groups depending on the nature of the radicals (amphotericity) of protein molecules are established. It was proved that the amino acid content in the proteins of fungal EP catalases and peroxidases indicates their acidic nature and this is confirmed by the pH values of aqueous solutions. Examination and toxicity testing of enzymatic preparations were carried out in certified laboratories, which confirmed their characteristics and compliance with safety requirements. The therapeutic properties of amino acids that are part of proteins or are in a free state in enzyme preparations are analyzed. In this way, the methods have been developed for producing enzymatic preparations of peroxidases and catalases of extra- and intracellular location, which allow new antioxidant enzymes with individual properties to be obtained, and, as a result, bring prospects for use in various industries and scientific research.

scholarly journals NATF (Native And Tissue-specific Fluorescence): A strategy for bright, tissue-specific GFP labeling of native proteins

2018 ◽  
Author(s):  
Siwei He ◽  
Andrea Cuentas-Condori ◽  
David M. Miller
Keyword(s):  
Cell Types ◽  
Specific Protein ◽  
Target Protein ◽  
Specific Cell ◽  
Genomic Locus ◽  
Intracellular Location ◽  
Tissue Specific ◽  
Specific Fluorescence ◽  
C Elegans ◽  
Native Proteins

ABSTRACTGFP labeling by genome editing can reveal the authentic location of a native protein but is frequently hampered by weak GFP signals and broad expression across a range cell types in multicellular animals. To overcome these problems, we engineered a Native And Tissue-specific Fluorescence (NATF) strategy which combines CRISPR/Cas-9 and split-GFP to yield bright, cell-specific protein labeling. We use CRISPR/Cas9 to insert a tandem array of seven copies of the GFP11 β-strand (gfp11x7) at the genomic locus of each target protein. The resultant gfp11x7 knock-in strain is then crossed with separate reporter lines that express the complementing split-GFP fragment (gfp1-10) in specific cell types thus affording tissue-specific labeling of the target protein at its native level. We show that NATF reveals the otherwise undetectable intracellular location of the immunoglobulin protein, OIG-1, and demarcates a receptor auxiliary protein LEV-10 at cell-specific synaptic domains in the C. elegans nervous system.

Prerequisites for tissue specific and position independent expression of a gene locus in transgenic mice

1996 ◽  
Vol 74 (11) ◽  
pp. 663-671 ◽  
Author(s):  
C. Bonifer ◽  
M. C. Huber ◽  
U. Jägle ◽  
N. Faust ◽  
A. E. Sippel
Keyword(s):  
Transgenic Mice ◽  
Gene Locus ◽  
Tissue Specific

scholarly journals Modification of isolation methods and physico-biochemical properties of preparations of fungal oxidoreductases

2020 ◽  
Vol 11 (2) ◽  
pp. 310-314
Author(s):  
O. V. Fedotov ◽  
Z. L. Usikova
Keyword(s):  
Amino Acids ◽  
Lentinula Edodes ◽  
Gel Filtration ◽  
Amino Acid Content ◽  
Toxicity Testing ◽  
Culture Fluid ◽  
Biochemical Properties ◽  
Individual Characteristics ◽  
Intracellular Location ◽  
Enzyme Preparations

The results of the modification of methods for producing enzymatic preparations (EP) of peroxidases and catalases of extra- and intracellular finding from fungal cultures are presented. Strains of Flammulina velutipes F-vv, Lentinula edodes 523 and Pleurotus ostreatus P-01 were used as producers of oxidoreductases. The producers were cultured in glucose-peptone medium, modified for each strain. Protein fractionation was carried out by leaching with ammonium sulfate at a saturation of 40–70% for peroxidases and 80% for catalases. The obtained solutions of protein fractions were additionally subjected to purification by dialysis, gel filtration on Molselect G-50 and G-75 granules, and also freeze drying. The yield of enzymatic preparations per unit mass of mycelium and the volume of culture fluid were calculated. The individual characteristics of EP – enzymatic activity, the mass percentage of protein and associated amino acids, the ratio of the latter in groups depending on the nature of the radicals (amphotericity) of protein molecules are established. It was proved that the amino acid content in the proteins of fungal EP catalases and peroxidases indicates their acidic nature and this is confirmed by the pH values of aqueous solutions. Examination and toxicity testing of enzymatic preparations were carried out in certified laboratories, which confirmed their characteristics and compliance with safety requirements. The therapeutic properties of amino acids that are part of proteins or are in a free state in enzyme preparations are analyzed. In this way, the methods have been developed for producing enzymatic preparations of peroxidases and catalases of extra- and intracellular location, which allow new antioxidant enzymes with individual properties to be obtained, and, as a result, bring prospects for use in various industries and scientific research.

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