Spectroscopic evidence for site-specific cellular activity in the tubular gland in human intestine

2002 ◽  
Vol 30 (8) ◽  
pp. 612-616 ◽  
Author(s):  
Jagannathan Ramesh, Shmuel Argov, Ahmad Salman,
Keyword(s):  
Human Intestine ◽  
Cellular Activity ◽  
Site Specific ◽  
Spectroscopic Evidence ◽  
Tubular Gland

Laser microdissection as a new tool to investigate site-specific gene expression in enteric ganglia of the human intestine

2010 ◽  
Vol 22 (2) ◽  
pp. 168-e52 ◽  
Author(s):  
m. böttner ◽  
f. bär ◽  
h. von koschitzky ◽  
k. tafazzoli ◽  
u. j. roblick ◽  
...  
Keyword(s):  
Gene Expression ◽  
Laser Microdissection ◽  
Specific Gene ◽  
Human Intestine ◽  
Site Specific ◽  
Specific Gene Expression ◽  
Enteric Ganglia

Nitroreductase-Mediated Release of Inhibitors of Lysine-Specific Demethylase 1 (LSD1) from Prodrugs in Transfected Acute Myeloid Leukaemia Cells

2019 ◽  
Author(s):  
Manfred Jung ◽  
Eva-Maria Herrlinger ◽  
Mirjam Hau ◽  
Desiree M. Redhaber ◽  
Gabriele Greve ◽  
...  
Keyword(s):  
Acute Myeloid Leukaemia ◽  
Myeloid Leukaemia ◽  
Specific Inhibition ◽  
Cellular Activity ◽  
Wild Type ◽  
Site Specific ◽  
Lysine Specific Demethylase ◽  
Organ Type ◽  
Promising Therapeutic Target ◽  
Acute Myeloid

Lysine-specific demethylase 1 (LSD1) has evolved as a promising therapeutic target for cancer treatment, especially in acute myeloid leukaemia (AML). To approach the challenge of site-specific LSD1 inhibition, we developed an enzyme-prodrug system with the bacterial nitroreductase NfsB (NTR) that was expressed in the virally transfected AML cell line THP1-NTR+. The cellular activity of the NTR was proven with a new luminescent NTR probe. We synthesised a diverse set of nitroaromatic prodrugs that by design do not affect LSD1 and are reduced by the NTR to release an active LSD1 inhibitor. The 2-nitroimidazolyl prodrug (1f) of a potent LSD1 inhibitor emerged as one of the best prodrug candidates with a pronounced selectivity window between wild-type and transfected NTR+ cells. Our prodrugs are selectively activated and release the LSD1 inhibitor locally in turn blocking colony formation. This system may be applied in future targeting approaches to reach tissue- or organ-type-specific inhibition of LSD1.<br>

scholarly journals Site-specific conjugation of drug-like fragments to an antimiR scaffold as a strategy to target miRNAs inside RISC

2016 ◽  
Vol 52 (1) ◽  
pp. 156-159 ◽  
Author(s):  
A. Brunschweiger ◽  
L. F. R. Gebert ◽  
M. Lucic ◽  
U. Pradère ◽  
H. Jahns ◽  
...  
Keyword(s):  
Dependent Manner ◽  
Cellular Activity ◽  
Site Specific

We synthesized a miR-122 antimiR library in which drug-like fragments were site-specifically introduced. This affected cellular activity in a position-dependent manner.

Nitroreductase-Mediated Release of Inhibitors of Lysine-Specific Demethylase 1 (LSD1) from Prodrugs in Transfected Acute Myeloid Leukaemia Cells

2019 ◽  
Author(s):  
Manfred Jung ◽  
Eva-Maria Herrlinger ◽  
Mirjam Hau ◽  
Desiree M. Redhaber ◽  
Gabriele Greve ◽  
...  
Keyword(s):  
Acute Myeloid Leukaemia ◽  
Myeloid Leukaemia ◽  
Specific Inhibition ◽  
Cellular Activity ◽  
Wild Type ◽  
Site Specific ◽  
Lysine Specific Demethylase ◽  
Organ Type ◽  
Promising Therapeutic Target ◽  
Acute Myeloid

Lysine-specific demethylase 1 (LSD1) has evolved as a promising therapeutic target for cancer treatment, especially in acute myeloid leukaemia (AML). To approach the challenge of site-specific LSD1 inhibition, we developed an enzyme-prodrug system with the bacterial nitroreductase NfsB (NTR) that was expressed in the virally transfected AML cell line THP1-NTR+. The cellular activity of the NTR was proven with a new luminescent NTR probe. We synthesised a diverse set of nitroaromatic prodrugs that by design do not affect LSD1 and are reduced by the NTR to release an active LSD1 inhibitor. The 2-nitroimidazolyl prodrug (1f) of a potent LSD1 inhibitor emerged as one of the best prodrug candidates with a pronounced selectivity window between wild-type and transfected NTR+ cells. Our prodrugs are selectively activated and release the LSD1 inhibitor locally in turn blocking colony formation. This system may be applied in future targeting approaches to reach tissue- or organ-type-specific inhibition of LSD1.<br>

Spectroscopic Evidence for Site Specific Chemistry at a Unique Iron Site of the [4Fe−4S] Cluster in Ferredoxin:Thioredoxin Reductase

2003 ◽  
Vol 125 (5) ◽  
pp. 1146-1147 ◽  
Author(s):  
Guy N. L. Jameson ◽  
Elizabeth M. Walters ◽  
Wanda Manieri ◽  
Peter Schürmann ◽  
Michael K. Johnson ◽  
...  
Keyword(s):  
Iron Site ◽  
Site Specific ◽  
Spectroscopic Evidence ◽  
Ferredoxin:Thioredoxin Reductase

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The effects of Cyclosporin-A (CYA) on the Ultrastructure of Gingival Mast Cells (GMC) in Behcet's disease (BD)

1990 ◽  
Vol 48 (3) ◽  
pp. 358-359
Author(s):  
Oktay Arda ◽  
Ulkü Noyan ◽  
Selgçk Yilmaz ◽  
Mustafa Taşyürekli ◽  
İsmail Seçkin ◽  
...  
Keyword(s):  
Unknown Etiology ◽  
Control Group ◽  
Target Cells ◽  
Gingival Hyperplasia ◽  
Cellular Activity ◽  
Direct Relation ◽  
Immune Disease ◽  
Genital Ulceration ◽  
Functional Changes ◽  
The Third

Turkish dermatologist, H. Beheet described the disease as recurrent triad of iritis, oral aphthous lesions and genital ulceration. Auto immune disease is the recent focus on the unknown etiology which is still being discussed. Among the other immunosupressive drugs, CyA included in it's treatment newly. One of the important side effects of this drug is gingival hyperplasia which has a direct relation with the presence of teeth and periodontal tissue. We are interested in the ultrastructure of immunocompetent target cells that were affected by CyA in BD.Three groups arranged in each having 5 patients with BD. Control group was the first and didn’t have CyA treatment. Patients who had CyA, but didn’t show gingival hyperplasia assembled the second group. The ones displaying gingival hyperplasia following CyA therapy formed the third group. GMC of control group and their granules are shown in FIG. 1,2,3. GMC of the second group presented initiation of supplementary cellular activity and possible maturing functional changes with the signs of increased number of mitochondria and accumulation of numerous dense cored granules next to few normal ones, FIG. 4,5,6.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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