scholarly journals Role of the septate junction in the regulation of paracellular transepithelial flow.

1976 ◽  
Vol 71 (3) ◽  
pp. 967-972 ◽  
Author(s):  
B A Lord ◽  
D R DiBona
Keyword(s):  
Small Molecules ◽  
Structural Response ◽  
Water Soluble ◽  
Septate Junction ◽  
Toad Urinary Bladder ◽  
Transport Function ◽  
Septate Junctions ◽  
Small Water ◽  
Paracellular Flow

A comparison of the distribution of septate junctions in invertebrate epithelia and tight junctions in vertebrate systems suggests that these structures may be functionally analogous. This proposition is supported by the internal design of each junction which constitutes a serial arrangement of structures crossing the intercellular space between cells to effectively provide resistance to the paracellular flow of water and small molecules. We have tested the validity of such an analogy by examining whether the osmotic sensitivity of the septate junctions of planarian epidermis follow the rather striking pattern observed for the junctions of very tight vertebrate epithelia (e.g. toad urinary bladder). It has been found that the septate junctions in this system respond in similar fashion to their vertebrate counterparts, blistering with accumulated fluid when the medium outside the epidermis is made hypertonic with small, water-soluble molecules. We conclude that the two types of junction probably are functionally analogous and that, in each case, this rectified structural response to transepithelial osmotic gradients may be indicative of the role of such structures in the transport function of epithelia.

Role of PKC isozymes in water transport in toad urinary bladder

1991 ◽  
Vol 49 ◽  
pp. 302-303
Author(s):  
A.J. Mia ◽  
L.X. Oakford ◽  
T. Yorio
Keyword(s):  
Urinary Bladder ◽  
Apical Membrane ◽  
Membrane Surface ◽  
Protein A ◽  
Cell Types ◽  
Leukemic Cells ◽  
Toad Urinary Bladder ◽  
Pkc Isozymes ◽  
Antibody Labeling

Protein kinase C (PKC) isozymes, when activated, are translocated to particulate membrane fractions for transport to the apical membrane surface in a variety of cell types. Evidence of PKC translocation was demonstrated in human megakaryoblastic leukemic cells, and in cardiac myocytes and fibroblasts, using FTTC immunofluorescent antibody labeling techniques. Recently, we reported immunogold localizations of PKC subtypes I and II in toad urinary bladder epithelia, following 60 min stimulation with Mezerein (MZ), a PKC activator, or antidiuretic hormone (ADH). Localization of isozyme subtypes I and n was carried out in separate grids using specific monoclonal antibodies with subsequent labeling with 20nm protein A-gold probes. Each PKC subtype was found to be distributed singularly and in discrete isolated patches in the cytosol as well as in the apical membrane domains. To determine if the PKC isozymes co-localized within the cell, a double immunogold labeling technique using single grids was utilized.

scholarly journals Did Cyclic Metaphosphates Have a Role in the Origin of Life?

2021 ◽  
Author(s):  
Thomas Glonek
Keyword(s):  
Organic Molecules ◽  
Water Soluble ◽  
Holliday Junction ◽  
Additional Energy ◽  
Condensed Phosphate ◽  
Geological Processes ◽  
The Origin Of Life ◽  
Complex Forms ◽  
Self Replication

AbstractHow life began still eludes science life, the initial progenote in the context presented herein, being a chemical aggregate of primordial inorganic and organic molecules capable of self-replication and evolution into ever increasingly complex forms and functions.Presented is a hypothesis that a mineral scaffold generated by geological processes and containing polymerized phosphate units was present in primordial seas that provided the initiating factor responsible for the sequestration and organization of primordial life’s constituents. Unlike previous hypotheses proposing phosphates as the essential initiating factor, the key phosphate described here is not a polynucleotide or just any condensed phosphate but a large (in the range of at least 1 kilo-phosphate subunits), water soluble, cyclic metaphosphate, which is a closed loop chain of polymerized inorganic phosphate residues containing only phosphate middle groups. The chain forms an intrinsic 4-phosphate helix analogous to its structure in Na Kurrol’s salt, and as with DNA, very large metaphosphates may fold into hairpin structures. Using a Holliday-junction-like scrambling mechanism, also analogous to DNA, rings may be manipulated (increased, decreased, exchanged) easily with little to no need for additional energy, the reaction being essentially an isomerization.A literature review is presented describing findings that support the above hypothesis. Reviewed is condensed phosphate inorganic chemistry including its geological origins, biological occurrence, enzymes and their genetics through eukaryotes, polyphosphate functions, circular polynucleotides and the role of the Holliday junction, previous biogenesis hypotheses, and an Eoarchean Era timeline.

The biological activity of glucagon–phospholipid complexes

1983 ◽  
Vol 61 (7) ◽  
pp. 688-691 ◽  
Author(s):  
J. J. Liepnieks ◽  
P. Stoskopf ◽  
E. A. Carrey ◽  
C. Prosser ◽  
R. M. Epand
Keyword(s):  
Biological Activity ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Bovine Brain ◽  
Water Soluble ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Dimyristoyl Phosphatidylcholine ◽  
Lipoprotein Complex ◽  
Stimulation Of

Glucagon can form water-soluble complexes with phospholipids. The incorporation of glucagon into these lipoprotein particles reduces the biological activity of the hormone. The effect is observed only at temperatures below the phase transition temperature of the phospholipid and results in a decreased stimulation of the adenylate cyclase of rat liver plasma membranes by the lipoprotein complex as compared with the hormone in free solution. Two- to five-fold higher concentrations of glucagon are required for half-maximal stimulation of adenylate cyclase when the hormone is complexed with dimyristoyl phosphatidylcholine, dipalmitoyl phosphatidylcholine, or bovine brain sphingomyelin. A possible role of lipoprotein-associated hormones in the development of insulin resistance is discussed.

scholarly journals Role of SpoVA Proteins in Release of Dipicolinic Acid during Germination of Bacillus subtilis Spores Triggered by Dodecylamine or Lysozyme

2006 ◽  
Vol 189 (5) ◽  
pp. 1565-1572 ◽  
Author(s):  
Venkata Ramana Vepachedu ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Small Molecules ◽  
Spore Germination ◽  
Dipicolinic Acid ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Ph Optimum ◽  
Inner Membrane ◽  
Temperature Sensitive Mutants

ABSTRACT The release of dipicolinic acid (DPA) during the germination of Bacillus subtilis spores by the cationic surfactant dodecylamine exhibited a pH optimum of ∼9 and a temperature optimum of 60°C. DPA release during dodecylamine germination of B. subtilis spores with fourfold-elevated levels of the SpoVA proteins that have been suggested to be involved in the release of DPA during nutrient germination was about fourfold faster than DPA release during dodecylamine germination of wild-type spores and was inhibited by HgCl2. Spores carrying temperature-sensitive mutants in the spoVA operon were also temperature sensitive in DPA release during dodecylamine germination as well as in lysozyme germination of decoated spores. In addition to DPA, dodecylamine triggered the release of amounts of Ca2+ almost equivalent to those of DPA, and at least one other abundant spore small molecule, glutamic acid, was released in parallel with Ca2+ and DPA. These data indicate that (i) dodecylamine triggers spore germination by opening a channel in the inner membrane for Ca2+-DPA and other small molecules, (ii) this channel is composed at least in part of proteins, and (iii) SpoVA proteins are involved in the release of Ca2+-DPA and other small molecules during spore germination, perhaps by being a part of a channel in the spore's inner membrane.

scholarly journals An Essential Role of the CAAT/Enhancer Binding Protein-α in the Vitamin D-Induced Expression of the Human Steroid/Bile Acid-Sulfotransferase (SULT2A1)

2006 ◽  
Vol 20 (4) ◽  
pp. 795-808 ◽  
Author(s):  
Chung S. Song ◽  
Ibtissam Echchgadda ◽  
Young-Kyo Seo ◽  
Taesung Oh ◽  
Soyoung Kim ◽  
...  
Keyword(s):  
Vitamin D ◽  
Binding Site ◽  
Essential Role ◽  
Binding Protein ◽  
Water Soluble ◽  
Induced Expression ◽  
Composite Element ◽  
Deoxyribonuclease I ◽  
Enhancer Binding Protein

Abstract The vitamin D receptor (VDR) regulates steroid and drug metabolism by inducing the genes encoding phase I and phase II enzymes. SULT2A1 is a liver- and intestine-expressed sulfo-conjugating enzyme that converts the alcohol-OH of neutral steroids, bile acids, and drugs to water-soluble sulfated metabolites. 1α,25-Dihydroxyvitamin D3 [1,25-(OH)2D3] induces SULT2A1 gene transcription after the recruitment of VDR to the vitamin D-responsive chromatin region of SULT2A1. A composite element in human SULT2A1 directs the 1,25-(OH)2D3-mediated induction of natural and heterologous promoters. This element combines a VDR/retinoid X receptor-α-binding site [vitamin D response element (VDRE)], which is an imperfect inverted repeat 2 of AGCTCA, and a CAAT/enhancer binding protein (C/EBP)-binding site located 9 bp downstream to VDRE. The binding sites were identified by EMSA, antibody supershift, and deoxyribonuclease I footprinting. C/EBP-α at the composite element plays an essential role in the VDR regulation of SULT2A1, because 1) induction was lost for promoters with inactivating mutations at the VDRE or C/EBP element; 2) SULT2A1 induction by 1,25-(OH)2D3 in C/EBP-α-deficient cells required the expression of cotransfected C/EBP-α; and 3) C/EBP-β did not substitute for C/EBP-α in this regulation. VDR and C/EBP-α were recruited concurrently to the composite element along with the coactivators p300, steroid receptor coactivator 1 (SRC-1), and SRC-2, but not SRC-3. VDR and C/EBP-α associated endogenously as a DNA-dependent, coimmunoprecipitable complex, which was detected at a markedly higher level in 1,25-(OH)2D3-treated cells. These results provide the first example of the essential role of the interaction in cis between C/EBP-α and VDR in directing 1,25-(OH)2D3-induced expression of a VDR target gene.

Topographical variations in the structure of the smooth septate junction

1979 ◽  
Vol 37 (1) ◽  
pp. 373-389
Author(s):  
H.B. Skaer ◽  
J.B. Harrison ◽  
W.M. Lee
Keyword(s):  
Musca Domestica ◽  
Functional Significance ◽  
Freeze Fracture ◽  
Rhodnius Prolixus ◽  
Malpighian Tubules ◽  
Septate Junction ◽  
Lanthanum Hydroxide ◽  
Septate Junctions ◽  
Standard Fixation

Smooth septate junctions in the midgut of Musca domestica and in Malpighian tubules of both Musca and Rhodnius prolixus are described. Details of the structures revealed after standard fixation, fixation in the presence of the stain, lanthanum hydroxide, and after freeze-fracture are discussed in the light of models previously put forward to explain the interrelations of the images obtained by these different methods. The organization of the junction between cells of the midgut varies in the apical-to-basal axis. At the apical border the septa (or ridges in freeze-fracture replicas) are packed tightly and follow an undulating but strictly parallel course. This packing loosens towards the middle of the junction until, at its basal extremity, the septa (ridges in replicas) are widely separated and follow independent meandering courses. That these features are found both in lanthanum-infiltrated specimens and freeze-fracture replicas allows a correlation to be made between the septa and the freeze-fracture ridges. The functional significance of these smooth septate junctions is discussed.

The Emerging Role of Nanosuspensions for Drug Delivery and Stability

2021 ◽  
Vol 12 ◽  
Author(s):  
Hitesh Kumar Dewangan
Keyword(s):  
Water Solubility ◽  
Size Range ◽  
Aqueous Solubility ◽  
Active Surface ◽  
Water Soluble ◽  
Active Surface Area ◽  
Specific Interest ◽  
Advanced Therapies ◽  
Processing Techniques

: Poor solubility of some medicinal compounds is a serious challenge that can be addressed by using a nano-suspension for improved delivery. The nanoparticles enhance the bioavailability along with the aqueous solubility of the drug, which is accomplished by increasing the active surface area of the drug. The gained attention of the nanosuspension is due to its stabilization facility, which is achieved by polymers, such as polyethylene glycol (PEG), having a particular size range of 10 - 100 nm. Hence, these nanoparticles have the capacity of binding to the targeted with very low damage to the healthy tissues. These are prepared by various methods, such as milling, high-pressure homogenization, and emulsification, along with melt emulsification. Moreover, surface modification and solidification have been used to add specific properties to the advanced therapies as post-processing techniques. For many decades, it has been known that water solubility hampers the bioavailability and not all drugs are water-soluble. In order to combat this obstacle, nanotechnology has been found to be of specific interest. For elevating the bioavailability by increasing the dissolution rate, the methodology of reduction of the associated drug particles into their subsequent submicron range is incorporated. For oral and non-oral administration, these nanosuspension formulations are used for the delivery of drugs.

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