scholarly journals Incorporation of [3H]leucine into an actin-like protein in response to 1,25-dihydroxycholecalciferol in chick intestinal brush borders

1978 ◽  
Vol 173 (2) ◽  
pp. 627-631 ◽  
Author(s):  
P W Wilson ◽  
D E M Lawson
Keyword(s):  
Isoelectric Focusing ◽  
Salt Solution ◽  
Gel Electrophoresis ◽  
Brush Borders ◽  
Mucosal Cells ◽  
Intestinal Mucosal Cells

1,25-Dihydroxycholecalciferol very rapidly stimulates the incorporation of [4,5-3H]leucine into at least two proteins of the chick intestinal mucosal cells. The smaller of the two proteins has mol.wt. approx. 42000, very similar to actin. Other properties of this protein were investigated, including its solubility in salt solution and its behaviour on gel electrophoresis and isoelectric focusing, and in all cases the 1,25-dihydroxycholecalciferol-stimulated protein was indistinguishable from intestinal actin. It was also shown that the brush borders of mucosal cells contain both beta- and gamma-actin in approximately equal amounts and that both forms of the protein appear to be affected by the hormone. It is concluded therefore that one of the earliest actions of 1,25-dihydroxycholecalciferol is to stimulate the incorporation of leucine into beta- and gamma-actin of the mucosal cells or into two proteins very like them.

scholarly journals Identification of albumin as the plasma carrier for zinc absorption by perfused rat intestine

1979 ◽  
Vol 184 (3) ◽  
pp. 627-633 ◽  
Author(s):  
K T Smith ◽  
M L Failla ◽  
R J Cousins
Keyword(s):  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Serum Zinc ◽  
Zinc Binding ◽  
Zinc Absorption ◽  
Rat Intestine ◽  
Protein Carrier ◽  
Mucosal Cells ◽  
Intestinal Mucosal Cells ◽  
Blue Sepharose

The isolated vascularly perfused rat intestine exhibits an obligatory need for a protein carrier in order to absorb zinc. Therefore this system is ideal for use as a model to identify the plasma carrier during zinc absorption. Affinity chromatography on Blue Sepharose CL-6B was employed to separate the major serum zinc-binding proteins in the portal effluent of the perfused intestine. It was found that 94% of newly absorbed 65Zn was transported in the portal serum-containing perfusate as an albumin-65Zn complex. The identity of albumin as the plasma carrier was confirmed by polyacrylamide-slab-gel electrophoresis. This evidence suggests that albumin is the plasma protein that is involved in removal of zinc from intestinal-mucosal cells and subsequent transport of the metal in portal blood to the liver.

Bacterial-Mucosal Cell Junctional Complexes

1974 ◽  
Vol 32 ◽  
pp. 144-145
Author(s):  
Roger C. Wagner
Keyword(s):  
Intestinal Wall ◽  
Rat Colon ◽  
Mucosal Cell ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Mucosal Cells ◽  
Mucosal Lining ◽  
Degenerative Alterations ◽  
Junctional Complexes ◽  
Intestinal Mucosal Cells

Bacteria exhibit the ability to adhere to the apical surfaces of intestinal mucosal cells. These attachments either precede invasion of the intestinal wall by the bacteria with accompanying inflammation and degeneration of the mucosa or represent permanent anchoring sites where the bacteria never totally penetrate the mucosal cells.Endemic gram negative bacteria were found attached to the surface of mucosal cells lining the walls of crypts in the rat colon. The bacteria did not intrude deeper than 0.5 urn into the mucosal cells and no degenerative alterations were detectable in the mucosal lining.

Fine Structural Localization of Acyltransferases Involved in Lipid Synthesis in Intestinal Mucosa.

1970 ◽  
Vol 28 ◽  
pp. 54-55
Author(s):  
R. J. Barrnett ◽  
J. A. Higgins
Keyword(s):  
Smooth Endoplasmic Reticulum ◽  
Lipid Synthesis ◽  
Mucosal Cell ◽  
Structural Localization ◽  
Morphological Studies ◽  
Mucosal Cells ◽  
Initial Appearance ◽  
Sh Group ◽  
Hydrolysis Of ◽  
Intestinal Mucosal Cells

The main products of intestinal hydrolysis of dietary triglycerides are free fatty acids and monoglycerides. These form micelles from which the lipids are absorbed across the mucosal cell brush border. Biochemical studies have indicated that intestinal mucosal cells possess a triglyceride synthesising system, which uses monoglyceride directly as an acylacceptor as well as the system found in other tissues in which alphaglycerophosphate is the acylacceptor. The former pathway is used preferentially for the resynthesis of triglyceride from absorbed lipid, while the latter is used mainly for phospholipid synthesis. Both lipids are incorporated into chylomicrons. Morphological studies have shown that during fat absorption there is an initial appearance of fat droplets within the cisternae of the smooth endoplasmic reticulum and that these subsequently accumulate in the golgi elements from which they are released at the lateral borders of the cell as chylomicrons.We have recently developed several methods for the fine structural localization of acyltransferases dependent on the precipitation, in an electron dense form, of CoA released during the transfer of the acyl group to an acceptor, and have now applied these methods to a study of the fine structural localization of the enzymes involved in chylomicron lipid biosynthesis. These methods are based on the reduction of ferricyanide ions by the free SH group of CoA.

Gel Electrophoresis, Isoelectric Focusing, and Localization of Thymidine Kinase in Normal and Simian Virus 40-Infected Monkey Cells

Intervirology ◽  
1973 ◽  
Vol 2 (3) ◽  
pp. 137-151 ◽  
Author(s):  
Saul Kit ◽  
Wai-Choi Leung ◽  
David Trkula ◽  
Del Rose Dubbs ◽  
George Jorgensen
Keyword(s):  
Thymidine Kinase ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Infected Monkey

Purification of Human Urokinase and its Topographical Localisation in Renal Parenchyma

1975 ◽  
Author(s):  
K. Andrassy ◽  
E. Ritz ◽  
U. Bleyl ◽  
R. Egbring
Keyword(s):  
Molecular Weight ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Renal Tissue ◽  
Clot Lysis ◽  
Agar Gel ◽  
High Molecular Weight Complex ◽  
Zone Electrophoresis ◽  
Human Serum Proteins

Urokinase Leo was separated by agar zone electrophoresis into an anodic and cathodic fraction. The cathodic fraction, isolated from agar gel by ultracentrifugation, showed two precipitation bands with rabbit Urokinase antibodies. Band I displayed main Urokinase activity, in band II Urokinase was present in a high molecular weight complex with human serum proteins (albumin, a2-macroglobulin, a2HS glycoprotein); with affinity chromatography further separation of Urokinase isoenzymes from serum proteins was possible. The isoelectric point of these two Urokinase isoenzymes were pH 6.8 and pH 8.7 respectively in preliminary results with isoelectric focusing. Purification steps were controlled by disc gel electrophoresis and immunological techniques (Ouchterlony technique, Immunoelectrophoresis, clot lysis test with Urokinase antibodies).Topographic localisation of Urokinase in renal tissue, investigated with antibodies against Urokinase isoenzymes, revealed Urokinase activity both in the iuxtamedullary region (V. arcuatae, V. interlobulares, less V. recta) and in calyceal epithelia of the renal pelvis.

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