scholarly journals Biochemical Studies on the Mode of Action of Cytochalasin B

1974 ◽  
Vol 249 (18) ◽  
pp. 5778-5783
Author(s):  
Shin Lin ◽  
James A. Spudich
Keyword(s):  
Mode Of Action ◽  
Cytochalasin B ◽  
Biochemical Studies

scholarly journals Biochemical Studies on the Mode of Action of Cytochalasin B

1974 ◽  
Vol 249 (7) ◽  
pp. 2268-2274 ◽  
Author(s):  
Shin Lin ◽  
Daniel V. Santi ◽  
James A. Spudich
Keyword(s):  
Mode Of Action ◽  
Cytochalasin B ◽  
Biochemical Studies

scholarly journals Degradation of connective tissue matrices by macrophages. III. Morphological and biochemical studies on extracellular, pericellular, and intracellular events in matrix proteolysis by macrophages in culture.

1980 ◽  
Vol 152 (6) ◽  
pp. 1537-1553 ◽  
Author(s):  
Z Werb ◽  
D F Bainton ◽  
P A Jones
Keyword(s):  
Connective Tissue ◽  
Cytochalasin B ◽  
Proteinase Inhibitors ◽  
Ultrastructural Observation ◽  
Elastin Degradation ◽  
Biochemical Studies ◽  
Inflammatory Stimuli ◽  
The Matrix ◽  
Inflammatory Macrophages

We have shown that macrophages in culture degrade the glycoproteins and amorphous elastin of insoluble extracellular matrices. Ultrastructural observation of the macrophage-matrix interaction revealed that connective tissue macromolecules were solubilized from the matrix extracellularly. At least part of the matrix breakdown was localized to the immediate vicinity of the cells, as shown by morphological and biochemical studies, although the rate of degradation correlated closely with the secretion of proteinases by various inflammatory stimuli in vivo, by glucocorticoids, prostaglandin E2 or colchicine, or by phagocytosis of latex, zymosan, or cholesterol-albumin complexes in culture was reflected in altered rates of glycoprotein and elastin degradation by the macrophages. Alteration of endocytosis and lysosomal digestion by cytochalasin B, NH4Cl, and proteinase inhibitors did not decrease the overall rate of matrix solubilization, but reduced the processing of the matrix fragments to peptides. Therefore, extracellular, pericellular, and lysosomal events each contribute to degradation of extracellular matrix macromolecules by inflammatory macrophages.

scholarly journals Biochemical Studies on the Mode of Action of Pyrethroidal Insecticides

1968 ◽  
Vol 32 (5) ◽  
pp. 628-640 ◽  
Author(s):  
Junshi MIYAMOTO ◽  
Yoshishige SATO ◽  
Kimiko YAMAMOTO ◽  
Michio ENDO ◽  
Shin-ichi SUZUKI
Keyword(s):  
Mode Of Action ◽  
Biochemical Studies

A Model for The Mode of Action of Cytochalasin B Inhibition of D-Glucose Transport in the Human Erythrocyte

1975 ◽  
Vol 53 (10) ◽  
pp. 1078-1084 ◽  
Author(s):  
N. F. Taylor ◽  
G. L. Gagneja
Keyword(s):  
Glucose Transport ◽  
Human Erythrocyte ◽  
Mode Of Action ◽  
Cytochalasin B ◽  
Transport Model ◽  
Molecular Model ◽  
Competitive Inhibitor ◽  
Carrier Protein ◽  
Human Erythrocyte Membrane ◽  
Competitive Inhibitors

By an optical method, cytochalasin B is shown to be a competitive inhibitor of D-glucose transport across the human erythrocyte membrane with Ki of 1.2 × 10−7 M. A Drieding molecular model of cytochalasin B reveals an almost identical spatial distribution of four oxygen atoms to those found in the C1-conformation of β-D-glucopyranose and implicated in hydrogen bonding to the carrier protein associated with D-glucose transport. The stereochemistry of this transport model is discussed.On the basis of the interoxygen distances found in cytochalasin B, hydrocortisone, prednisolone, corticosterone, and phenolphthalein are considered as analogues and are shown to be competitive inhibitors of D-glucose transport with Ki values of 2.2 × 10−4 M, 3.0 × 10−4 M, 4.0 × 10−4 M, and 2.5 × 10−5 M, respectively. These results are considered to be consistent with the proposed mode of action of cytochalasin B and also provide further support for the model of D-glucose stereospecifically hydrogen-bonded to a carrier protein.

scholarly journals Effects of cytochalasin B on membrane-associated microfilaments in a cell-free system.

1981 ◽  
Vol 91 (2) ◽  
pp. 524-530 ◽  
Author(s):  
M J Phillips ◽  
M Oda ◽  
I M Yousef ◽  
K Funatsu
Keyword(s):  
Molecular Weight ◽  
Plasma Membrane ◽  
Rat Liver ◽  
Mode Of Action ◽  
Actin Filaments ◽  
Cytochalasin B ◽  
Bile Canaliculus ◽  
Free System ◽  
A Cell

The mode of action of cytochalasin B was examined in vitro using bile canaliculus-enriched plasma membrane fractions isolated from rat liver. The pericanalicular microfilaments, which are mainly actin filaments and which are normally attached to the canalicular membranes, were dissociated from the membranes by cytochalasin B treatment. A microfilamentous network was found in the supernate of the cytochalasin B treatment. A microfilamentous network was found in the supernate of the cytochalasin-treated specimens and a number of polypeptides, of which a polypeptide corresponding in molecular weight to actin was a notable member. These results suggest that actin filaments become detached from the canaliculus membranes by cytochalasin B.

Biochemical Studies on the Mode of Action of Pyrethroidal Insecticides

1968 ◽  
Vol 32 (5) ◽  
pp. 628-640 ◽  
Author(s):  
Junshi Miyamoto ◽  
Yoshishige Sato ◽  
Kimiko Yamamoto ◽  
Michio Endo ◽  
Shin-ichi Suzuki
Keyword(s):  
Mode Of Action ◽  
Biochemical Studies

Effects of 5-5'-Diphenyl-2-thiohydantoin (DPTH) and Thyroxine on the Ultrastructure and Chemical Composition of Rat Liver

1971 ◽  
Vol 29 ◽  
pp. 570-571
Author(s):  
E. A. Elfont ◽  
R. B. Tobin ◽  
D. G. Colton ◽  
M. A. Mehlman
Keyword(s):  
Chemical Composition ◽  
Rat Liver ◽  
Future Study ◽  
Mode Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Effective Inhibitor ◽  
Biochemical Effects ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

Summary5,-5'-diphenyl-2-thiohydantoin (DPTH) is an effective inhibitor of thyroxine (T4) stimulation of α-glycerophosphate dehydrogenase in rat liver mitochondria. Because this finding indicated a possible tool for future study of the mode of action of thyroxine, the ultrastructural and biochemical effects of DPTH and/or thyroxine on rat liver mere investigated.Rats were fed either standard or DPTH (0.06%) diet for 30 days before T4 (250 ug/kg/day) was injected. Injection of T4 occurred daily for 10 days prior to sacrifice. After removal of the liver and kidneys, part of the tissue was frozen at -50°C for later biocheailcal analyses, while the rest was prefixed in buffered 3.5X glutaraldehyde (390 mOs) and post-fixed in buffered 1Z OsO4 (376 mOs). Tissues were embedded in Araldlte 502 and the sections examined in a Zeiss EM 9S.Hepatocytes from hyperthyroid rats (Fig. 2) demonstrated enlarged and more numerous mitochondria than those of controls (Fig. 1). Glycogen was almost totally absent from the cytoplasm of the T4-treated rats.

Ruthenium Red Staining of Human Hard Keratin Fibers

1982 ◽  
Vol 40 ◽  
pp. 278-279
Author(s):  
M. C. Buhrer ◽  
R. A. Mathews
Keyword(s):  
Human Hair ◽  
Ruthenium Red ◽  
Acid Mucopolysaccharides ◽  
Biochemical Studies ◽  
Keratin Fibers ◽  
Ruthenium Red Staining ◽  
Extracellular Materials

Ruthenium red has been used as a stain to demonstrate a variety of extracellular materials, especially acid mucopolysaccharides. It also reacts with certain intracellular and extracellular lipids. Since biochemical studies in our laboratory demonstrated the presence of a variety of monosaccharides in human hair ruthenium red staining procedures were adopted in order to evaluate the presence and morphological location of acid oligosaccharides in the keratinized aspect of hair.

Effects of Hypophysectomy on the Fine Structure of Rat Liver Cells

1967 ◽  
Vol 25 ◽  
pp. 156-157
Author(s):  
Robert R. Cardell
Keyword(s):  
Electron Microscopy ◽  
Fine Structure ◽  
Rat Liver ◽  
Liver Cell ◽  
Anterior Pituitary ◽  
Liver Cells ◽  
Biochemical Studies ◽  
Liver Functions ◽  
Rat Liver Cells ◽  
And Control

Hypophysectomy of the rat renders this animal deficient in the hormones of the anterior pituitary gland, thus causing many primary and secondary hormonal effects on basic liver functions. Biochemical studies of these alterations in the rat liver cell are quite extensive; however, relatively few morphological observations on such cells have been recorded. Because the available biochemical information was derived mostly from disrupted and fractionated liver cells, it seemed desirable to examine the problem with the techniques of electron microscopy in order to see what changes are apparent in the intact liver cell after hypophysectomy. Accordingly, liver cells from rats which had been hypophysectomized 5-120 days before sacrifice were studied. Sham-operated rats served as controls and both hypophysectomized and control rats were fasted 15 hours before sacrifice.

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