Functional heterogeneity in the myenter is plexus: Demonstration using cytochrome oxidase as a verified cytochemical probe of the activity of individual enteric neurons

1986 ◽  
Vol 249 (3) ◽  
pp. 381-391 ◽  
Author(s):  
Gary M. Mawe ◽  
Michael D. Gershon
Keyword(s):  
Cytochrome Oxidase ◽  
Enteric Neurons ◽  
Functional Heterogeneity

scholarly journals Classification of human enteric neurons

2021 ◽  
Author(s):  
Axel Brehmer
Keyword(s):  
Enteric Neurons ◽  
Morphological Data ◽  
Type I ◽  
Type Ii ◽  
Functional Heterogeneity ◽  
Structural Investigations ◽  
Innovative Methods ◽  
Further Development ◽  
Dogiel Type Ii

AbstractMajor advances in our understanding of the functional heterogeneity of enteric neurons are driven by the application of newly developed, innovative methods. In contrast to this progress, both animal and human enteric neurons are usually divided into only two morphological subpopulations, “Dogiel type II” neurons (with several long processes) and “Dogiel type I” neurons (with several short processes). This implies no more than the distinction of intrinsic primary afferent from all other enteric neurons. The well-known chemical and functional diversity of enteric neurons is not reflected by this restrictive dichotomy of morphological data. Recent structural investigations of human enteric neurons were performed by different groups which mainly used two methodical approaches, namely detecting the architecture of their processes and target-specific tracing of their axonal courses. Both methods were combined with multiple immunohistochemistry in order to decipher neurochemical codes. This review integrates these morphological and immunohistological data and presents a classification of human enteric neurons which we believe is not yet complete but provides an essential foundation for the further development of human gastrointestinal neuropathology.

Initial Polymerization Sites Indicated During Mitochondrial Oxidation of Diaminobenzidine after Toluene Treatment

1977 ◽  
Vol 35 ◽  
pp. 408-409
Author(s):  
W. A. Shannon ◽  
M. A. Matlib
Keyword(s):  
Membrane Permeability ◽  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Precise Definition ◽  
Cytochemical Localization ◽  
Oxidative Reaction ◽  
Mitochondrial Oxidation ◽  
Definition Of ◽  
Exogenous Substrates

Numerous studies have dealt with the cytochemical localization of cytochrome oxidase via cytochrome c. More recent studies have dealt with indicating initial foci of this reaction by altering incubation pH (1) or postosmication procedure (2,3). The following study is an attempt to locate such foci by altering membrane permeability. It is thought that such alterations within the limits of maintaining morphological integrity of the membranes will ease the entry of exogenous substrates resulting in a much quicker oxidation and subsequently a more precise definition of the oxidative reaction.The diaminobenzidine (DAB) method of Seligman et al. (4) was used. Minced pieces of rat liver were incubated for 1 hr following toluene treatment (5,6). Experimental variations consisted of incubating fixed or unfixed tissues treated with toluene and unfixed tissues treated with toluene and subsequently fixed.

O activation in cytochrome oxidase and in other heme proteins

1992 ◽  
Vol 1101 (2) ◽  
pp. 192-194
Author(s):  
G BABCOCK ◽  
C VAROTSIS ◽  
Y ZHANG
Keyword(s):  
Cytochrome Oxidase ◽  
Heme Proteins

Transient cytochrome oxidase deficiency with Ohtahara syndrome

2000 ◽  
Vol 42 (11) ◽  
pp. 785-786 ◽  
Author(s):  
Cathy Higgins ◽  
George Gray ◽  
Pramila Ramani ◽  
Kelvin Poulton ◽  
William Whitehouse
Keyword(s):  
Cytochrome Oxidase ◽  
Oxidase Deficiency ◽  
Ohtahara Syndrome

First record of body colour polymorphism in giant African snail Achatina fulica (Bowdich, 1822) - a comparative study using mitochondrial cytochrome oxidase subunit I (COI) gene

ENTOMON ◽  
2019 ◽  
Vol 44 (2) ◽  
pp. 155-160
Author(s):  
Keerthy Vijayan ◽  
R. Sugantha Sakthivel ◽  
T.V. Sajeev
Keyword(s):  
Cytochrome Oxidase ◽  
South India ◽  
The Body ◽  
Colour Polymorphism ◽  
Coi Gene ◽  
Body Colour ◽  
Cytochrome Oxidase Subunit ◽  
Cytochrome Oxidase Subunit I ◽  
Black And White ◽  
Oxidase Subunit

The presence of the body colour polymorphism in the tropical invasive pest giant African snail is reported for the first time from South India. Three different body colour polymorphs were recognised viz. grey, black and white. The grey body colour is the most common polymorph. The black and white colour polymorphs are found to be in almost equal proportions in the reported localities with the grey counterparts. The cytochrome oxidase subunit I (COI) sequences of the three colour polymorphs are found to be identical. The presence of the body colour polymorphism in south India may be attributed to the avian predation and other selection pressures.

FUNCTIONAL HETEROGENEITY OF THE THYROID AND POSSIBLE PRESENCE OF IODOTYROSINE-LIKE COMPOUNDS IN NORMAL SERUM

1965 ◽  
Vol 48 (2) ◽  
pp. 199-208 ◽  
Author(s):  
J. D. Wiener
Keyword(s):  
Human Subjects ◽  
Thyroid Tissue ◽  
Normal Serum ◽  
Schematic Model ◽  
Functional Heterogeneity ◽  
Rat Serum ◽  
Iodine Metabolism ◽  
Normal Rat ◽  
Isotope Equilibrium ◽  
Equilibrium Experiment

ABSTRACT After the administration of 131I to normal animals or human subjects, labelled thyroxine and triiodothyronine, but at most traces of labelled iodotyrosines can be detected in the serum. However, several investigators using various methods claim to have found considerable amounts of one or both of these iodotyrosines when assaying the stable (non-radioactive) iodinated compounds in the serum. Considering the available evidence as convincing for the present, an attempt has been made to explain this discrepancy. A schematic model of the thyroidal iodine metabolism is proposed, based on (a) the hypothesis that the iodotyrosines are present in the circulation in a »masked« form (i. e. protected against deiodination), and (b) the known functional heterogeneity of the thyroid tissue. This heterogeneity should be of a qualitative as well as quantitative nature. As the physical decay rate of 131I is short in comparison with the turnover rate of the masked iodotyrosine pool, an isotope equilibrium experiment with rats was carried out, using the long-lived isotope 125I. The results of this experiment, viewed together with those of a similar investigation published by others, seem to lend support to the proposed mechanism. The presence of non-negligible amounts of a diiodotyrosine-like compound in normal rat serum seems fairly well established.

Cytochrome Oxidase Activity at The Hepatic Parenchyma Different Periods of Ischemia and Obstructive Jaundice

2019 ◽  
Vol 9 (5) ◽  
pp. p8944
Author(s):  
Askarov Tahir Askarovich ◽  
Akhmedov Mirhalil Dzhalilovich ◽  
Fayziev Yokub Nishanovic ◽  
Ashurmetov Ahmadjon Makhamadjonovich ◽  
Dalimov Kenjabek Sabutaevich ◽  
...  
Keyword(s):  
Obstructive Jaundice ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Hepatic Parenchyma ◽  
Cytochrome Oxidase Activity
Sign in / Sign up

Export Citation Format

Share Document