scholarly journals ENZYME HISTOCHEMISTRY OF BONE INDUCTION BY URINARY BLADDER EPITHELIUM

1965 ◽  
Vol 13 (4) ◽  
pp. 255-264 ◽  
Author(s):  
SHOHEI KAGAWA
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Urinary Bladder ◽  
Intermediate Layer ◽  
Succinic Dehydrogenase ◽  
Basal Layer ◽  
Oxidative Enzymes ◽  
Bladder Epithelium ◽  
Malic Dehydrogenase ◽  
Normal Bladder

Homogenous transplants of urinary bladder mucosa were made in guinea pigs, and induced bone formation was observed histochemically for alkaline phosphatase, acid phosphatase, esterase, β-glucuronidase, aminopeptidase, and oxidative enzymes, i.e., succinic dehydrogenase, diphosphopyridine nucleotide-dependent dehydrogenase (lactate, malate, glutamate, α-glycerophosphate, β-hydroxybutyrate) and triphosphopyridine nucleotide-dependent dehydrogenase (glucose-6-phosphate and isocitrate). Normal urinary bladder epithelium contained intense alkaline phosphatase and slight acid phosphatase activity throughout. There was weak esterase activity in intermediate layer and weak β-glucuronidase activity in intermediate layer. Succinic dehydrogenase was present throughout the epithelium, and was most active in the basal layer. Lactic and malic dehydrogenase activities were intense. Glutamic, α-glycerophosphate and β-hydroxybutyric dehydrogenase activities were low, but glucose-6-phosphate and isocitric dehydrogenase activities were high. In the initial stage after transplantation, alkaline phosphatase, aminopeptidase and lactic dehydrogenase appeared in the connective tissue surrounding the transplanted mucosa in association with an inflammatory infiltration. Epithelial transplants formed cysts. Lactic, malic and triphosphopyridine nucleotide-dependent dehydrogenases in cystic epithelium were as intense as in normal bladder, though other enzymes decreased. Hyaline formation occurred around the cyst. No appreciable enzyme activity was demonstrated in this hyalinized portion, but when bone appeared marked activity of alkaline and acid phosphatases was seen around it. Histochemical patterns in the induced bone were essentially the same as in normal bone.

A Histological and Histochemical Study of the Brown and Yellow Adipose Tissue of the Bat, Hipposideros speoris

1959 ◽  
Vol s3-100 (51) ◽  
pp. 369-375
Author(s):  
J. C. GEORGE ◽  
J. EAPEN
Keyword(s):  
Alkaline Phosphatase ◽  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Histological Structure ◽  
Brown Adipose ◽  
Aldehydes And Ketones ◽  
Sulphydryl Groups

A study of the histology and histochemical reactions for lipase, alkaline phosphatase, acid phosphatase, adenosine triphosphatase, succinic dehydrogenase, lactic dehydrogenase, phospholipids, cholesterol, sulphydryl groups, and water-insoluble aldehydes and ketones in the brown and yellow adipose tissue of the bat (Hipposideros speoris) revealed that the two types of adipose tissue differ in histological structure as well as physiological activity. The histological structure of the two types of adipose tissue was found to be different, resembling that of the two corresponding types of the rat. The brown adipose tissue showed a higher concentration of succinic dehydrogenase, lactic dehydrogenase, phospholipids, cholesterol, and sulphydryl groups. No detectable difference between brown and yellow adipose tissue was, however, found with respect to lipase, alkaline phosphatase, acid phosphatase, adenosine triphosphatase, and water-insoluble aldehydes and ketones.

scholarly journals A HISTOCHEMICAL STUDY OF PHAGOCYTIC AND ENZYMATIC FUNCTIONS OF RABBIT MONONUCLEAR AND POLYMORPHONUCLEAR EXUDATE CELLS AND ALVEOLAR MACROPHAGES

1963 ◽  
Vol 17 (3) ◽  
pp. 465-486 ◽  
Author(s):  
Arthur M. Dannenberg ◽  
Marvin S. Burstone ◽  
Paul C. Walter ◽  
June W. Kinsley
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Alveolar Macrophages ◽  
Histochemical Study ◽  
Succinic Dehydrogenase ◽  
Enzymatic Activities ◽  
Dust Particles ◽  
Cell Type ◽  
Microbial Agents

The cytochrome oxidase (CO), aminopeptidase (AMP), succinic dehydrogenase (SD), acid phosphatase, esterase, and alkaline phosphatase of rabbit mononuclear (MN) and polymorphonuclear (PMN) peritoneal exudate cells and pulmonary alveolar macrophages (AM) - air dried on Mylar strips - were characterized by histochemical techniques with respect to stability, activators, inhibitors, and pH optima. A granule count method was established for the quantitation of these enzymes. For the acid phosphatase of MN, in which the most precise results were obtained, time, pH, substrate, and inhibitor curves resembled those commonly obtained biochemically. Five of these enzymes were usually more active in AM than MN, whereas the sixth, alkaline phosphatase, was not present in either cell type. AM also tended to consume more oxygen than MN and to divide more frequently. Since the most active cells in the population would be first involved in the host's defense against microbial agents, a comparison was made of the 10 per cent of the AM and MN with the highest enzymatic activities. No differences were found in the granule counts that were not reflected by the means. However, within a given AM population, cells containing ingested dust particles seemed to have higher enzymatic activities than those without particles. MN had greater acid phosphatase and SD activities than PMN and consumed more oxygen, but the CO, AMP, and esterase activites of both types of cells were of similar magnitude. PMN showed high alkaline phosphatase activity; MN showed none. A survey of the histochemical literature indicates that a positive correlation between the enzymatic and phagocytic activities of both MN and PMN exists in vivo.

scholarly journals CYTOCHEMISTRY AND ELECTRON MICROSCOPY

1963 ◽  
Vol 17 (1) ◽  
pp. 19-58 ◽  
Author(s):  
David D. Sabatini ◽  
Klaus Bensch ◽  
Russell J. Barrnett
Keyword(s):  
Electron Microscopy ◽  
Alkaline Phosphatase ◽  
Fine Structure ◽  
Acid Phosphatase ◽  
Adenosine Triphosphatase ◽  
Osmium Tetroxide ◽  
Enzyme Histochemistry ◽  
Succinic Dehydrogenase ◽  
Optimal Conditions ◽  
Fixation Procedure

The aldehydes introduced in this paper and the more appropriate concentrations for their general use as fixatives are: 4 to 6.5 per cent glutaraldehyde, 4 per cent glyoxal, 12.5 per cent hydroxyadipaldehyde, 10 per cent crotonaldehyde, 5 per cent pyruvic aldehyde, 10 per cent acetaldehyde, and 5 per cent methacrolein. These were prepared as cacodylate- or phosphate-buffered solutions (0.1 to 0.2 M, pH 6.5 to 7.6) that, with the exception of glutaraldehyde, contained sucrose (0.22 to 0.55 M). After fixation of from 0.5 hour to 24 hours, the blocks were stored in cold (4°C) buffer (0.1 M) plus sucrose (0.22 M). This material was used for enzyme histochemistry, for electron microscopy (both with and without a second fixation with 1 or 2 per cent osmium tetroxide) after Epon embedding, and for the combination of the two techniques. After fixation in aldehyde, membranous differentiations of the cell were not apparent and the nuclear structure differed from that commonly observed with osmium tetroxide. A postfixation in osmium tetroxide, even after long periods of storage, developed an image that—notable in the case of glutaraldehyde—was largely indistinguishable from that of tissues fixed under optimal conditions with osmium tetroxide alone. Aliesterase, acetylcholinesterase, alkaline phosphatase, acid phosphatase, 5-nucleotidase, adenosine triphosphatase, and DPNH and TPNH diaphorase activities were demonstrable histochemically after most of the fixatives. Cytochrome oxidase, succinic dehydrogenase, and glucose-6-phosphatase were retained after hydroxyaldipaldehyde and, to a lesser extent, after glyoxal fixation. The final product of the activity of several of the above-mentioned enzymes was localized in relation to the fine structure. For this purpose the double fixation procedure was used, selecting in each case the appropriate aldehyde.

MORPHOLOGICAL AND GENETIC DIFFERENTIATION IN APHIDS (APHIDIDAE)

1981 ◽  
Vol 113 (6) ◽  
pp. 539-550 ◽  
Author(s):  
S. M. Singh ◽  
T. K. Cunningham
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Developmental Stages ◽  
Morphological Features ◽  
Malic Dehydrogenase ◽  
Enzyme Pattern ◽  
Parthenogenetic Reproduction ◽  
Host Plant Specificity ◽  
Leucine Alanine Peptidase ◽  
Phosphatase Alkaline

AbstractSix species of aphids belonging to four genera were measured for 12 morphological features at five developmental stages. It was concluded that reliable identification of species based on morphological features is possible only at adult stages. Samples were also analyzed for seven enzymes by gel electrophoresis. There were no enzyme pattern differences among developmental stages in any species. Three enzymes, malic dehydrogenase, malic enzyme and tetrazolium oxidase, showed the same band pattern in all species. The other four, acid phosphatase, alkaline phosphatase, esterase and leucine-alanine peptidase, showed “diagnostic” patterns specific to a given species. All species are easily identifiable by their esterase pattern which could be confirmed by acid phosphatase, alkaline phosphatase, and leucine-alanine peptidase patterns. The enzyme pattern differences were used to establish a dendrogram of genetic relationship among species which was compared with a dendrogram of morphological similarities. The close genetic similarity among species suggests that significant adaptive differentiation leading to speciation may have occurred within the context of relatively few genie changes. This is compatible with speciation in aphids being due primarily to their obligate parthenogenetic reproduction, frequent bottlenecks (drastic reduction in number), and host plant specificity.

scholarly journals HISTOCHEMICAL LOCALIZATION OF ENZYME ACTIVITY IN THE KIDNEYS OF THREE MAMMALIAN SPECIES DURING THEIR POSTNATAL DEVELOPMENT

1965 ◽  
Vol 13 (1) ◽  
pp. 44-56 ◽  
Author(s):  
MAX WACHSTEIN ◽  
MAIRE BRADSHAW
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Guinea Pig ◽  
Adenosine Triphosphatase ◽  
Rat Kidney ◽  
Single Cells ◽  
General Pattern ◽  
Succinic Dehydrogenase ◽  
Oxidative Enzymes ◽  
Adenosine Triphosphatase Activity

The activities of various enzymes were studied histochemically in two species which at birth have a kidney with an active nephrogenic zone, the rat and rabbit, and one (the guinea pig) in which this organ is at this time apparently fully matured. The histochemical reactions, in general, reflect the degree of maturity found in kidneys of newborn and growing animals. Immature proximal convoluted tubules lack enzymatic activity or show only minimal amounts. As these tubules mature, the adult pattern is noted at about the 14th to 16th day after birth in rat, and after 21 to 28 days in rabbit. Within this general pattern, however, considerable variations are noted. Glucose-6-phosphatase, e.g., is less active at birth, even in mature tubules, while acid phosphatase localized in granular "lysosomal" bodies is as prominent in newborn kidney as in adult. Newborn guinea pig kidney lacks glomerular adenosine triphosphatase activity in spite of its general enzymatic maturity, while rat kidney at birth has no tubular adenosine triphosphatase activity, even in more mature proximal convolutions. Oxidative enzymes, particularly succinic dehydrogenase, and acid phosphatase are active in tubules of the inner portion of medulla in rat and rabbit at birth. This appears to be an expression of the immaturity of newborn kidney. With the progress of zonal differentiation, this enzyme activity is no longer found in the papillary portion of medulla where thin limbs of Henle's loop are now located. In rat kidney, best seen in cryostat sections briefly postfixed in very cold neutral formalin, single cells are found in the collecting ducts with striking 5-nucleotidase activity. The number of these cells is greater in neonatal kidney than in adult kidney. The physiological significance of many of the findings described in this report has still to be clarified.

scholarly journals HISTOCHEMICAL LOCALIZATION OF CERTAIN OXIDATIVE ENZYMES IN THE RAT TESTIS

1964 ◽  
Vol 12 (8) ◽  
pp. 587-590 ◽  
Author(s):  
P. M. AMBADKAR ◽  
J. C. GEORGE
Keyword(s):  
Enzyme Activity ◽  
Distribution Pattern ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Oxidative Enzymes ◽  
Metabolic Adaptation ◽  
Seminiferous Tubules ◽  
Malic Dehydrogenase ◽  
Rat Testis ◽  
Subcellular Level

The localization and distribution of β-hydroxybutyrate dehydrogenase, succinic dehydrogenase, malic dehydrogenase, and lactic dehydrogenase in the rat testis have been studied histochemically. Intense enzyme activity in the interstitium as well as tubules was observed. However, malic dehydrogenase was found to be more active in the interstitium than in the tubules. The distribution pattern of enzyme activity appeared in four different phases in the seminiferous tubules corresponding to the gradient in the spermatogenetic wave, thereby indicating a metabolic adaptation at subcellular level.

Epithelial Changes in Porcine Exudative Epidermitis

1968 ◽  
Vol 5 (3) ◽  
pp. 253-269 ◽  
Author(s):  
Anna-Lisa Obel
Keyword(s):  
Alkaline Phosphatase ◽  
Lactic Acid ◽  
Acid Phosphatase ◽  
Succinic Dehydrogenase ◽  
Transitional Zone ◽  
Resistant Material ◽  
Cutaneous Lesions ◽  
Viral Origin ◽  
Cytoplasmic Rna ◽  
Stratum Spinosum

The cutaneous lesions in 25 spontaneous cases of porcine exudative epidermitis (EE) were studied. During the first 4 days mild acanthosis, increase of cytoplasmic RNA, enlarged nucleoli, and intercellular oedema in the stratum spinosum with formation of vesicles occur. A PAS-positive, diastase-resistant material accumulates in the stratum intermedium. The keratohyaline granules disappear and parakeratotic horn containing abundant protein-bound SH-groups and lipids is produced. Beyond 4 days duration acanthosis and the formation of parakeratotic horn with microabscesses are increased. During healing keratohyaline granules reappear and the formation of normal horn cells is resumed. Acid phosphatase and succinic dehydrogenase are increased in the parakeratotic horn. Lactic acid dehydrogenase is increased in the transitional zone and alkaline phosphatase in the stratum basale. The observations indicate inhibition in the stratum intermedium of the differentiation of epithelial cells to horny cells. The disease is believed to be of viral origin.

Initial effects of cyclophosphamide on urinary bladder epithelium in the rat

Pathology ◽  
1974 ◽  
Vol 6 (4) ◽  
pp. 343-350 ◽  
Author(s):  
Mary E. Schultz ◽  
Michael W. Weldon
Keyword(s):  
Urinary Bladder ◽  
Bladder Epithelium
Sign in / Sign up

Export Citation Format

Share Document