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.

Histochemical distribution of succinic dehydrogenase in the lymphatic system of a trematode Ceylonocotyle scoliocoelium

1978 ◽  
Vol 52 (2) ◽  
pp. 159-162 ◽  
Author(s):  
P. N. Sharma
Keyword(s):  
Enzyme Activity ◽  
Distribution Pattern ◽  
Succinate Dehydrogenase ◽  
Lymphatic System ◽  
Succinic Dehydrogenase ◽  
First Report

ABSTRACTHistochemical observations have been made on the localization and distribution pattern of succinate dehydrogenase (SDH) in the lymphatic system of Ceylonocotyle scoliocoelium by employing tetrazolium nitro BT. The enzyme activity appeared in the form of diformazon granules which are believed to consist of mitochondrial aggregates. It is further suggested that this enzyme helps in the transportation of the metabolites. This is the first report of SDH in the lymph channels involving transportation.

DISTRIBUTION PATTERNS OF OXIDATIVE ENZYMES IN EXPERIMENTALLY INDUCED TUMORS, REGENERATION AND INFLAMMATION OF MOUSE SKIN

1966 ◽  
Vol 14 (1) ◽  
pp. 84-93 ◽  
Author(s):  
TAKENORI HASHIMOTO ◽  
M. S. BURSTONE
Keyword(s):  
Distribution Pattern ◽  
Succinic Dehydrogenase ◽  
Mouse Skin ◽  
Distribution Patterns ◽  
Early Embryo ◽  
Oxidative Enzymes ◽  
Polarization Pattern ◽  
Induced Tumors ◽  
Enzyme Distribution ◽  
Well Differentiated

Enzyme histochemical studies of normal and burned mouse skin as well as those treated with methylcholanthrene or 2,4-dinitro-1-chlorobenzene revealed that the irritant (or stimulus) carcinogenic or noncarcinogenic, initially results in a more distinct polarization2 of the localization of oxidative enzymes including glucose 6-phosphate dehydrogenase (predominant in the upper layers of the hypertrophic epidermis) and DPN-dependent dehydrogenases, succinic dehydrogenase and cytochrome oxidase in the lower layers. Subsequently, only the carcinogen disrupted the polarization pattern. Methylcholanthrene-induced squamous cell carcinomas were classified from a histochemical standpoint according to the following three types: (1) those well differentiated and having a distinctly polarized pattern of oxidative enzymes; (2) those showing disruption of the polarization pattern and marked activity of oxidative enzymes; and (3) those that were undifferentiated and characterized by absence of a polarized pattern and weak activity of oxidative enzymes. Type 1 showed an enzyme distribution pattern resembling that of the inflammatory hypertrophic epidermis; type 2 was similar in enzymatic pattern to the advancing proximal portion of the regenerating epidermis; and type 3 was similar enzyme-histochemically to the undifferentiated epithelium of the early embryo skin. Thus, a great variation in the distribution pattern of enzyme activities appears during the carcinogenesis process.

THE ACTIVITY OF ENZYMES IN THE RABBIT UTERUS AND EFFECT OF PROGESTERONE AND OESTRADIOL

1969 ◽  
Vol 43 (2) ◽  
pp. 167-174 ◽  
Author(s):  
R. N. MURDOCH ◽  
I. G. WHITE
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Glutamate Oxaloacetate Transaminase ◽  
Oestrogen Treatment ◽  
Uterine Endometrium ◽  
Uterine Fluid ◽  
Activity Of Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

SUMMARY The activity of several enzymes has been measured in the uterine endometrium of the rabbit during oestrus and pseudopregnancy and after injecting oestradiol benzoate or progesterone 28 days after ovariectomy. The enzyme activity of the uterine fluid has been determined during oestrus and the effect of uterine ligation studied. Progesterone and the induction of pseudopregnancy stimulated succinic dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (GDH) activity and depressed amylase and lactic dehydrogenase (LDH) activity. In ovariectomized does, glutamate-oxaloacetate transaminase (GOT) activity increased after the injection of progesterone. Progesterone also stimulated endometrial phosphatase after ovariectomy but, when given after a period of oestrogen treatment, it limited the even greater response of acid and alkaline phosphatase to oestrogen; the activity then attaining the same level as when progesterone alone was given. SDH, GDH and glycerylphosphorylcholine (GPC) diesterase could not be detected in uterine fluid but amylase and alkaline phosphatase were in greater concentration than in the endometrium. GPC diesterase was, however, found to be present in uterine tissue. Ligation of the uterus did not significantly alter the enzyme activity of the endometrium.

scholarly journals The Effect of Cryptorchidism on the Quantitative Histology, Histochemistry and Hydrolytic Enzyme Activity of the Rat Testis

1978 ◽  
Vol 31 (1) ◽  
pp. 53 ◽  
Author(s):  
AW Blackshaw ◽  
PF Massey
Keyword(s):  
Enzyme Activity ◽  
Meiotic Prophase ◽  
Hydrolytic Enzyme ◽  
Seminiferous Tubules ◽  
Quantitative Histology ◽  
Rat Testis ◽  
Germinal Cells ◽  
Enzyme Patterns

Cryptorchidism of the mature rat testis led to degeneration of the seminiferous tubules and changes in enzyme patterns and activities. Spermatogenic stages 1--4, containing pachytene primary spermatocytes in late meiotic prophase, and stage 5, containing recently formed round spermatids, were damaged by 48 h. Within 96 h stages showed a loss of germinal cells into the lumen and this was almost complete by 192 h.

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.

scholarly journals Histochemical fiber typing and staining intensity in cat and rat muscles.

1975 ◽  
Vol 23 (6) ◽  
pp. 395-401 ◽  
Author(s):  
H Schmalbruch ◽  
Z Kamieniecka
Keyword(s):  
Gastrocnemius Muscle ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Staining Intensity ◽  
Oxidative Enzymes ◽  
Type I ◽  
Fiber Types ◽  
Glycerophosphate Dehydrogenase ◽  
C Fibers ◽  
Type I Fibers

In the gastrocnemius muscle of cat and rat, staining for oxidative enzymes differentiated three fiber types (A,B,C) and staining for adenosine triphosphate at pH 9.4 differentiated two fiber types (I, II) with a reliability of 90% and 98%, respectively. In cat 96% and in rat 90% of the fibers were typed identically after staining for nicotinamide adenine dinucleotidelinked lactic dehydrogenase (LDH) and succinic dehydrogenase (SDH). When differentiated by staining for LDH, A and B fibers were of type I. IN RAT, 80-90% OF ALL FIBERS WERE OF TYPE 22, COMPPRISING A, B and C fibers. Type I fibers stained for LDH intensely as did C fibers of type II, but stained intermediately for SDH. The degree of staining was measured by photometry. When fibers were stained for LDH, histograms of density showed three peaks corresponding to A, B and C fibers in cat, but only two peaks corresponding to A and C fibers in rat, In cat and rat, the densities of A, B and C fibers belonged to different populations. In soleus muscle of cat and rat stained for LDH, menadione-linked alpha-glycerophosphate dehydrogenase and adenosine triphosphatase at pH 9.4, the degree of staining differed from thatin any type of fiber in gastrocnemius muscle

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.

Steroidogenic enzyme activity in the rat testis following Leydig cell destruction by ethylene-1,2-dimethanesulphonate and during subsequent Leydig cell regeneration

1991 ◽  
Vol 131 (3) ◽  
pp. 451-457 ◽  
Author(s):  
P. J. O'Shaughnessy ◽  
L. Murphy
Keyword(s):  
Enzyme Activity ◽  
Leydig Cell ◽  
Leydig Cells ◽  
Seminiferous Tubules ◽  
Cell Regeneration ◽  
Significant Activity ◽  
Steroidogenic Enzyme ◽  
Control Activity ◽  
Rat Testis ◽  
Cell Destruction

ABSTRACT Ethylene-1,2-dimethanesulphonate (EDS) rapidly destroys Leydig cells in the rat testis, although repopulation occurs within 5–7 weeks. In this study we have examined the activity of testicular steroidogenic enzymes after Leydig cell destruction and during regeneration. This was designed to measure the contribution of cells, other than Leydig cells, to steroidogenic activity in the testis, and to determine whether changes in steroidogenic enzyme activity during Leydig cell regeneration after EDS parallel those which occur during normal Leydig cell development. The enzymes studied are those responsible for androgen synthesis and metabolism in the testis. Adult male Wistar rats (300–350 g) were injected with EDS (100 mg/kg, i.p.) and testicular steroidogenic enzyme activity was measured on days 0, 3, 7, 14, 21 and 35. On day 3, when no Leydig cells remain in the testis, cholesterol side-chain cleavage (CSCC) activity, per testis, declined to undetectable levels, while 3βhydroxysteroid dehydrogenase (3βHSD) and 17α-hydroxylase retained only 0·04 and 0·15% of control activity respectively. In contrast, 17-ketosteroid reductase (17-KSR) and 5α-reductase retained 33 and 10% of control activity respectively. On day 7 there was a further loss of 17-KSR activity (to 20% of control) but no change in other enzymes. The 17-KSR activity remaining on day 7 after EDS was contained almost exclusively in the seminiferous tubules, while the low 3β-HSD activity remaining was confined largely to the interstitial tissue. Other enzymes showed a more even distribution between the two compartments. On day 14 after EDS there was a tenfold increase in 3β-HSD activity (compared with day 7), with no change in CSCC, 17α-hydroxylase or 5α-reductase and a further loss of 17-KSR (to 11% of control). Between days 14 and 21 there were marked increases in the activities of CSCC, 3β-HSD, and 17α-hydroxylase, while 17-KSR showed no change in activity from day 14. Activity of 5α-reductase increased between days 14 and 21 to levels greater than those seen in control animals. By day 35 the activities of all enzymes had returned to control levels. The results show that, in the adult rat testis, the activities of CSCC, 3β-HSD and 17α-hydroxylase are confined, almost entirely, to the Leydig cells, and only 17-KSR shows significant activity in another cell type. During regeneration of Leydig cells after EDS the pattern of changes in enzyme activity is very similar to that seen in the normal development of the adult population of Leydig cells. Journal of Endocrinology (1991) 131, 451–457

Succinic and Malic Oxidase in Gastric Hydrochloric Acid Production

1956 ◽  
Vol 187 (3) ◽  
pp. 427-431 ◽  
Author(s):  
Joseph J. Vitale ◽  
Oscar M. Jankelson ◽  
Patricia Connors ◽  
D. Mark Hegsted ◽  
Norman Zamcheck
Keyword(s):  
Gastric Mucosa ◽  
Guinea Pig ◽  
Succinic Dehydrogenase ◽  
Titratable Acidity ◽  
Spectrophotometric Analysis ◽  
Parietal Cells ◽  
Human Gastric Mucosa ◽  
City Hospital ◽  
Malic Dehydrogenase ◽  
Oxidase System

Effect of histamine on the activity of succinic oxidase and malic dehydrogenase was studied in guinea pig and human gastric mucosa. Human tissue was obtained through the surgical services of the Boston City Hospital. Control value for the succinic oxidase system of the proximal half of the guinea pig stomach was approximately 480 ( Qo2 (N) (µl O2/mg nitrogen/hr.)). After histamine, this value rose to 550 in 30 minutes with a simultaneous rise in titratable acidity of the stomach contents. Animals fasted for 72 hours had a Qo2 (N) of approximately 500 and after histamine a Qo2 (N) of 700 was observed. Spectrophotometric analysis of succinic dehydrogenase and cytochrome oxidase activities, two of the major components of the succinic oxidase system, revealed that both components are increased following histamine administration. Malic dehydrogenase, however, was not affected by histamine treatment. Succinic dehydrogenase was demonstrated by histochemical localization and was concentrated below the superficial mucous layer where parietal cells were abundant. Succinic oxidase activity of human gastric mucosa was demonstrable only in those specimens containing abundant parietal cells. This study confirms the view that HCl production by parietal cells is associated with aerobic metabolism and is perhaps under enzymatic control. The study suggests that the succinic oxidase system may be involved in the production or secretion of HCl.

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