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 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.

scholarly journals The Oleaginous Conglomerate- Multiple Symmetric Lipomatosis

2021 ◽  
pp. 1-6
Keyword(s):  
Adipose Tissue ◽  
Subcutaneous Tissue ◽  
Histological Structure ◽  
Thoracic Region ◽  
Metabolic Disturbances ◽  
Multiple Symmetric Lipomatosis ◽  
Brown Adipose ◽  
Simple Obesity ◽  
Upper Thoracic ◽  
Adipose Tissue Cells

Multiple symmetric lipomatosis (MSL) is an exceptional disorder of adipose tissue metabolism and lipid storage. The condition was initially scripted by Sir Benjamin Brodie in 1846 and is additionally designated as Made lung’s disease, Launois-Bensaude syndrome or benign symmetric lipomatosis (1). Characteristically, multiple symmetric lipomatosis displays multiple foci of accumulated, non-encapsulated, mature adipose tissue with predominant infiltration within subcutaneous tissue of cephalic, cervical and upper thoracic region. Multiple, non-encapsulated, symmetrically distributed lipomas which spare distal extremities are enunciated in multiple symmetric lipomatosis (1,2). The condition can be misinterpreted as simple obesity on account of identical clinical features and symptoms. Therefore, antecedent evaluation of pertinent manifestations and differentiation of dual entities is necessitated. The disease is presumed to be a condition diverse from accumulation of brown adipose tissue. Histological structure of constituent adipose tissue cells is dystrophic with characteristics akin to lipoma and liposarcoma. The condition may be associated with significant morbidity, metabolic disturbances, neuropathy, malignant metamorphosis and sudden death (1,2).

Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases

1979 ◽  
Vol 53 (1) ◽  
pp. 45-49 ◽  
Author(s):  
T. K. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Functional Significance ◽  
Adenosine Triphosphatase ◽  
Vas Deferens ◽  
Gland Cells ◽  
Vitelline Gland ◽  
Receptaculum Seminis ◽  
Almost All

ABSTRACTCertain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; tsetes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.

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.

Role of acid proteases in brown adipose tissue atrophy caused by fasting in mice

1990 ◽  
Vol 68 (2) ◽  
pp. 441-447 ◽  
Author(s):  
M. Desautels ◽  
E. Michalska ◽  
B. Mozaffari
Keyword(s):  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Brown Adipose Tissue ◽  
Protein Degradation ◽  
Protein Loss ◽  
Rapid Reduction ◽  
C Protein ◽  
Proteolytic Pathway ◽  
Brown Adipose ◽  
Specific Activities

The lysosomal proteolytic capacity of mouse brown adipose tissue (BAT) and its role during fasting were evaluated. The specific activities of acid phosphatase and cathepsins B, D, H, and L were measured in BAT of mice acclimated at 33, 21, and 4 °C and in BAT undergoing different rates of protein loss during a 24- to 48-h fast. The specific activities of lysosomal proteases in BAT did not vary with the acclimation status of the animals. Mice acclimated at 33 °C showed no significant atrophy of BAT after a fast. In mice kept at 21 °C, protein loss from BAT was observed after a fast without change in tissue DNA content. Protein loss from BAT was partially reduced by injection of the acidotropic agent chloroquine. Furthermore, tyrosine release from BAT during fasting was also reduced by injections of chloroquine or leupeptin, a thiol-protease inhibitor. Tyrosine release from BAT was maximum within 24 h and returned to prefast values by 36 h, suggesting rapid activation followed by inhibition of the tissue proteolytic activity. However, there was no change in acid protease specific activities, suggesting that these enzymes were not limiting for protein degradation. When cold-acclimated mice were fasted at 21 °C, BAT protein loss was markedly enhanced and increases in cathepsin D and L activities were observed, but there was no change in cathepsin B and H and acid phosphatase specific activities. These results indicate that BAT contains an important lysosomal proteolytic pathway that is involved in the rapid reduction of the tissue thermogenic capacity during a fast.Key words: temperature regulation, protein degradation, lysosomes, brown fat.

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.

Histochemical localization of phosphomonoesterases in Avhellina lahorea Woodland, 1927 (Cestoda: Anoplocephalida)

1984 ◽  
Vol 58 (2) ◽  
pp. 169-173 ◽  
Author(s):  
Rashid Farooq ◽  
H.U. Farooqi
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Adenosine Triphosphatase ◽  
Intestinal Parasite ◽  
Histochemical Localization ◽  
Sheep And Goats ◽  
Almost All ◽  
Phosphatase Alkaline

AbstractNon-specific and specific phosphatases have been histochemically localized in the tissues of Avitellina lahorea, an intestinal parasite of sheep and goats. Large quantities of acid phosphatase, alkaline phosphatase and adenosine triphosphatase were observed in almost all organs except the parenchyma where there were moderate amounts of acid phosphatase and no alkaline phosphatase; the reproductive ducts contained moderate amounts of alkaline phosphatase. 5-nucleotidase was observed only in the uterus, egg pouches and eggs and glucose-6-phosphatase activity was restricted to the tegument. The probable functions of these moieties at different sites are discussed.

Sign in / Sign up

Export Citation Format

Share Document