Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). III. Esterases

1980 ◽  
Vol 54 (3) ◽  
pp. 219-222 ◽  
Author(s):  
T. K. Roy

ABSTRACTNonspecific esterase (NSE), acetylcholinesterase (AChE) and pseudocholinesterase (ChE) have been localized by histochemical methods in various tissues of a cestode, Raillietina (Raillietina) johri obtained from the intestine of pigeon.NSE has been found in the rostellum, suckers, hooks, tegument, subtegumental muscle, excretory canal, cirrus sac, vagina and eggs. Two types of cells have been recognized on the scolex surface—some are NSE positive and others are NSE negative. AChE, besides being localized in nerves, has also been visualized in almost all the structures as in case of NSE except in hooks, excretory canal and eggs. Additionally AChE has been observed in the vas deferens and sperm ductules. ChE has been observed only in nerves, vas deferens, cirrus sac and vagina; the intensity of enzyme activity being low when compared with AChE. Possible involvement of these enzymes in the physiology of the parasite has been discussed.

1979 ◽  
Vol 53 (3) ◽  
pp. 261-263 ◽  
Author(s):  
T. K. Roy

ABSTRACTThiamine pyrophosphatase and nucleoside diphosphatase have been studied histochemically in Raillietina (Raillietina) johri. Thiamine pyrophosphatase activity has been observed in the tegument, subtegumental muscle, subtegumental cells, medullary parenchyma, excretory canal and various reproductive structures like testes, ovary, vas deferens, spermatozoa and vitellaria. Eggs exhibit moderate enzyme activity. Various nucleoside diphosphates have been found to be hydrolyzed by thiamine pyrophosphatase. CaC12, MgC12 and MnC12 each activated the enzyme at a final concentration of 6 mM whereas cysteine, reduced glutathione and PCMB inhibited the enzyme activity at a final concentration of 10 mM, 10 mM and 20mM, respectively. KCN and NaF had no effect on the enzyme staining at concentration as high as 50 mM and 30 mM, respectively. Possible roles of the enzyme in the parasite have been discussed.


1974 ◽  
Vol 11 (6) ◽  
pp. 465-476 ◽  
Author(s):  
L. H. J. C. Danse ◽  
W. A. Steenbergen-Botterweg

Adipose tissue of piglets with yellow fat disease had increased activity of nonspecific esterase, 5-nucleotidase, and acid phosphatase. Since these enzymes are associated with different cell structures and damage to these structures can result in increased enzyme activity, they are criteria for pathogenetic study of yellow fat disease.


PEDIATRICS ◽  
1992 ◽  
Vol 90 (6) ◽  
pp. 982-983
Author(s):  
RAN GOSHEN ◽  
EITAN KEREM ◽  
TZIPORA SHOSHANI ◽  
BAT-SHEVA KEREM ◽  
ELAD FEIGIN ◽  
...  

Cystic fibrosis (CF) is the most common autosomal recessive inherited disease in whites. Among whites of European ancestry, approximately 1 in 2000 live births are affected, implying a carrier frequency of 1:25.1 The disease is characterized by chronic lung disease, which usually leads to the patient's death. Furthermore, patients with CF suffer from pancreatic insufficiency and other less common manifestations, such as meconium ileus, hepatobiliary abnormalities, diabetes mellitus, and musculoskeletal problems.1 Almost all males with CF are infertile. Absence of the vas deferens has been reported in 70% to more than 90% of male patients affected by CF.2 Although 4% of full-term male neonates have un-descended testes at birth, 0.8% to 1.0% of 1-year-old boys have cryptorchism and may be subjected to a later surgical intervention.3


Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen

Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.


1979 ◽  
Vol 53 (1) ◽  
pp. 45-49 ◽  
Author(s):  
T. K. Roy

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.


Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen

Abstract Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.


1968 ◽  
Vol 16 (4) ◽  
pp. 249-262 ◽  
Author(s):  
ZOLTAN POSALAKI ◽  
DEZSÖ SZABÓ ◽  
ERNÖ BÁCSI ◽  
ISTVÁN ÖKRÖS

The localization of lipids and the activities of nonspecific esterase, aryl sulfatase and acid phosphatase were studied in different stages of spermatogenesis in rats. In addition, the distribution of acid phosphatase activity was demonstrated electron histochemically. The spermatogenetic cycle was divided into two phases—corresponding to the first and the last four stages of Roosen-Runge-Giesel (RG) classification. Spermatids in the first phase contained abundant endoplasmic reticulum with rosette formation and well developed Golgi apparatus with numerous vesicles. They displayed high activity of hydrolytic enzymes but contained no appreciable amount of lipids. The Sertoli cells contained large lipid granules but showed minimal enzyme activity. During the second phase reduction of the cytoplasm of spermatids with fragmentation of the endoplasmic reticulum and Golgi lamellae, accumulation of lipids, aggregation of ribonucleo-protein particles, formation of residual bodies and marked decrease of enzyme activity were seen. The Sertoli cells contained large mitochondria, well developed endoplasmic reticulum and numerous dense bodies and revealed high activities of hydrolytic enzymes and rapid depletion of lipids. These ultrastructural and histochemical findings suggested an interaction between the Sertoli cells and the developing spermatids which probably contributed to the regulation of spermatogenesis.


1969 ◽  
Vol 17 (6) ◽  
pp. 411-417 ◽  
Author(s):  
PADMAKAR K. DIXIT

Quantitative histochemical methods were used for assaying several dehydrogenases in various cell zones of the rachitic rat epiphyseal cartilage during healing brought about by either vitamin D administration or fasting for 48 hr. 6-Phosphogluconic dehydrogenase activity was significantly greater in the cells of both the proliferating and hypertrophic zones of rachitic control rats as compared to those from vitamin D-treated or fasted rats. Activity of 6-phosphogluconic dehydrogenase in the cells from proliferating and hypertrophic zones was identical in the different groups. Lactic dehydrogenase activity of proliferating and hypertrophic cells obtained from rachitic controls was markedly higher than those from the fasted animals. Minor differences were noted in the malic and isocitric dehydrogenases and peptidase in the cartilage cells obtained from vitamin D-treated, untreated and fasted rats.


1972 ◽  
Vol 20 (5) ◽  
pp. 319-330 ◽  
Author(s):  
THOMAS F. MUTHER

The histochemical methods for carbonic anhydrase are not based on the postulated dehydration of HCO3–. The staining is caused by the formation of an unknown reactive Co compound in the surface layer secondary to enzyme-independent alkalinization of the medium. Kinetic analysis of the reaction shows that loss of CO2 from the medium is rate-limiting. Carbonic anhydrase inhibitors delay the staining by interacting with Co and not by inhibiting the enzyme; they are effective when used after the reaction is complete. The reaction can also be inhibited by agents which are not carbonic anhydrase inhibitors, such as sodium lauryl sulfate and 5-aminothiadiazole, but not by in vivo administered acetazolamide. A comparison of the effect of various fixatives on the biochemical and histochemical enzyme activity shows no correlation. While carbonic anhydrase itself is stained by the reaction, the methods lack the claimed specificity for it.


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