Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Thiamine Pyrophosphatase”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1979

Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). II. Nucleoside diphosphatase and thiamine pyrophosphatase.

Thiamine 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. CaCl2, MgCl2 and MnCl2 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 20 mM, 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.

Acid Anhydride Hydrolases↗
PubMed1971

Isolation of a Golgi apparatus-rich fraction from rat liver. IV. Thiamine pyrophosphatase.

The thiamine pyrophosphatase (the enzyme [s] catalyzing the release of inorganic phosphate with thiamine pyrophosphate as the substrate) activities of Golgi apparatus-, plasma membrane-, endoplasmic reticulum-, and mitochondria-rich fractions from rat liver were compared at pH 8. Activity was concentrated in the Golgi apparatus fractions, which, on a protein basis, had a specific activity six to eight times that of the total homogenates or purified endoplasmic reticulum fractions. However, only 1-3% of the total activity was recovered in the Golgi apparatus fractions under conditions where 30-50% of the UDPgalactose:N-acetylglucosamine-galactosyl transferase activity was recovered. Considering both recovery of galactosyl transferase and fraction purity, we estimate that approximately 10% of the total thiamine pyrophosphatase activity of the liver was localized within the Golgi apparatus, with a specific activity of about ten times that of the total homogenate. Cytochemically, reaction product was found in the cisternae of the endoplasmic reticulum as well as in the Golgi apparatus. This is in contrast to results obtained in most other tissues, where reaction product was restricted to the Golgi apparatus. Thus, enzymes of rat liver catalyzing the hydrolysis of thiamine pyrophosphate, although concentrated in the Golgi apparatus, are widely distributed among other cell components in this tissue.

Animals↗
PubMed1977

Histochemical evaluation of thiamine pyrophosphatase activity during first molar odontogenesis of the neonatal hairless mouse.

Localization of thiamine pyrophosphatase activity has been evaluated in the developing first molar of the neonatal hairless mouse. Postnatal animals from parturition to five days of age were decapitated and the severed heads frozen and sectioned in a frontal plane on a cryostat. 14 micron thick sections were fixed and subsequently incubated for thiamine pyrophosphatase activity according to the method of GOLDFISCHER et al. (1971). The tissue was visualized, dehydrated, cleared and mounted. Light microscopy was utilized in evaluating thiamine pyrophosphatase activity. Thiamine pyrophosphatase activity in the first molar of the hairless mouse is presented in tabular form and compared to similar data for the Swiss albino mouse. Enzyme activity increased as the metabolic activities of various cell layers increased. Thus, thiamine pyrophosphatase activity appeared to be related to the degree of differentiation and functional completency of the odontogenic tissues in the hairless mouse.

Animals↗
PubMed1990

The occurrence of the Golgi apparatus in mouse oocytes. Demonstration of thiamine pyrophosphatase activity.

Location of thiamine pyrophosphatase activity as a marker of the Golgi apparatus was studied ultracytochemically in mouse oocytes with germinal vesicle (OGV), oocytes at metaphase I (OMI) and oocytes at metaphase II (OMII), and further in cells of the respective cumulus oophorus serving as comparative objects. TPPase activity in cumulus oophorus cells and in OGV was found exclusively in the Golgi apparatus. In OMI the reaction product of TPPase activity was observed in isolated smooth vesicles, and in only one case in structures identifiable as the Golgi apparatus. In OMII the occurrence of TPPase activity was also recorded in isolated smooth vesicles in cortical cytoplasm and further, exceptionally, in smooth concentrically arranged vesicles or tubules. The TPPase activity was not present in vesicular complexes. The results have shown that after the resumption of meiosis the occurrence of the reaction product of TPPase activity drops abruptly due to the reduction of the Golgi apparatus. Changes affecting the Golgi apparatus after the resumption of meiosis are related to the loss of the nucleus after the germinal vesicle breakdown.

Animals↗
PubMed1988

Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct from microsomal nucleoside diphosphatase.

The properties of thiamine pyrophosphatase in the Golgi apparatus of rat liver were studied. Thiamine pyrophosphatase in an extract of the Golgi apparatus was separated into 6 bands of between pH 5.4 and 6.3 by isoelectric focusing on polyacrylamide gel. On the gels all these subforms catalyzed the hydrolyses of GDP, IDP, UDP, and CDP as well as that of thiamine pyrophosphate. The characteristics resembled those of Type B nucleoside diphosphatase of rat brain, though the enzyme did not have 3 subforms of Type B nucleoside diphosphatase in the higher pH region on isoelectric focusing. Thiamine pyrophosphatase of the Golgi apparatus was separated from microsomal nucleoside diphosphatase by DEAE-cellulose column chromatography. The properties of the enzyme were quite similar to those of Type B nucleoside diphosphatase with respect to its substrate specificity, optimum pH for activity, and inhibition by ATP. These findings suggest that thiamine pyrophosphatase in the Golgi apparatus is different from microsomal nucleoside diphosphatase and that it might be basically the same enzyme as Type B nucleoside diphosphatase except for different extents of modification.

Acid Anhydride Hydrolases↗
PubMed1983

The origin of the zymogen granule membrane of the pancreatic acinar cell as examined by ultrastructural cytochemistry of acid phosphatase, thiamine pyrophosphatase, and ATP-diphosphohydrolase activities.

Cytochemical distributions of acid phosphatase, thiamine pyrophosphatase, and ATP-diphosphohydrolase activities have been examined on thin sections of rat pancreas and on isolated zymogen-granule membranes. Acid phosphatase was found in the rigid lamellae separated from the Golgi stacked cisternae, in condensing vacuoles, and in the trans-saccules of Golgi apparatus; it was not detected in purified zymogen-granule membranes. Thiamine pyrophosphatase was detected in trans-saccules of the Golgi apparatus, in purified zymogen-granule membranes, and in the plasmalemma of the acinar cell. It was absent in condensing vacuoles. The ATP-diphosphohydrolase activity has a distribution similar to thiamine pyrophosphatase. These observations illustrate the similarity between the trans-saccules of the Golgi apparatus and the membrane of mature zymogen granules and the disparity between the latter membrane and the membrane of the condensing vacuole. They suggest that the condensing vacuole might not be the immediate precursor of the zymogen granule as commonly assumed. An alternative possibility would be that condensing vacuoles would fuse with the trans-saccule (transition) of the Golgi apparatus which in turn would form mature zymogen granules.

Acid Phosphatase↗
PubMed1975

Histochemical localization of adenosine triphosphatase and thiamine pyrophosphatase in the digestive system of a teleost fish, Ophiocephalus punctatus.

The localization of ATPase and thiamine pyrophosphatase in the digestive system of Ophiocephalus punctatus has been studied. In stomach ATPase is found in the free border of the mucosa, gastric glands, submucosal connective tissue nuclei and muscularis. Thiamine pyrophosphatase is localized only in the mucosa and gastric gland cells. In the intestine, pyloric caeca and rectum, ATPase is distributed along the brush border of the columnar epithelial cells, their nuclei and cytoplasm. Mild activity is also found in the nuclei of submucosa and muscularis. The activity is stronger in the intestine than in the other portions. Thiamine pyrophosphatase activity in these portions is restircted only to the goblet cells. In the liver ATPase activity is associated both with the cytoplasm and nucleus of the hepatic cells. Thiamine pyrophosphatase activity is maximum in the centro-lobular portion.

Adenosine Triphosphatases↗
PubMed1981

Localization of thiamine pyrophosphatase activity in motor end plates.

Thiamine pyrophosphatase (TPPase) activity was localized in the terminal arborization of the motor end plates both in rat and frog striated muscles. Electron microscopically the end product of the enzyme was seen in synaptic vesicles. That TPPase was axonally transported was indicated by its localization following experimental ligation of peripheral nerves. It is thus possible that TPPase may play a role in the synthesis of the synaptic mediator substance of the neuromuscular junction.

Animals↗
PubMed1982

Thiamine pyrophosphatase activity of the prenatal mouse molar. A histochemical investigation.

Thiamine pyrophosphatase (TPPase), an enzyme associated with the Golgi apparatus, has been implicated in the regulation of cellular oxidation as well as of transport across cell membranes. This enzyme has been localized in odontogenic tissues of the postnatal mouse and it was the intent of the present study to localize TPPase during prenatal odontogenesis. Mouse fetuses (CDI, Charles River) 14 through 19 days postconception were decapitated, the heads were frozen and mounted on the chuck of a cryostat. Frontal sections, 14 micrometers thick, were air-dried and incubated for TPPase activity. Subsequent to incubation the activity was visualized by immersion in 1% ammonium sulfide. The degree of enzyme activity varied not only with the chronological age of the fetus but also as a function of the tissue's metabolic state. Regions, such as the dental lamina, evidenced decreased TPPase activity with increasing age, while tissue layers such as the IEE displayed greater enzyme activity with increasing age.

Animals↗
PubMed1979

Is thiamine pyrophosphatase a reliable marker of the neuronal Golgi apparatus? A critical analysis.

The thiamine pyrophosphatase histochemical technique is believed to be a suitable approach to the selective staining of the Golgi vesicles of all animal cells, icluding the neuron. However, during the past decade a considerable number of data have been published, suggesting that the TPPase is in general a membrane-associated enzyme in the brain, which can be found in subcellular fractions other than Golgi lamellae. It has therefore become necessary to reconsider the view that thiamine pyrophosphatase is an exclusive marker enzyme of the Golgi apparatus.

Animals↗
PubMed1981

Effect of colchicine on the Golgi apparatus and on GERL of rat jejunal absorptive cells. Ultrastructural localization of thiamine pyrophosphatase and acid phosphatase activity.

Ultrastructural localization of thiamine pyrophosphatase (TTP) and acid phosphatase (AcPase) activity was performed on jejunal absorptive cells of rats pretreated with the antimicrotubular agent colchicine and of control animals. Demonstration of TPP activity showed that most of the dislocated Golgi stacks after colchicine application lacked positively staining cisternae of the mature side. This cytochemical finding is in agreement with the morphologically demonstrable changes of the Golgi stacks resulting in a loss of polarity and give evidence for a colchicine-induced deficiency of the Golgi apparatus. The cytochemical localization of AcPase activity showed deposits of reaction product over lysosomes and GERL and demonstrated a dislocation of GERL occurring concomitantly with the changes of the Golgi apparatus. The antimicrotubular effect of colchicine is well documented; thus the morphological and cytochemical changes of the Golgi apparatus and of GERL might be due to a disturbed microtubular function after application of this agent suggesting an influence of microtubules in the maintenance of the integrity of these organelles. This hypothesis includes the possibility of an involvement of microtubules in formation and differentiation of Golgi stacks and GERL as well as a kind of "skeletal"function being responsible for their characteristic structure and fashion.

Acid Phosphatase↗
PubMed1982

The localization of thiamine pyrophosphatase activity in Meckel's cartilage cells during endochondral ossification.

The cytochemical distribution of thiamine pyrophosphatase (TPPase) activity in Meckel's cartilage cells of the mouse embryo has been studied during the endochondral ossification. All the cartilage cells contain reaction product within the Golgi apparatus. In immature chondrocytes, at the reserve cell zone, TPPase activity is restricted to several inner cisternae of independent Golgi apparatus. In mature cells at the proliferative cell zone, several Golgi complexes form a Golgi network connecting with each other by the TPPase positive tubular stalks. Golgi cisternae, condensing vacuoles and vesicles also contain reaction product. In the hypertrophic chondrocytes located in the calcifying zone, their disorganized Golgi apparatus still retain reaction product. Some chondrocytes, even those located within calcified or opened lacunae, exhibit intact structures and normal cytochemical enzyme distribution. These data indicate the possibility that some chondrocytes may survive and contribute the formation of mandible.

Animals↗
PubMed1979

Fine structural localization of thiamine pyrophosphatase and acid phosphatase activities in the mouse pancreatic acinar cell.

The fine structural localization of thiamine pyrophosphatase (TPPase) and acid phosphatase (AcPase) was examined in pancreatic acinar cells of fasting and fed mice. The results were not affected by these conditions. TPPase activity was positive in two and sometimes three cisternae of the inner Golgi lamellae as well as in the condensing vacuoles of the trans area, but negative in the rigid lamellae and small vesicles of the trans area. AcPase activity was demonstrated in two and sometimes three cisternae of inner Golgi lamellae, condensing vacuoles, rigid lamellae, lysosomes and smooth or coated vesicles in the trans area. The inner Golgi lamellae and the condensing vacuoles were positive for both enzyme activities. From these facts, the lysosome is considered to be formed not only in the GERL system but also through the rough endoplasmic reticulum-Golgi apparatus route. It is reasonable to consider that Novikoff's GERL is not independent from the Golgi apparatus but represents a part of this organelle.

Acid Phosphatase↗