Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “CESTODA”

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 91 records · Page 5Linked to original sources
PubMed1998

Ultrastructure of spermiogenesis and the spermatozoon of Vampirolepis microstoma (Cestoda, Hymenolepididae), intestinal parasite of Rattus rattus.

Spermiogenesis in Vampirolepis microstoma begins with the formation of a nuclear cone and a differentiation zone. This is delimited at the front by arched membranes, bordered by cortical microtubules, and contains two parallel centrioles linked together at their bases by electron-dense, amorphous material. The nuclear cone elongates, becomes filiform, and migrates into the spermatid body. Later, one of the centrioles gives rise to a flagellum that grows at the same pace as the cortical microtubules. Subsequently, 6 crested bodies form and the old spermatid separates from the residual cytoplasm. The mature V. microstoma spermatozoon is filiform and lacks mitochondria. Its anterior end exhibits six crested bodies 100 to 200 nm thick of unequal lengths. The axoneme is of the 9+"1" pattern. The cortical microtubules are spiralized and make an angle of about 20 to 30 degrees to the spermatozoon axis, except at their posterior extremity where they become parallel to this axis. The nucleus is an electron-dense cord coiled in a spiral around the axoneme. The cytoplasm is slightly dense but contains many electron-dense granules in regions III, IV, and V of the spermatozoon. The presence of centrioles linked together at their bases by electron-dense material has never, to our knowledge, been reported in a Platyhelminth. Likewise, a nuclear migration, right from the beginning to the end of spermiogenesis, has never been described in a cestode. In addition, we observe for the first time the existence of six crested bodies in a cestode from a Mammal.

Animals↗
PubMed1975

Multienzymic nature of pyruvate kinase during development of Hymenolepis diminuta (Cestoda).

H. diminuta at different stages of development contained as many as five pyruvate kinase isozymes. Four of these were unusually sensitive to allosteric activation by fructose-1,6-P2. One isozyme which occurred only in adults or near-adults was insensitive but had a relatively low Km. All were inhibited by ATP and Ca2+, none by alanine, and the pH optimum was unaffected by fructose-1,6-P2. The five isozymes were present in gravid or reproductively active proglottids. Two of them occurred after eight days growth in the rat intestine, and three after four days. These three were also present in the immature, anterior proglottids of adult parasites. Hexacanth larvae from gravid proglottids, as well as cysticercoids developing from these larvae in Tenebrio molitor, possessed only two isozymes. It was inferred from information on tissue concentrations of ADP, ATP, phosphoenolypyruvate (PEP) and on K0.5S and Km that competition between pyruvate kinase and PEP carboxykinase is probably controlled by fructose-1,6-P2 concentrations. Since H. diminuta is an obligatory fermenter in which gluconeogenesis is minimal, the probable function of its L-type pyruvate kinases is to control the specific composition of lactic, acetic and succinic acid mixtures that are excreted at different stages of development.

Adenosine Diphosphate↗
PubMed1977

The phosphoenol-pyruvate branchpoint in adult Hymenolepis diminuta (Cestoda): a study of pyruvate kinase and phosphoenol-pyruvate carboxykinase.

The properties of pyruvate kinase (PK) and phosphoenol pyruvate carboxykinase (PEP CK), two enzymes that determine the preferrential accumulation of either succinate or lactate as endproducts of carbohydrate metabolism, are described in adult Hymenolepis diminuta. PK activity at Vmax and Km levels of PEP was unaffected by ATP, alanine, FDP4, OR H+ ions, but was inhibited by 50% at 6.3 mM L-lactate and 30 mM HCO3. The addition of 30 mM HCO3 increased the Km(PEP) by 6-fold but did not alter the Vmax. The inhibition of PK by HCO3 cannot be explained entirely by an effect of ionic strength, but probably represents a specific modulator-enzyme interaction. Under similar conditions PEP CK was maximally activated. Although L-lactate inhibited PEP CK (Ki(lac) = 1.8 mM), this effector may play a minor role in regulation of PEP flux. These results implicate the poise of the HCO3-:CO2 system as a major determiner of endproduct accumulation in H. diminuta.

Animals↗
PubMed1994

Grillotia erinaceus (Cestoda, Trypanorhyncha): localization of neuroactive substances in the plerocercoid, using confocal and electron-microscopic immunocytochemistry.

Indirect immunocytochemistry, in conjunction with confocal scanning laser microscopy and electron-microscopic immunogold labeling, has been used to localize neuropeptide and 5-hydroxytryptamine (5-HT) immunoreactivities (IRs) in the plerocercoid (scolex and surrounding blastocyst) of the trypanorhynch tapeworm, Grillotia erinaceus. Antisera directed to two native cestode neuropeptides, neuropeptide F and the FMRFamide-related peptide, GNFFRFamide, were used to demonstrate the presence of a well-developed and extensive peptide-immunoreactive nervous system of central and peripheral elements in the juvenile scolex. Neuronal connectivity exists between the scolex and the surrounding blastocyst, in which there is a rich innervation of varicose fibers displaying peptide IR. Ultrastructurally, gold labeling of the peptide IR was found exclusively over the contents of dense secretory vesicles in the axons and somatic cytoplasm of neurons. Double-labeling experiments demonstrated an apparent colocalization of peptide IR, although the results of antigen preadsorption procedures indicated substantial cross-reactivity of the two antisera. A separate and well-differentiated 5-HT-immunoreactive nervous system, with a similar anatomical arrangement as the peptide-immunoreactive nervous system, is present in both the scolex and blastocyst.

Animals↗