[Histochemistry of selected peptidases in small intestine mucosa in piglets experimentally infected with Isospora suis]. 1990

M Kudweis, and Z Lojda, and I Julis
Parazitologický ústav CSAV, Ceské Budĕjovice.

In the small intestine mucosa of 24 gnotobiotical piglets experimentally infected the first day post partum with oocysts of the coccidium Isospora suis, the activities of dipeptidylpeptidase IV (EC.3.4.14.5.; DAP IV) and gamma-glutamyl transferase (EC.2.3.2.2.; GGT) in the microvillous zone of enterocytes were evaluated by scanning densitometry. The tissue of the small intestine in piglets infected with a dose of 100,000 oocysts of the coccidia of I. suis was examined in the period from the first till the eleventh day post infection (DPI). In the control piglets at the age of 2-5 days it was found that most of the DAP IV activity was located in the microvillous zone of the enterocytes of the middle jejunum, rear jejunum and ileum. The DAP IV activity of duodenum mucosa was lower; as compared with the activity in the mucosa of the jejunum and ileum it reached 53-57%. In the case of GGT activity, the highest density values of the reaction product were recorded in the microvillous zone of enterocytes of the duodenum and the whole jejunum, the lowest in the ileum mucosa (86-89%) of the activity found in the duodenum and jejunum). During the experimental infection the infected piglets had a significant deficit of both peptidases, especially DAP IV (the whole studied period). The development of GGT activity was slightly different with the onset of the marked decline of the enzyme activity only on the fifth DPI. The lower GGT activity persisted till the eighth DPI. The density of the GGT reaction product began to return to the normal on the ninth to eleventh DPI. No predisposition in the location of the deficit was observed in the peptidases studied during the infection. The decline of the activity of both enzymes influenced also the mucosa of all studied parts of the small intenstine. The difference lay in the relevance of lowering of the density of reaction product of DAP IV and GGT on other DPI and in the different intensities of the return of the activity to the physiological normal.

UI MeSH Term Description Entries
D007413 Intestinal Mucosa Lining of the INTESTINES, consisting of an inner EPITHELIUM, a middle LAMINA PROPRIA, and an outer MUSCULARIS MUCOSAE. In the SMALL INTESTINE, the mucosa is characterized by a series of folds and abundance of absorptive cells (ENTEROCYTES) with MICROVILLI. Intestinal Epithelium,Intestinal Glands,Epithelium, Intestinal,Gland, Intestinal,Glands, Intestinal,Intestinal Gland,Mucosa, Intestinal
D007421 Intestine, Small The portion of the GASTROINTESTINAL TRACT between the PYLORUS of the STOMACH and the ILEOCECAL VALVE of the LARGE INTESTINE. It is divisible into three portions: the DUODENUM, the JEJUNUM, and the ILEUM. Small Intestine,Intestines, Small,Small Intestines
D003048 Coccidiosis Protozoan infection found in animals and man. It is caused by several different genera of COCCIDIA. Besnoitiasis,Besnoitiosis,Besnoitiases,Besnoitioses,Coccidioses
D004152 Dipeptidyl-Peptidases and Tripeptidyl-Peptidases A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain. Dipeptidyl Peptidase,Dipeptidyl Peptidases,Dipeptidylpeptide Hydrolase,Tripeptidyl-Peptidase,Dipeptidylpeptide Hydrolases,Tripeptidyl-Peptidases,Dipeptidyl Peptidases and Tripeptidyl Peptidases,Hydrolase, Dipeptidylpeptide,Peptidase, Dipeptidyl,Tripeptidyl Peptidase,Tripeptidyl Peptidases,Tripeptidyl-Peptidases and Dipeptidyl-Peptidases
D005723 gamma-Glutamyltransferase An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid. GGTP,Glutamyl Transpeptidase,gammaglutamyltransferase,gamma-Glutamyl Transpeptidase,Transpeptidase, Glutamyl,Transpeptidase, gamma-Glutamyl,gamma Glutamyl Transpeptidase,gamma Glutamyltransferase
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013552 Swine Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA). Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog
D013553 Swine Diseases Diseases of domestic swine and of the wild boar of the genus Sus. Disease, Swine,Diseases, Swine,Swine Disease
D018819 Dipeptidyl Peptidase 4 A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation. Antigens, CD26,CD26 Antigens,Dipeptidyl-Peptidase IV,Adenosine Deaminase Complexing Protein 2,CD26 Antigen,Antigen, CD26,Dipeptidyl Peptidase IV

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