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T Glant

Publications and source records attributed to T Glant.

29 records · Page 2Linked to original sources
PubMed1975

Studies on cartilage formation. XX. Histochemical investigation of some enzymes of glycogen metabolsim in regenerative articular surfaces.

In 28 dogs the distal articular cartilage of the femur was removed and the regenerating articular surface on the 70th postoperative day was studied histochemically for hexokinase, glucose-6-phosphatase, phosphohexose-isomerase, fructose-1, 6-diphosphatase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, lactate dehydrogenase isoenzymes, phosphoglucomutase, phosphorylase, glycogen synthetase, UDP--glucose dehydrogenase, and UDP-glucuronic acid-4-epimerase. The articular surface consisted of fibrous tissue and of cartilage islets. The latter contained cells differentiating into cartilage and young chondrocytes. The glycolytic enzymes reacted positively in the regenerative articular surface. Enzyme activities were higher in the cells (particularly the chondroblasts and young chondrocytes) of the cartilage islets than in the connective tissue. In the cells differentiations into cartilage, beside the LDH isoenzymes characteristic of glycolysis, a significant LDH1 and LDH2 activity was observed. At the same site the presence of fructose-1, 6-diphosphatase-activity could be assumed, but there was no glucose-6-phosphatase activity. Glycogen synthesis proceeded in the cells of the cartilage islets and UDP-glucuronic acid-4-epimerase activity was observed in the differentiated cells. UDP-glucose dehydrogenase activity was positive in every section of the articular surface.

Animals↗
PubMed1975

Species-common antigen of connective tissues.

Collagen-free extracts were prepared from bovine, porcine and canine hyaline, elastic and fibrous cartilages, articular capsule, tendon, aorta, cortical bone and regenerating articular surfaces. The extracts were investigated with antisera to bovine nasal septal cartilage, dog articular cartilage and non-collagenous protein fraction of bovine cortical bone. Immunodiffusion, immunoelectrophoresis, and immunohistochemical methods were used. In the different supporting tissues of the three animal species a common antigen, probably of proteoglycan origin, was demonstrated. The finer differences in antigenicity between the different tissues are probably due to the variations in proteoglycan composition of the given supporting tissues. Owing to the wide-spread occurrence of the antigen, the authors suggest the term "species-common connective tissue antigen" instead of the "species-common cartilage antigen" used so far.

Animals↗
PubMed1975

Antigenicity of bone tissue. I. Immunological and immunohistochemical study of non-collagenous proteins of the bovine cortical bone.

From powdered bovine bone cortex an extract has been prepared with 0.15 M NaCl and its collagen-free fraction obtained on DEAE-cellulose column was used for the immunization of rabbits. The non-collagenous protein fraction (NCP) produced against immune serum two precipitation arcs both on agarose double gel-diffusion and with immune electrophoresis. After decalcination in 10% EDTA PH 7.4, direct and indirect immune histochemical examinations were performed with fresh, freshly lyophilized, as well as with bones kept for three and six months at 20 degrees C, and the antigens were localized. Prolonged storage increased the antibody-binding capacity of the bones, whereas lyophilization decreased it. Fixation in cold acetone was suited best for immunohistochemical study of the cortical bones.

Animals↗
PubMedDate not supplied

Epitopes of cartilage core proteins and GAG pattern in human non-Hodgkin lymphoma xenografts.

Glycosaminoglycan and core protein components of proteoglycans (PGs) have been studied in three human non-Hodgkin lymphoma xenografts of B cell origin. Lymphomas showed similar GAG content, but different composition of GAG subtypes. This variability was accompanied by an individual capacity to adhere to extracellular matrix elements. The core proteins identified by monoclonal antibodies raised against human cartilage chondroitin sulfate PG were also distinctly expressed and released. These proteins shared by different cell types may have biological significance.

Aggrecans↗