alpha-chymotrypsin and Hyperplasia

Rheumatoid arthritis (RA) is mainly characterized by synovial hyperplasia, angiogenesis, inflammatory cells infiltration. Chymotrypsin is a proteolytic enzyme with anti-inflammatory effects. The current project was intended to test the efficacy and mechanism of chymotrypsin in adjuvant-induced arthritis (AIA) rats to provide an experimental basis for the clinical application of chymotrypsin.. The body weight of the rats in each group showed an increasing trend, and there was no significant difference in weight between the groups. CHD and piroxicam suppressed paw swelling and arthritic scores and decreased synovial hyperplasia, inflammatory cell infiltration, pannus formation, and bone destruction. Furthermore, the overproduction of MMP-1, TNF-α, IL-1β, and IL-6 in serum was remarkably attenuated in the chymotrypsin- and piroxicam-treated rats. The protein levels of TLR4 and NF-κB in the synovial tissue of the chymotrypsin group and the piroxicam group were significantly lower than those in the model group. Likewise, the rats treated with chymotrypsin and piroxicam had a substantial decline in the mRNA expression of TLR4, NF-κB, TNF-α, IL-1β, and IL-6 in synovial tissue.. Chymotrypsin alleviates the joint damage of AIA rats, probably by reducing the expression of MMP-1, TNF-α, IL-1β, and IL-6 through TLR4/NF-κB signaling pathway.

Topics: Animals; Arthritis; Body Weight; Chymotrypsin; Hyperplasia; Interleukin-6; Matrix Metalloproteinase 1; NF-kappa B; Rats; Rats, Sprague-Dawley; RNA, Messenger; Toll-Like Receptor 4; Tumor Necrosis Factor-alpha

The in vivo effects of epidermal growth factor (EGF) on pancreatic growth and digestive enzyme concentrations were compared with the actions of the pancreatic secretagogue caerulein in the adult rat. EGF (10 micrograms/kg BW) did not alter pancreatic weight or protein content. However, this concentration of EGF inhibited [3H]thymidine incorporation into DNA by 44%, decreased DNA content by 20%, and increased the concentrations of amylase, chymotrypsinogen, and protein by 106%, 232%, and 42%, respectively. Pancreatic acini prepared from EGF-treated rats exhibited a characteristic secretory response to caerulein that was superimposable to that obtained in acini from saline-treated rats. In both groups of acini half-maximal and maximal stimulation of amylase release occurred at approximately 5 pM and 50 pM caerulein, respectively. In contrast to EGF, caerulein (1 microgram/kg BW) increased pancreatic weight by 29% and protein content by 59%, and enhanced [3H]thymidine incorporation into DNA by 70%. Although caerulein increased the concentrations of pancreatic amylase and chymotrypsinogen by 38% and 297%, respectively, pancreatic acini prepared from caerulein-treated rats were less sensitive to the actions of caerulein in vitro when compared with acini from control rats. Indeed, the EC50 was shift from 4.8 pM to 9.8 pM after 4 days of treatment. EGF potentiated the actions of caerulein on pancreatic weight, protein content, and chymotrypsinogen concentration, and prevented the caerulein-induced alteration in the secretory responsiveness of the acinar cell. Conversely, caerulein reversed the inhibitory effect of EGF on thymidine incorporation. These findings suggest that EGF may modulate the trophic effects of certain gastrointestinal hormones, and may participate in the regulation of pancreatic exocrine function in vivo.

Topics: Amylases; Animals; Cell Division; Ceruletide; Chymotrypsin; DNA Replication; Epidermal Growth Factor; Hyperplasia; Hypertrophy; Male; Organ Size; Pancreas; Rats; Rats, Inbred Strains; Reference Values

Alpha-1-antitrypsin (A1AT) has been shown to be a useful tumor marker for hepatocellular carcinoma (HCC) and some other neoplasms. No studies of alpha-1-antichymotrypsin (A1AChy) in HCC have been reported. A comparative study of A1AT and A1AChy in HCC was undertaken. While 19/33 HCC were positive for A1AT, all 33 HCC contained immunoreactive A1AChy. Cells showing positive immunoreaction for both A1AT and A1AChy were more numerous in moderately differentiated HCC than in well differentiated or poorly differentiated HCC. Although the pattern of staining with both antisera was similar, in cases showing positive staining for both antisera, A1AChy-positive cells were more numerous than A1AT-positive cells. The results suggest a useful role for A1AChy as a marker of HCC.

Topics: alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Carcinoma, Hepatocellular; Cell Transformation, Neoplastic; Chymotrypsin; Histocytochemistry; Humans; Hyperplasia; Immunoenzyme Techniques; Liver; Liver Cirrhosis; Liver Neoplasms

Topics: Aging; Amylases; Animals; Body Weight; Cholecystokinin; Chymotrypsin; DNA; Hyperplasia; Hypertrophy; Lipase; Organ Size; Pancreas; Proteins; Rats; RNA; Stimulation, Chemical

Topics: Animals; Benz(a)Anthracenes; Cell Division; Cell Nucleus; Cell Transformation, Neoplastic; Chymotrypsin; DNA; Epithelial Cells; Epithelium; Fluorometry; Hyperplasia; Male; Methods; Mice; Mitosis; Neoplasms, Experimental; Precancerous Conditions; Skin; Skin Neoplasms

Topics: Body Weight; Body Weights and Measures; Chymotrypsin; Diet; Hematologic Tests; Hyperplasia; Hypertrophy; Pancreatic Extracts; Pancreatin; Peptide Hydrolases; Pharmacology; Rats; Research; Submandibular Gland; Trypsin