Reference

The V2 carcinoma of the rabbit as a model for tumor invasion: 3

The V2 carcinoma of the rabbit as a model for tumor invasion: 3. Proteolytic activities. Baici, Antonio; Graf, Markus; Gyger-Marazzi, Maya (Dep. Rheumatol., Univ. Hosp., Zurich CH-8091, Switz.). Tumour Prog. Markers, Proc. Meet. Eur. Assoc. Cancer Res. (E.A.C.R.), 6th, Meeting Date 1981, 47-50. Edited by: Lapis, Karoly; Jeney, A.; Price, M. R.There are some reagents with their cas registry numbers 9047-22-7 and 9001-12-1 are used in this study. Kugler Publ.: Amsterdam, Neth. (English) 1982. CODEN: 50WUAX. DOCUMENT TYPE: Conference CA Section: 14 (Mammalian Pathological Biochemistry) In V2 carcinoma homogenates, elastase-like, chymotrypsin-like, and plasminogen activator activities were found, but the activities corresponded more or less to those found in serum. A cysteine proteinase with cathepsin B-like activity was found in tumor homogenates at higher concns. than those of serum. Collagenase was found in high amts. in the homogenates and was absent from serum. In tumor explant cultures, elastase-like, chymotrypsin-like, and plasminogen activator activities were absent or low over the 9-day culture period. Cathepsin B-like activity was found in the media of s.c. and i.p. tumor explants and was absent in explants from normal s.c. tissue. In confrontation cultures (i.p. tumor with s.c. tissue), cathepsin B-activity release was increased over the controls (s.c. tissue alone). Collagenase was almost exclusively released in the latent form from cultures of s.c. tissue and i.p. tumor. S.c. grown V2 carcinoma released only latent collagenase at 0 days of culture; active collagenase increased 14 and 29% of the total activity at 7 and 9 days of culture, resp. In confrontation cultures, the active collagenase increased up to 70%. Purified cathepsin B from rabbit liver activated in vitro the latent form of collagenase of V2 carcinomas. Studies suggested that cathepsin B is produced by host cells surrounding the tumor which are stimulated by the tumor. The results are discussed with respect to the metastatic process. .

Stimulation by human interleukin 1 of cartilage breakdown and production of collagenase and proteoglycanase by human chondrocytes but not by human osteoblasts in vitro

Stimulation by human interleukin 1 of cartilage breakdown and production of collagenase and proteoglycanase by human chondrocytes but not by human osteoblasts in vitro. Gowen, Maxine; Wood, David D.; Ihrie, Earl J.; Meats, Judith E.; Russell, R. Graham G. (Med. Sch., Univ. Sheffield, Sheffield S10 2RX, UK). Biochim. Biophys. Acta, 797(2), 186-93 (English) 1984. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Section cross-reference(s): 13 Human articular chondrocytes in culture synthesize collagenase and neutral proteoglycanase in response to addn. of a 12-17 kilodalton protein produced by cultured human monocytes. This factor copurifies with interleukin 1, as assessed by lymphocyte-activating factor activity, on gel filtration chromatog. and isoelec. focusing. The interleukin 1 and chondrocyte-stimulating activities are destroyed by pretreatment of the material with phenylglyoxal. The same materials also promote the release of glycosaminoglycans from cultures of intact bovine nasal cartilage. 9001-12-1 and 79955-99-0 which are cas registry numbers of chemicals are mentioned. The proteoglycanase activity released from chondrocytes appears to be a metalloproteinase because it is inhibited by EDTA and not by phenylmethylsulfonyl fluoride, and because detection of its activity is dependent on the presence of 4-aminophenylmercuric acetate. Human osteoblast-like cells do not respond to this factor by increased proteinase prodn., but are stimulated to produce prostaglandins. Apparently, interleukin 1 has activities upon non-immune cells which promote the degrdn. of connective tissue matrices. Human osteoblasts do not synthesize neutral collagen- and proteoglycan-degrading enzymes and, thus, are unlikely to be directly responsible for the matrix degrdn. which occurs during bone resorption. .