Basal cell carcinoma and risk of subsequent malignancies: A cancer registry-based study in southwest England.

Background: A possible link between basal cell carcinoma (BCC) and an increased subsequent risk of experiencing further noncutaneous malignancies has been suggested in previous cancer-registry and cohort studies.

Objective: The purpose of this study was to establish whether a possible link between BCC and subsequent malignancies could be confirmed in a new population in which environmental and genetic risk factors may vary from previously studied populations.

Methods: A cohort of 13,961 cancer registry-listed persons from the southwest of England, in whom BCC had been diagnosed during the period of 1981 to 1988, was examined for the relative risk of experiencing various further malignancies.

Head and neck cancer in the South West of England: influence of socio-economic status on incidence and second primary tumours.

This study examined possible links between the incidence of head and neck squamous cell carcinoma (HNSCC) and social deprivation. Data on all HNSCC registered between 1985 and 1991 in the South West of England were collected. Excluding tumours of the lip and skin there were 1570 cases, 72% in males.

An ecological study of cancer incidence and radon levels in South West England.

To investigate the relationship of domestic radon levels and cancer, the incidence of 14 major cancers in Devon and Cornwall were examined in relation to the local radon levels. Cancer registrations for 1989-1992 were provided by the South-Western Regional Cancer Registry. The average radon levels for postcode sectors were sorted into ten categories from low (< 40 Bq/m3) to extremely high (> or = 230 Bq/m3) and age-standardised incidence rates were calculated for each radon category.

Uterine collagen during pregnancy in cattle.

Uteri were collected at the slaughter of non-pregnant dairy cattle and cattle at various stages of gestation. The weight of the whole uterus increased about 12-fold during the 9 month gestation period. The greatest increase was in the weight of the pregnant horn.

Improving the comparability of cancer registry treatment data and proposals for a new national minimum dataset.

Background: There is no consistent or standardized practice for the collection of treatment data in UK cancer registries. This limits the usefulness and effectiveness of undertaking multiregional or national studies of treatment outcomes and survival.

Methods: A working group was established to examine the practices for recording the type and the amount of treatment data held in the cancer records at different registries.

Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef.

Levels of calpains I and II, cathepsins B and L and β-glucuronidase were determined in extracts of electrically stimulated and control beef M. Pectoralis profundus stored at temperatures between 0 and 30°C and varied to avoid muscle shortening. The level of lysosomal enzymes remained essentially unchanged throughout storage.

The effect of modification on the susceptibility of collagen to proteolysis: I. Chemical modification of amino acid side chains.

A series of chemically modified collagens were subjected to proteolysis by lysozomal cathepsins, pepsin and trypsin. Modifications of the collagens included acetylation, succinylation, methylation and borohydride reduction. Changes in the integrity of the materials were also monitored by differential scanning calorimetry (DSC).

Uterine collagen during involution in cattle.

Post-partum involution of the bovine uterus was assessed by clinical examination and monitored biochemically by measuring the total urinary excretion of hydroxyproline and the collagen cross-link, pyridinoline. Uterine tissue contained 0.13 +/- 0.

The solubilization of myofibrillar proteins by calcium ions.

The effect of elevated levels (30 mm) of Ca(2+) and other divalent metals ions on rabbit psoas myofibrils was studied to determine whether these caused solubilization of structural proteins and if so whether the effect was due to salting-in or to proteolytic fragmentation resulting from activation of calpains. Incubation of myofibrils in 30 mm CaCl(2) at either pH 5·6 or 7·0 did not cause any apparent solubilization of the major Z-disc proteins, but there was an immediate ( < 1 min) solubilization of C-protein and troponin I together with small amounts of Mr 80 000 protein, troponin T and tropomyosin. Longer incubations with CaCl(2) extracted little additional C-protein but there was a steady increase with time in the solubilization of proteins with Mr values of 45 000 and 42 000, troponin T, tropomyosin and troponin I.

Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L.

We have investigated the susceptibility of both the helical and non-helical regions of isolated rat chondrosarcoma collagens, types II, IX and XI, to degradation by the cysteine proteinases, cathepsins B and L. Both enzymes degrade these collagens at temperatures from 20 to 37 degrees C and pH values from 3.5 to 7.

Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle.

Control, electrically stimulated (ES) and glycogen-depleted (GD) chicken muscles were conditioned at 15°C with continuous mechanical testing for extensibility. The ES and GD muscles went into rigor 3·6 and 2·8 h earlier, respectively, than control muscle. At 24h post-rigor the extensibility of control muscle (11·2%) was markedly less than ES (19·2%) and GD (27·3%) muscles indicating that these latter two treatments should provide more tender meat.

Immunodetection of cathepsins B and L present in and secreted from human pre-malignant and malignant colorectal tumour cell lines.

Pre-malignant and malignant human colorectal tumour epithelial cell lines both secreted precursor forms of the 2 cysteine proteinases, cathepsins B and L. The amount of proteinases secreted by these cell lines varied according to the cell density. Comparison at similar cell densities showed that the pre-malignant, adenoma-derived cell line (PC/AA) secreted as much, or more, of both cathepsin B and L precursors as did the malignant, carcinoma-derived cell line (PC/JW/FI).

A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen.

We have separated four cathepsins (B, L, N and S) from rabbit spleen. They are all collagen-degrading cysteine proteinases, with Mr values of 25,250, 23,500, 34,000 and 30,000 for cathepsin B, L, N and S respectively. Cathepsins B, N and S have isoelectric points of 5.

Elevation of cathepsin L levels in the synovial lining of rabbits with antigen-induced arthritis.

The activity and distribution of the collagenolytic lysosomal enzyme, cathepsin L, has been assessed in the synovial lining of the rabbit during the initiation and development of chronic (antigen-induced) arthritis. Biochemical assay of homogenates of synovial lining revealed a marked increase in the activity of lysosomal enzymes, including cathepsin L, between 1 and 5 days following initiation of arthritis. Elevated levels of these enzymes were still present at 4 weeks duration of arthritis.

Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts.

Osteoclasts and activated macrophages in culture were shown to generate an acidic microenvironment specifically in the attachment zone between the cell and the base of the culture dish. Measurements using pH microelectrodes revealed that osteoclasts, when firmly attached, could achieve a pH fall of about 1 unit min-1 to a limit value of pH 3.0 or less.

Examination of cathepsins B, D, H and L activities in dry-cured hams.

Cathepsins B, D, H and L as well as the glycosidases β-glucuronidase and N-acetyl-β-glucosaminidase were assayed for activity in fresh pork muscles stored for up to 20 days at 4°C and in 3- and 8-month dry-cured hams. Cathepsin B, H and L activities fell by 40-79% after 20 days while cathepsin D activity remained unchanged. All the enzymes were still active after 8 months of dry curing; with the recoveries found to be in the range 14-73%.

Collagenolytic cathepsins of rabbit spleen: a kinetic analysis of collagen degradation and inhibition by chicken cystatin.

We have investigated the steady state kinetics of the degradation of native fibrillar collagen at pH 3.4 by four collagenolytic cathepsins of rabbit spleen. For each enzyme, the dependence of initial velocity on collagen concentration was well described by the Michaelis-Menten mechanism.

The influence of dissolved calcium salts on the degradation of hard-tissue collagens by lysosomal cathepsins.

Bone, calvaria and dentine collagens were incubated with crude preparations of lysosomal cathepsins obtained from liver, spleen and bone cells. Degradation was most rapid near or below pH 4 and the rate of degradation was increased two-to four-fold in the presence of 50-75 mM CaCl2. This concentration of Ca2+ ions was close to the saturating level of ions released from calcium hydroxyapatite in the pH range 3.

Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase.

The conditioning times for beef, calf, lamb, pig and chicken M. pectoralis profundus were determined from extensibility measurements at 15°C. Extracts from the same muscle from these animals and also rabbit were assayed for free and total cathepsin activities using a new method to determine the extent of inhibition by cystatins.

Degradation of myofibrils from rabbit, chicken and beef by cathepsin l and lysosomal lysates.

The degradation of rabbit, chicken and beef myofibrils by cathepsin L or lysosomal lysates was studied by SDS-polyacrylamide-gel electrophoresis and electron microscopy (EM). Similar degradation patterns were observed for each myofibrillar preparation incubated with cathepsin L, except that myosin heavy chain and tropomyosin of beef were more susceptible than those of rabbit and chicken. Otherwise, troponin T, troponin in I and C-protein were rapidly degraded with slower degradation of titin, nebulin, myosin heavy chain, α-actinin, α-tropomyosin, actin and myosin light chains, LC1 and LC2.

The immunohistochemical location of cathepsin L in rabbit skeletal muscle. Evidence for a fibre type dependent distribution.

The immunohistochemical location of cathepsin L in rabbit soleus, plantaris and psoas muscles was investigated using the peroxidase-anti-peroxidase (PAP) technique. The amount of enzyme detected varied according to the fibre type, which were identified by histochemical staining of serial sections for succinate dehydrogenase and alkali-stable myosin ATPase. In the three muscles studied labelling was strongest in the highly oxidative fibres and weaker in the other fibre types with least staining in the fast white fibres.