Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To determine whether immune complex-like material is incorporated into the extracellular matrix (ECM) of proliferated RA synovium, cell-free matrices were isolated from pannus removed at joint replacement surgery, and were subjected to differential extraction. When the IgG and albumin concentrations in the ECM extracts were compared to those in simultaneously obtained synovial fluids, the IgG was found to be enriched 8.8-fold. Approximately 95% of the IgG was extractable with 6M Guanidine-HCl and 8 M Urea-B-ME. Further extraction with collagenase and low-pH buffers did not result in any additional recovery of IgG. Matrix-associated IgG demonstrated a restricted mobility on IEF with a pI of 4.8. The extracellular matrix of RA pannus is enriched in an acidic IgG species. Incorporation of IgG appears to be secondary to non-covalent interactions and may represent an additional reservoir of immune complex material in the rheumatoid joint.
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PMID:Synovial extracellular matrix II. Specific incorporation of immunoglobulin into the cell-free matrix of pannus. 139 21

Matrix proteins of bone, dentin and cementum have been shown to play a role in bone induction during the mineralization process, and in regulating the activities of several types of mesenchymal cells. Whether these biological functions are mediated through the same mechanism or whether there is specific modulation in each biological process is still open to speculation. The purpose of this pilot investigation was to compare the non-collagenous proteins among these tissues. Bone and teeth, obtained from clinically healthy subjects, were sectioned into 1 mm thick pieces. With the aid of a dissecting microscope, cementum and dentin were separated and collected. Tissue specimens were extracted sequentially in three steps by solutions containing 0.5 M acetic acid, 4 M Guanidine/0.5 M EDTA, and 250 units/ml bacterial collagenase, respectively. Proteins extracted were dialyzed, lyophilized and then further analyzed by both 10% SDS-PAGE (1-D) and two-dimensional (2-D) SDS-PAGE. Comparison showed that the three extraction buffers had relatively different extraction capacities within and among each tissue. The components extracted by acetic acid and Guanidine/EDTA were similar, but seemed different from that extracted by bacterial collagenase as shown by 10% SDS-PAGE. Two-dimensional SDS-PAGE further characterized numerous distinct protein spots from bone (MW of 61, 55, 40, 35, 34, 33 kD and eleven distinct spots which showed MW between 10 and 29 kD, pI range of 5.6-6.4), dentin (MW of 59, 54, 35, 28, 25, 24, 21 kD), and cementum (MW of 71, 64-65, 58, 55, 52, 50, 47, 43, 40, 31, 19 kD).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Biochemical comparisons of matrix proteins extracted from healthy human alveolar bone, dentin and cementum. 149 6

Non-confluent cell cultures were exposed to both guanidine and guanidine-EDTA extracts of cementum, dentine and alveolar bone, at concentrations from 2 to 50 micrograms/ml for 48 h. The cells were radioactively labelled during the last 24 h. Total protein production was measured via incorporation of radioactive proline; collagen production was estimated by digestion of the radioactive protein mixture with bacterial collagenase. All guanidine-EDTA extracts elicited statistically-significant increases in total protein production when compared to controls. At 50 micrograms/ml of extract, the increase in protein production was 340, 143 and 338 per cent for bone, cementum and dentine, respectively. Similar results were obtained for collagen production. Guanidine-EDTA extracts also stimulated an increase in the production of specific proteins, as ascertained by gel electrophoresis. In contrast, the guanidine extracts had no effect on either protein or collagen production. Thus the functions of gingival fibroblasts can be altered by proteins from associated mineralized tissues. Identification of such proteins and their biological functions would enhance knowledge of the mechanisms that regulate connective-tissue regeneration.
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PMID:Enhancement by extracts of mineralized tissues of protein production by human gingival fibroblasts in vitro. 350 58

RNA was extracted from fetal calf skin by two different procedures, using phenol or guanidine hydrochloride. Poly(A)-rich RNA was separated by oligo(dT)-cellulose affinity chromatography and was further fractionated by sucrose density gradient centrifugation. When translated in an optimized wheat germ extract cell-free system, unfractionated guanidine-hydrochloride-extracted poly(A)-rich RNA directed the synthesis of two collagenase-sensitive protein bands, while phenol-extracted poly(A)-rich RNA with a sedimentation coefficient higher than 25 S was the only fraction to direct the same synthesis. On the basis of their electrophoretic mobility on a sodium dodecylsulfate/urea/polyacrylamide gel, these proteins were identified with procollagen alpha 1(I) and procollagen alpha 2. Inhibition of translation by phenol-extracted poly(A)-rich RNA with a sedimentation coefficient lower than 25 S was also observed. Guanidine-hydrochloride-extracted poly(A)-rich RNA from fetal skin directed the synthesis of three distinct collagenase-sensitive proteins in the micrococcal-nuclease-digested rabbit reticulocyte cell-free system; these seemed to correspond to procollagen alpha 1(I), procollagen alpha 2 and procollagen alpha 1 (III).
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PMID:Extraction and translation of collagen mRNA from fetal calf skin. 615 27

When skeletal, cardiac, and smooth muscle is exhaustively extracted with a protein-unfolding reagent such as 6 M guanidine HCl and a disulfide-reducing reagent such as 5% beta-mercaptoethanol, a tissue ghost remains intact and retains the characteristic shape and dimensions of the tissue before extraction. In the case of chicken pectoral muscle, the tissue ghost contains 1% of the original muscle proteins. Guanidine HCl extraction followed by collagenase treatment of glycerol-extracted chicken pectoral muscle releases a clean preparation of elongated structures containing 0.2% of the original protein and representing the covalently cross-linked remnants of the muscle fibers. The material of these muscle fiber ghosts extends throughout the interior of the cell. Antibodies raised against the tissue ghosts of smooth muscle cross-react with glycerol extracted skeletal myofibrils, forming a banding pattern which coincides with the banding pattern observed when myofibrils are reacted with antibodies against titin. Titin, a large and soluble protein found in skeletal muscle, cross-reacts with our antigizzard antibody. However, amino acid analysis of the muscle fiber ghosts indicates that titin cannot be the only subunit of the insoluble polymer, but that one or more proteins with a very high glycine and alanine content and a very low basic and acidic amino acid content must also form part of the covalently cross-linked matrix. The possibility is presented that this matrix may be the basis of the superthin 2-3-nm filaments which have been observed in a variety of cell types.
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PMID:A covalently cross-linked matrix in skeletal muscle fibers. 636 89