Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.24.3 (collagenase)
18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cold-insoluble globulin was detected in both trophoblast and alveolar basement membrane preparations, whereas it was not detected in GBM preparations. Acidic structural glycoproteins from both placental villi and lung parenchyma, which were extracted with 0.3 M acetic acid and recovered by adjusting the pH to 4.7, also contained CIg. Fractions of TBM, solubilized by either dilute alkali (0.01 N NaOH), by reduction and alkylation of the disulfide bonds, or by 0.3 M acetic acid extraction, all contained the antigen and possessed properties similar to those of ASG. The ASG fractions also reacted with antifibrinogen, but proof that the two types of determinants occur on a given molecular species is lacking at present. Purified collagenase solubilized CIg from ABM, from lung parenchyma, and from the stroma of placental villi, and this finding is strong evidence for an association of CIg with collagen in these connective tissues.
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PMID:Presence of fibronectin in basement membranes and acidic structural glycoproteins from human placenta and lung. 9 37

Basement membrane (type IV) collagens were extracted from a mouse tumour with acetic acid and from human placenta after limited enzymatic digestion. Antisera were produced against both collagens in rabbits and guinea-pigs and examined by various assays. These antisera were found to be specific for basement membrane collagen and showed little or no cross-reactions with the interstitial collagens, types I, II and III or with human placenta collagen consisting of alpha A and alpha B chains. Varying degrees of cross-reaction were observed between antisera to human and mouse type IV collagen. Immunochemical analyses demonstrated the presence of three distinct determinants in the tumour type IV collagen. Rabbit antisera against this antigen reacted with either collagenase-resistant segments or with a collagenous, disulphide-bonded segment (P3). Guinea-pig antisera recognized primarily antigenic determinants in the P3 segment. Antisera to placenta type IV collagen reacted with another collagenous, pepsin fragment (P1) which lacks disulphide bonds. These antisera showed complete cross-reaction with collagenous alpha 1 (IV) chains prepared from pepsin-digests of human placenta and bovine lens capsule.
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PMID:Immunochemical study on basement membrane (type IV) collagens. 9 54

The presence of collagen in lung is fundamental in normal lung structure and function. Methods have been developed to examine human fetal and adult lung collagen with respect to its composition and synthesis. The second trimester fetal lung has a large number of cells per unit lung mass (36.6 plus or minus 2.7 mug DNA/mg dry wt) and relatively small amounts of collagen (17.0 plus or minus 5.3 mug collagen/mg dry wt). The number of cells per unit lung mass in the adult lung (11.1 plus or minus 3.4 mug DNA/mg dry wt) is 30% of the number of cells in the fetal lung, but the adult has 11 times more collagen (196 plus or minus 25 mug collagen/mg dry wt). The composition of fetal lung collagen can be partially characterized by extraction with salt at neutral pH, acetic acid, or guanidine. The extracted chains, representing 10% of the total lung collagen, chromatograph as alpha1 and alpha2 chains, each with a mol wt of 100,000 and an animo acid composition characteristic for collagen but not specific for lung. Short-term explant cultures of fetal and adult lung synthesize alpha chains which can be isolated by ion-exchange chromatography. These chains, representing 30-40% of the total collagen synthesized by the explants, coelectrophorese with extracted collagen chains on acrylamide gels: they are destroyed by clostridial collagenase and they have a mol wt of 100,000. Although the composition of the collagen synthesized by these explants can be only partially characterized, the rate of synthesis of both collagen and noncollagen protein can be quantitated. In fetal lung, 4.0 plus or minus 1.2% of the amino acids incorporated into protein per hour are incorporated into collagen. In normal adult lung, this percentage (4.2 plus or minus 0.9%) is remarkably similar. These values are almost identical to the relative rate of collagen synthesis in rabbit lung in the same age range. This technology should be applicable to answer specific questions regarding collagen synthesis and degradation in human lung disease.
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PMID:Collagen in the human lung. Quantitation of rates of synthesis and partial characterization of composition. 16 49

Two genetic types of collagenous proteins, type I and type III, were isolated by extraction and differential salt precipitation from rat skin. The yield of collagen precursors was increased by injecting animals with colchicine 30 min before sacrifice to inhibit secretion of collagen. DEAE-cellulose chromatography was used to separate collagen from collagen precursors. Although these preparations contained more type I collagen than type III collagen, there were always more type III than type I precursors. The precursor chains of type I fractions were separated on CM-cellulose chromatography after denaturation. Three precursor forms were found for each collagen alpha chain, a complete chain (proalpha chain), and a precursor chain with only an amino-terminal (pNalpha chain) and carboxy-terminal extension (pCalpha chain). Species differences were demonstrated between rat collagen precursors and other species using rat calvaria (frontal and parietal) bones extracted with either 0.5 N acetic acid or neutral salt buffers containing protease inhibitors. Native rat procollagen elutes earlier than chicken or human procollagen on DEAE-cellulose chromatography and does not separate significantly from the pC collagen form. The collagenase resistant amino terminal peptides of rat pNalpha1 and pNalpha2 were the same size (16 000) but could be separated by DEAE-cellulose chromatography.
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PMID:Characterization of collagen precursors found in rat skin and rat bone. 19 97

The present report describes high yield enzymatic radio-iodination of the apical and basal-lateral plasma membranes of toad bladder epithelium, by a procedure that does not breach the functional integrity of the epithelium, as assessed by the basal and vasopressin-sensitive short-circuit current (SCC). Restriction of the label to the membrane surface, was ascertained by light and electron-microscopic autoradiographs. On the apical surface, the grains were over the glycocalyx and the plasma membrane. Analysis of the labeled glycocalyx by agarose gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), as well as enzymatic and pH-dependent hydrolysis indicated that the glycocalyx is a trichloro-acetic acid-soluble macromolecular complex of high molecular weight composed of a peptide moiety attached to large prosthetic groups (presumably carbohydrates) by O-glycosidic bonds. Analysis of the labeled apical plasma membrane components by agarose gel filtration and SDS-PAGE disclosed the presence of six major species of apparent molecular weights: 23,000, 28,000, 37,000, 44,000, 68,000, and 95,000. More than half of the membrane-associated radio-iodine was in two bands of molecular weights 37,000 and 44,000. Concentrations of vasopressin and cyclic AMP sufficient to increase the SCC significantly did not modify the extent of membrane labeling or the distribution of the label among the apical membrane components (presumably proteins) as assessed by SDS-PAGE. Iodination in the presence of amiloride inhibited incorporation but did not change the pattern of the distribution of the label among the components resolved by SDS-PAGE. Iodination of basal-lateral plasma membranes, at a yield comparable to that obtained with apical labeling, was attained after about 30 min of exposure of the intact bladder to the labeling solutions. Approximately 25% of the basal-lateral labeling was lost when the epithelial cells were harvested after collagenase treatment, implying that some iodination of the basement membrane had taken place. Less than 10% of iodination of the apical or basal-lateral surfaces was accounted for by lipid-labeling. Analysis of the labeled apical and basal-lateral species by enzymatic digestion and thin layer chromatography disclosed that virtually all the radioactivity was present as mono-iodotyrosine (MIT).
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PMID:Radio-iodination of plasma membranes of toad bladder epithelium. 37 44

The extraction of isolated vertebrate smooth muscle cells at high and low ionic strength yields cell ghosts which are seen in the electron microscope to be composed of a complex network of 10-nm filaments, together with residual actin. After SDS-gel electrophoresis of the cell ghosts only 2 bands may be recognized, one corresponding to actin and the other migrating at about 55 000 mol. wt that arises from the 10-nm filaments. The 10-nm filaments are extremely sensitive to proteolysis and are absent from cells exposed to crude collagenase in the presence of Triton X-100. Such cells, lacking 10-nm filaments, still contract in response to ATP. The data indicate that the 10-nm filaments are not essential for contraction, but rather form a specialized intracellular cytoskeleton. While completely insoluble in concentrated salt solutions the 55 000 mol. wt protein is readily extracted with acetic acid from homogenized and salt-extracted smooth muscle residue. The extracted protein reassembles, on dialysis, into filaments of about 10-nm diameter and has an amino acid composition almost identical to that deduced for vertebrate neurofilaments. From the cytoskeletal role that the 10-nm filaments play in smooth muscle and, as appears likely, in other cell types the filament protein has been tentatively termed 'skeletin'. Results relating to the proportion of skeletin in smooth muscle and the structure of the 10-nm filaments are described and discussed.
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PMID:Studies on the function and composition of the 10-NM(100-A) filaments of vertebrate smooth muscle. 56 Oct 84

Cold-insoluble globulin (CIG), which is immunochemically indistinguishable from the fibroblast surface protein known as large external transformation-sensitive glycoprotein and fibronectin, was detected immunologically in connective tissue fractions from adult human lung. The fractions tested were (a) intact parenchyma, (b) acidic structural glycoproteins (ASG) extracted from lung parenchyma with 0.3 M acetic acid, and (c) isolated alveolar basement membrane (ABM). For comparison with ABM, preparations of human glomerular basement membrane and human trophoblast basement membrane (TBM) were tested. CIG was not detected in glomerular basement membrane but was present in large amounts in TBM. The CIG antigen could be solubilized from the parenchyma and from ABM by collagenase digestion which indicates that CIG occurs in lung connective tissue in association with collagen. Fibrinogen antigenic determinants were present in the ASG fraction, but the question of whether CIG and fibrin(ogen) are associated in lung connective tissue requires further study. When CIG was quantified by electroimmunoassay, intact lung parenchyma contained approximately equal to 0.4% CIG, ASG contained 3-4.5% CIG, ABM contained 0.1-0.9% CIG and TBM contained 1.5%-7.2% Cg. the evidence suggests that CIG is a chemical constituent of lung connective tissue matrix where it may influence the function of alveoli.
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PMID:Cold-insoluble globulin (fibronectin) in connective tissues of adult human lung and in trophoblast basement membrane. 70 73

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

The susceptibility of the organic matrix from permanent bovine incisor roots to proteolytic breakdown after in vitro lesion formation was investigated. Root surfaces were exposed to 0.1 M acetic acid, pH 4.0, to produce erosive lesions or to 0.1 M lactic acid, 0.2 mM methane hydroxy diphosphonate, pH 5.0, to produce subsurface lesions. After demineralization, the roots were treated with a bacterial collagenase. The quantity of enzyme-degradable collagen in the root tissue was found to be proportional to the calcium released during demineralization, until a plateau value was reached at calcium concentrations in solution of 3.3 mM at pH 4.0 and 2.7 mM at pH 5.0. The degradability of collagen was found to be substantially less in subsurface lesions than in erosive lesions. The presence of cementum-free areas did not affect the results. These findings suggest that the mineral component of the roots is composed of several fractions which differ in their solubility properties in weak acids.
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PMID:Susceptibility of the collagenous matrix from bovine incisor roots to proteolysis after in vitro lesion formation. 164 3

To investigate the destructive process of connective tissues in gastric ulcer, both collagenolytic and gelatinolytic activities were examined in the homogenates of rat acetic acid-induced gastric ulcer, a typical model of chronic ulcer. Gelatinolytic activity in the ulcerous lesion was significantly higher than that in the normal tissue. However, collagenase was not detected in both normal and ulcerated tissues either by the enzyme assay or by the immunoblotting. By gelatin-gel-zymographic analyses, the gelatinolytic activity was found to be composed of a number of species, mainly 60-, 72- and 92-kDa, all of which were inhibited by ethylenediaminetetraacetic acid. Among the induced matrix metalloproteinases, one crossreacted with a sheep anti-(rabbit prostromelysin)antibody. Thus, in chronic gastric ulcer, it is likely that several metalloproteinases participate in degradation of connective tissue matrices including components of basement membranes. The elevated levels of gelatinolytic activities in the ulcerous tissues and ulcer index were significantly suppressed by treating the animals with famotidine or a new H2-receptor antagonist, 3-amino-4-[4-[4-(1-piperidinomethyl)-2-pyridyloxy]-cis-2- butenylamino]-3-cyclobutene-1,2-dione hydrochloride (IT-066).
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PMID:Effects of H2-receptor antagonists on matrix metalloproteinases in rat gastric tissues with acetic acid-induced ulcer. 168 58


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