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)

Type IX collagen from chick embryonic cartilage is unique among the collagens in that it contains chondroitin sulfate covalently linked to the alpha 2(IX) polypeptide chain. We have isolated and sequenced the glycosaminoglycan-containing peptide released by collagenase digestion from type IX collagen, labeled biosynthetically with [35SO4] and 3H-aminoacids. This peptide was purified by gel filtration and, following chondroitinase ABC digestion, by reverse-phase high performance liquid chromatography. The amino acid sequence obtained for this peptide has 23 residues, beginning and ending with a collagenous sequence, indicating that it spans an internal noncollagenous domain. Comparison of this sequence with the one predicted from cDNA clone pYN 1738 for the alpha 1(IX)chain and pYN 1731 and pDM 222 for the alpha 2(IX)chain revealed the peptide to be the noncollagenous NC3 domain of alpha 2(IX). The glycosylated sequence Val-Glu-Gly-Ser*-Ala-Asp- of type IX collagen does not have the Ser-Gly normally functioning as the attachment sequence but does have an acidic residue preceding the serine which should improve the acceptability of this sequence for the xylosyltransferase. That it is an adequate acceptor can be inferred from the observation that type IX collagen carries a glycosaminoglycan chain on over 70% of the molecules isolated.
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PMID:Isolation and sequence analysis of the glycosaminoglycan attachment site of type IX collagen. 333 23

Electrical currents associated with sodium-coupled alanine transport in mouse pancreatic acinar cells were studied using the method of whole-cell recording with patch pipettes. Single cells or small clusters of (electrically coupled) cells were isolated by collagenase treatment. The composition of the intracellular solution could be controlled by internal perfusion of the patch pipette. In this way both inward and outward currents could be measured under "zero-trans" conditions, i.e., with finite concentrations of sodium and L-alanine on one side and zero concentrations on the other. Inward and outward currents for equal but opposite concentration gradients were found to be of similar magnitude, meaning that the cotransporter is functionally nearly symmetric. The dependence of current on the concentrations of sodium and L-alanine exhibited a Michaelis-Menten behavior. From the sodium-concentration dependence of current as well as from the reversal potential of the current in the presence of an alanine-concentration gradient, a sodium/alanine stoichiometric ratio of 1:1 can be inferred. The finding that N-methylated amino acids may substitute for L-alanine, as well as the observed pH dependence of currents indicate that the pancreatic alanine transport system is similar to (or identical with) the "A-system" which is widespread in animal cells. The transport system is tightly coupled with respect to Na+; alanine-coupled inward flow of Na+ is at least 30 times higher than uncoupled Na+ flow mediated by the cotransporter. The current-voltage characteristic of the cotransporter could be (approximately) determined from the difference of transmembrane current in the presence and in the absence of L-alanine. The sodium-concentration dependence of the current-voltage characteristic indicates that a Na+ ion approaching the binding site from the extracellular medium has to cross part of the transmembrane electric field.
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PMID:Electrogenic properties of the sodium-alanine cotransporter in pancreatic acinar cells: I. Tight-seal whole-cell recordings. 356 Feb 1

1. Experiments were made to determine whether the purified lysosomal proteinases, cathepsins B1 and D, degrade acid-soluble collagen in solution, reconstituted collagen fibrils, insoluble collagen or gelatin. 2. At acid pH values cathepsin B1 released (14)C-labelled peptides from collagen fibrils reconstituted at neutral pH from soluble collagen. The purified enzyme required activation by cysteine and EDTA and was inhibited by 4-chloromercuribenzoate, by the chloromethyl ketones derived from tosyl-lysine and acetyltetra-alanine and by human alpha(2)-macroglobulin. 3. Cathepsin B1 degraded collagen in solution, the pH optimum being pH4.5-5.0. The initial action was cleavage of the non-helical region containing the cross-link; this was seen as a decrease in viscosity with no change in optical rotation. The enzyme also attacked the helical region of collagen by a mechanism different from that of mammalian neutral collagenase. No discrete intermediate products of a specific size were observed in segment-long-spacing crystalloids (measured as native collagen molecules aligned with N-termini together along the long axis) or as separate peaks on gel filtration chromatography. This suggests that once an alpha-chain was attacked it was rapidly degraded to low-molecular-weight peptides. 4. Cathepsin B1 degraded insoluble collagen with a pH optimum below 4; this value is lower than that found for the soluble substrate, and a possible explanation is given. 5. The lysosomal carboxyl proteinase, cathepsin D, had no action on collagen or gelatin at pH3.0. Neither cathepsin B1 nor D cleaved Pz-Pro-Leu-Gly-Pro-d-Arg. 6. Cathepsin B1 activity was shown to be essential for the degradation of collagen by lysosomal extracts. 7. Cathepsin B1 may provide an alternative route for collagen breakdown in physiological and pathological situations.
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PMID:Cathepsin B1. A lysosomal enzyme that degrades native collagen. 420 88

Actively growing aerobic and anaerobic bacteria were screened by a plate assay, with reconstituted guinea pig collagen as a substrate, for their ability to produce a collagenolytic factor. Collagenolytic activity was not demonstrated among the aerobic organisms tested, with the exception of one strain of Staphylococcus aureus (only when grown under anaerobic conditions). Collagenolytic activity, however, was detected in cultures of Clostridium tetani and Bacteroides species other than B. melaninogenicus. Collagenolytic activity of these organisms could be confirmed by measuring the amount of hydroxyproline liberated from the collagen gel during growth. Although collagenase production by Pseudomonas aeruginosa has been suggested in previous reports, our results were negative. An extracellular fraction of P. aeruginosa was able to hydrolyze a synthetic hexapeptide Cbz-glycyl-l-prolyl-glycyl-glycyl-l-prolyl-l- alanine, but was without detectable effect on reconstituted collagen.
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PMID:Collagenolytic activity of bacteria. 430 39

1. A hydroxyproline-containing protein was isolated from the soluble fraction of sandal leaves (Santalum album L.) and the purified protein was homogeneous by disc electrophoresis. 2. It is a glycoprotein containing 16% carbohydrate, the components of which were mainly arabinose, with only small amounts (about 5%) of galactose. The principal amino acids were glutamic acid, aspartic acid, glycine, alanine, arginine, lysine, proline and hydroxyproline, which together comprised 60% of the total. The number of acidic amino acids exceeds the number of basic amino acids. By Sephadex gel filtration, the approximate molecular weight was found to be about 63000. The ratio of residues of hydroxyproline to those of arabinose was 1:2. 3. The native protein is resistant to the action of several proteolytic enzymes. After partial hydrolysis with 0.1m-HCl, the protein became susceptible to attack by Pronase but remained resistant to collagenase.
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PMID:Isolation and characterization of a hydroxyproline-containing protein from soluble extracts of the leaves of sandal (Santalum album L.). 437 67

Six collagenases present in the culture filtrate of Clostridium histolyticum have been purified to homogeneity. Chromatography over hydroxylapatite, Sephacryl S-200, and L-arginine-Affi-Gel 202 removes the brown pigment and the great majority of the contaminating proteinases active against casein, benzoyl-L-arginine ethyl ester, and elastin. Reactive Red 120 dye ligand chromatography subdivides the collagenases, which have very similar physicochemical properties, among four fractions. The final purification is achieved by chromatography over DEAE-cellulose and SP-Sephadex. All six collagenases, designated alpha, beta, gamma, delta, epsilon and zeta by the order of their purification, are highly active against collagen and devoid of other proteolytic activities. Each exhibits a single band on sodium dodecyl sulfate-polyacrylamide gels. Two distinct subspecies of the alpha and gamma enzymes have been isolated, which have the same molecular weight and activity but different isoelectric points. There is some less pronounced microheterogeneity for the other collagenases. On the basis of their activities toward native collagen and the synthetic peptide 2-furanacryloyl-L-leucylglycyl-L-prolyl-L-alanine (FALGPA), the six collagenases are divided into two classes. Class I collagenases (alpha, beta, and gamma) have high collagenase activity and moderate FALGPA activity while the class II collagenases (sigma, epsilon, and sigma) have moderate collagenase and high FALGPA activities. The relationship between these six collagenases and other reported to have been isolated in the literature has also been examined.
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PMID:Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. 608 87

To facilitate the structural studies of invertebrate collagens, a sensitive and effective method was developed, using reverse-phase high-performance liquid chromatography for preparative isolation of the collagen subunits and their clostridial collagenase-derived peptides; the methods have been applied to Nereis cuticle collagen. The two subunits of denatured Nereis cuticle collagen, termed A and B, were initially separated by high-performance liquid chromatography. These polypeptides, with Mr of about 0.5 million, were each exhaustively digested with clostridial collagenase. The digest of the A subunit, which contains all of the uronic acid, was enriched for the uronic acid-containing glycopeptides by means of gel filtration. These glycopeptides were resolved into 23 major peaks, using reverse-phase HPLC, over a 5-h elution time, with an acetonitrile gradient (0-20%) containing 0.1% TFA. The amino acid composition data suggests that the peptides are of variable length, from 5 to 17 residues, while beta-elimination studies show that the uronic acid-containing moieties are all O-glycosidically linked to threonine residues, in the peptides examined. The amino acid sequence of one of the major glycopeptides was determined and found to be Gly-Hyp-Ala-Gly-Gly-Ile-Gly-Glu-Thr-Gly-Ala-Val-Gly-Leu-Hyp. The amino acid compositions of glycosylated and nonglycosylated peptides which had eluted, numbering about 100, showed a correspondence between hydrophobicity or hydrophilicity and emergence time from the column. We also found that the peptides most enriched in 4-hydroxyproline emerged earliest. These studies provide a foundation for elucidating the detailed structures of the large, unusual subunits of a well-characterized cuticle collagen.
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PMID:High-performance liquid chromatographic separation of glycopeptides from Nereis cuticle collagen. 609 22

To investigate the possible participation of prostaglandins in the activation of collagenolytic enzymes of the follicular wall at ovulation, we measured the activities of neutral and acid collagenase in the rabbit ovaries at various stages of follicular development by using synthetic substrate DNP-Pro-Gln-Ile-Ala-Gly-Gln-D-Arg OH (DNP peptide) with its optimal pH 7.6 and alpha-N-benzoyl-DL-arginine-2-naphthylamide HCl (BANA) with pH 6.0, and the effect of ovulation-blocking doses of indomethacin (4 mg/kg) on DNP peptidase and BANA hydrolase activities were investigated. DNP peptidase and BANA hydrolase activities were increased toward ovulation with the highest level 7 to 9hrs after the hCG injection and then decreased significantly at 10hr. At 11hr, around the time of ovulation, the activity stayed at its low level, then rose by 13hr. Following the concomitant administration of IM with hCG, ovulation was blocked and the preovulatory increases in DNP peptidase and BANA hydrolase activities were not observed and their activities stayed at the low level until 20hr. It is suggested that collagenolytic activity for the ovulatory process started to intensiby 6hrs and ended 3hrs prior to ovulation and PGs are necessary for the enzymatic activation of DNP peptidase and BANA hydrolase.
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PMID:[Effect of indomethacin on collagenolytic enzyme activities in rabbit ovary]. 609 61

To elucidate the mechanisms of follicular rupture at ovulation in human, activities of collagenolytic enzymes were measured in the human follicles at various stages of development by using two kinds of synthetic substrates, alpha-N-benzoyl-DL-arginine-2-naphthylamide HCl and N-carbobenzoxy-glycyl-prolyl-glycyl-glycyl-prolyl-alanine. The result clarified that human ovaries did have two kinds of collagenolytic activities, one cathepsin B1 with its optimal pH 6.0, the other neutral collagenase with its optimal pH 7.5. To examine the subtle changes of these enzymatic activities in the follicles during ovulatory processes, the follicle wall was dissected into three parts, namely, the granulosal layer, the apical wall and the basal wall without the granulosal layer. Activity of neutral collagenase presented a continuous increase in the follicular wall, while in the granulosal layer its gradual depletion was observed. Cathepsin B1 revealed a significant drop of its activity in the apical wall around a preovulatory period. These results indicate an involvement of collagenolytic enzymes in the human ovulatory process.
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PMID:[Activities of collagenolytic enzymes in the human ovary (author's transl)]. 626 91

To investigate the role of non-ACTH pituitary peptides on steroidogenesis, we studied the effects of synthetic beta-lipotropin, beta-melanotropin, and beta-endorphin on aldosterone and corticosterone stimulation using rat adrenal collagenase-dispersed capsular and decapsular cells. beta-lipotropin induced a significant aldosterone stimulation in a dose-dependent fashion (10 nM-1 muM). beta-endorphin, which is the carboxyterminal fragment of beta-lipotropin, did not stimulate aldosterone production at the doses used (3 nM-6 muM). beta-melanotropin, which is the middle fragment of beta-lipotropin, showed comparable effects on aldosterone stimulation. beta-lipotropin and beta-melanotropin did not affect corticosterone production in decapsular cells. Although ACTH(1-24) caused a significant increase in cyclic AMP production in capsular cells in a dose-dependent fashion (1 nM-1 muM), beta-lipotropin and beta-melanotropin did not induce an increase in cyclic AMP production at the doses used (1 nM-1 muM). The beta-melanotropin analogue (glycine[Gly](10)-beta-melanotropin) inhibited aldosterone production induced by beta-lipotropin or beta-melanotropin, but did not inhibit aldosterone production induced by ACTH(1-24) or angiotensin II. Corticotropin-inhibiting peptide (ACTH(7-38)) inhibited not only ACTH(1-24) action but also beta-lipotropin or beta-melanotropin action; however it did not affect angiotensin II-induced aldosterone production. (saralasin [Sar](1); alanine [Ala](8))-Angiotensin II inhibited the actions of beta-lipotropin and beta-melanotropin as well as angiotensin II. These results indicate that (a) beta-lipotropin and beta-melanotropin cause a significant stimulation of aldosterone production in capsular cells, (b) beta-lipotropin and beta-melanotropin have a preferential effect on zona glomerulosa cells, (c) beta-melanotropin contains the active peptide core necessary for aldosterone stimulation, (d) the effects of these peptides on aldosterone production may be independent of cyclic AMP, and (e) the receptors for beta-lipotropin or beta-melanotropin may be different from those for ACTH or angiotensin II.
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PMID:Effects of beta-lipotropin and beta-lipotropin-derived peptides on aldosterone production in the rat adrenal gland. 626 63


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