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  • 1
    Online Resource
    Online Resource
    Hydrolases in GtoPdb v.2023.1
    University of Edinburgh ; 2023
    In:  IUPHAR/BPS Guide to Pharmacology CITE Vol. 2023, No. 1 ( 2023-04-26)
    Details
    In: IUPHAR/BPS Guide to Pharmacology CITE, University of Edinburgh, Vol. 2023, No. 1 ( 2023-04-26)
    Abstract: Listed in this section are hydrolases not accumulated in other parts of the Concise Guide, such as monoacylglycerol lipase and acetylcholinesterase. Pancreatic lipase is the predominant mechanism of fat digestion in the alimentary system; its inhibition is associated with decreased fat absorption. CES1 is present at lower levels in the gut than CES2 (P23141), but predominates in the liver, where it is responsible for the hydrolysis of many aliphatic, aromatic and steroid esters. Hormone-sensitive lipase is also a relatively non-selective esterase associated with steroid ester hydrolysis and triglyceride metabolism, particularly in adipose tissue. Endothelial lipase is secreted from endothelial cells and regulates circulating cholesterol in high density lipoproteins.
    Type of Medium: Online Resource
    ISSN: 2633-1020
    URL: Article
    DOI: 10.2218/gtopdb/F799/2023.1
    Language: Unknown
    Publisher: University of Edinburgh
    Publication Date: 2023
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  • 2
    Online Resource
    Online Resource
    Hydrolases (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database
    University of Edinburgh ; 2019
    In:  IUPHAR/BPS Guide to Pharmacology CITE Vol. 2019, No. 4 ( 2019-09-16)
    Details
    In: IUPHAR/BPS Guide to Pharmacology CITE, University of Edinburgh, Vol. 2019, No. 4 ( 2019-09-16)
    Abstract: Listed in this section are hydrolases not accumulated in other parts of the Concise Guide, such as monoacylglycerol lipase and acetylcholinesterase. Pancreatic lipase is the predominant mechanism of fat digestion in the alimentary system; its inhibition is associated with decreased fat absorption. CES1 is present at lower levels in the gut than CES2 (P23141), but predominates in the liver, where it is responsible for the hydrolysis of many aliphatic, aromatic and steroid esters. Hormone-sensitive lipase is also a relatively non-selective esterase associated with steroid ester hydrolysis and triglyceride metabolism, particularly in adipose tissue. Endothelial lipase is secreted from endothelial cells and regulates circulating cholesterol in high density lipoproteins.
    Type of Medium: Online Resource
    ISSN: 2633-1020
    URL: Article
    DOI: 10.2218/gtopdb/F799/2019.4
    Language: Unknown
    Publisher: University of Edinburgh
    Publication Date: 2019
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  • 3
    Online Resource
    Online Resource
    Hydrolases & Lipases in GtoPdb v.2023.3
    University of Edinburgh ; 2023
    In:  IUPHAR/BPS Guide to Pharmacology CITE Vol. 2023, No. 3 ( 2023-11-29)
    Details
    In: IUPHAR/BPS Guide to Pharmacology CITE, University of Edinburgh, Vol. 2023, No. 3 ( 2023-11-29)
    Abstract: Listed in this section are hydrolases not accumulated in other parts of the Concise Guide, such as monoacylglycerol lipase and acetylcholinesterase. Pancreatic lipase is the predominant mechanism of fat digestion in the alimentary system; its inhibition is associated with decreased fat absorption. CES1 is present at lower levels in the gut than CES2 (P23141), but predominates in the liver, where it is responsible for the hydrolysis of many aliphatic, aromatic and steroid esters. Hormone-sensitive lipase is also a relatively non-selective esterase associated with steroid ester hydrolysis and triglyceride metabolism, particularly in adipose tissue. Endothelial lipase is secreted from endothelial cells and regulates circulating cholesterol in high density lipoproteins.
    Type of Medium: Online Resource
    ISSN: 2633-1020
    URL: Article
    DOI: 10.2218/gtopdb/F799/2023.3
    Language: Unknown
    Publisher: University of Edinburgh
    Publication Date: 2023
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  • 4
    Online Resource
    Online Resource
    Hydrolases (version 2019.5) in the IUPHAR/BPS Guide to Pharmacology Database
    University of Edinburgh ; 2019
    In:  IUPHAR/BPS Guide to Pharmacology CITE Vol. 2019, No. 5 ( 2019-11-13)
    Details
    In: IUPHAR/BPS Guide to Pharmacology CITE, University of Edinburgh, Vol. 2019, No. 5 ( 2019-11-13)
    Abstract: Listed in this section are hydrolases not accumulated in other parts of the Concise Guide, such as monoacylglycerol lipase and acetylcholinesterase. Pancreatic lipase is the predominant mechanism of fat digestion in the alimentary system; its inhibition is associated with decreased fat absorption. CES1 is present at lower levels in the gut than CES2 (P23141), but predominates in the liver, where it is responsible for the hydrolysis of many aliphatic, aromatic and steroid esters. Hormone-sensitive lipase is also a relatively non-selective esterase associated with steroid ester hydrolysis and triglyceride metabolism, particularly in adipose tissue. Endothelial lipase is secreted from endothelial cells and regulates circulating cholesterol in high density lipoproteins.
    Type of Medium: Online Resource
    ISSN: 2633-1020
    URL: Article
    DOI: 10.2218/gtopdb/F799/2019.5
    Language: Unknown
    Publisher: University of Edinburgh
    Publication Date: 2019
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  • 5
    Online Resource
    Online Resource
    Use of a Fluorogenic Septapeptide Matrix Metalloproteinase Assay to Assess Responses to Periodontal Treatment
    Wiley ; 2000
    In:  Journal of Periodontology Vol. 71, No. 5 ( 2000-05), p. 690-700
    Details
    In: Journal of Periodontology, Wiley, Vol. 71, No. 5 ( 2000-05), p. 690-700
    Abstract: Background: Quantification of gingival crevicular fluid matrix metalloproteinase activity may provide improved assessment of periodontal disease status and response to treatment. A fluorogenic matrix metalloproteinase substrate assay (FSA) has been developed using a methoxycoumarin‐containing septapeptide analog of the α2(I) collagen cleavage site. This substrate exhibits increased fluorescence following cleavage by many matrix metalloproteinases, and the enzyme activity can be readily estimated with a fluorimeter. Here we compared this assay with classical methods of periodontal assessment including bleeding on probing, crevicular fluid flow, and probing depth to assess its utility as an indicator of changes in periodontal status and treatment response. Methods: Complete measurements of probing depth were obtained for Ramfjord teeth on subjects who had been previously treated for periodontitis. Subjects were subsequently divided into groups based on existing periodontal disease severity: gingivitis (n = 21), stable periodontitis (n = 41), and severe periodontitis (n = 50). Crevicular fluid volume, bleeding on probing, and FSA were measured at each Ramfjord tooth or substitute. After baseline measurements, subjects received subgingival scaling and prophylaxis; 3 months later, they were reassessed. Results: FSA measurements were positively associated with severity of disease at baseline. After treatment there were substantial reductions of FSA in gingivitis (∼51%; P 〈 0.01) and severe periodontitis (∼45%; P 〈 0.001), but not in stable periodontitis (13%; P 〉 0.2). All groups showed a positive association between FSA measurements and higher bleeding scores at individual sites. FSA measurements were also positively associated with crevicular fluid flow at baseline, but after treatment there was a ∼67% decrease ( P 〈 0.01) in the highest crevicular fluid flow class. There were significant reductions of FSA at follow‐up for sites with probing depths between 0 to 3 mm (23%; P 〈 0.05) and 4 to 6 mm (31%; P 〈 0.05). However, the largest reduction was for sites with probing depth between 7 to 9 mm (49%; P 〈 0.001). Conclusions: These results indicate that monitoring patients by measurement of matrix metalloproteinase levels in gingival crevicular fluid with the quenched fluorescent substrate assay provides estimates of inflammatory status, periodontal destruction, and response to treatment, especially in more severe periodontitis lesions. J Periodontol 2000; 71:690‐700.
    Type of Medium: Online Resource
    ISSN: 0022-3492 , 1943-3670
    URL: Article
    DOI: 10.1902/jop.2000.71.5.690
    Language: English
    Publisher: Wiley
    Publication Date: 2000
    detail.hit.zdb_id: 2040047-0
    detail.hit.zdb_id: 390921-9
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  • 6
    Online Resource
    Online Resource
    Inflammation Dampened by Gelatinase A Cleavage of Monocyte Chemoattractant Protein-3
    American Association for the Advancement of Science (AAAS) ; 2000
    In:  Science Vol. 289, No. 5482 ( 2000-08-18), p. 1202-1206
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 289, No. 5482 ( 2000-08-18), p. 1202-1206
    Abstract: Tissue degradation by the matrix metalloproteinase gelatinase A is pivotal to inflammation and metastases. Recognizing the catalytic importance of substrate-binding exosites outside the catalytic domain, we screened for extracellular substrates using the gelatinase A hemopexin domain as bait in the yeast two-hybrid system. Monocyte chemoattractant protein–3 (MCP-3) was identified as a physiological substrate of gelatinase A. Cleaved MCP-3 binds to CC-chemokine receptors–1, –2, and –3, but no longer induces calcium fluxes or promotes chemotaxis, and instead acts as a general chemokine antagonist that dampens inflammation. This suggests that matrix metalloproteinases are both effectors and regulators of the inflammatory response.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.289.5482.1202
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2000
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    SSG: 11
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  • 7
    Online Resource
    Online Resource
    A Critical Role for the Membrane-type 1 Matrix Metalloproteinase in Collagen Phagocytosis
    American Society for Cell Biology (ASCB) ; 2006
    In:  Molecular Biology of the Cell Vol. 17, No. 11 ( 2006-11), p. 4812-4826
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 17, No. 11 ( 2006-11), p. 4812-4826
    Abstract: Degradation of collagen is important for the physiological remodeling of connective tissues during growth and development as well as in wound healing, inflammatory diseases, and cancer cell invasion. In remodeling adult tissues, degradation of collagen occurs primarily through a phagocytic pathway. However, although various steps in the phagocytic pathway have been characterized, the enzyme required to initially fragment collagen fibrils for subsequent phagocytosis has not been identified. We have used laser confocal microscopy, transmission electron microscopy, and biochemical assays to show that human fibroblasts initiate degradation of collagen through the collagenase activity of the membrane-bound metalloproteinase MT1-MMP. Degradation of natural and reconstituted collagen substrates correlated with the expression of MT1-MMP, which was localized at sites of collagen cleavage at the surface of the cells and also within the cells, whereas collagen degradation was abrogated when MT1-MMP expression was blocked by small interfering RNA treatment. In contrast to MT1-MMP, the gelatinolytic activity of MMP-2 was not required for collagen phagocytosis. These studies demonstrate a pivotal role of catalytically active MT1-MMP in preparing collagen fibrils for phagocytic degradation.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e06-06-0486
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2006
    detail.hit.zdb_id: 1098979-1
    detail.hit.zdb_id: 1474922-1
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Identification of polymorphonuclear leukocyte collagenase and gelatinase activities in mouthrinse samples: Correlation with periodontal disease activity in adult and juvenile periodontitis
    Wiley ; 1990
    In:  Journal of Periodontal Research Vol. 25, No. 5 ( 1990-09), p. 257-267
    Details
    In: Journal of Periodontal Research, Wiley, Vol. 25, No. 5 ( 1990-09), p. 257-267
    Abstract: In previous studies, elevations in the levels of active and latent collagenase in gingival crevicular fluid (GCF) have been correlated positively with periodontal disease activity. To provide a simple diagnostic approach for testing collagenolytic activity, the feasibility of using a 3.0 ml water mouthrinse to collect GCF simultaneously from all sites in the mouth was assessed. Patients with adult periodontitis (AP, n = 23) and local juvenile periodontitis (LJP, n = 7) were sampled before periodontal therapy and some (12 AP, 4 LJP) were also assessed longitudinally after scaling and root planing, administration of antibiotics, and following periodontal surgery. Healthy patients (n = 19) were used as controls. The levels of active collagenase, procollagenase, and collagenase inhibitor activity were determined by functional assays and quantitated after SDS‐PAGE and fluorography. Gelatinase and progelatinase were assayed by enzymography on gelatin‐substrate gels. Active collagenase levels were found to be significantly higher (14‐ to 20‐fold) in AP and LJP patients compared to controls, whereas matrix metalloproteinase activity was not detected in mouthrinses from edentulous patients. Collagenase inhibitor levels were generally low in all groups of subjects tested. Following clinical treatment the levels of active collagenase and gelatinase were reduced; the reduction was significant for active collagenase after tetracycline treatment and scaling in LJP patients. Of the clinical indices recorded (gingival index, plaque index, and pocket depth) there were no significant correlations with enzyme activity but similar trends were observed between the changes in active collagenase and gingival index. In patients with untreated periodontal disease, collagenase occurred predominantly in the active form. N‐ethylmaleimide (NEM) and p ‐aminophenylmercuric acetate (AMPA) were equally effective as activators of the latent collagenase, indicating that the collagenase was derived from PMNs, which were also the source of the gelatinase. The results of these studies indicate that measurement of active collagenase and gelatinase in mouthrinse samples is potentially useful in the diagnosis and assessment of periodontal disease activity.
    Type of Medium: Online Resource
    ISSN: 0022-3484 , 1600-0765
    URL: Issue
    URL: Article
    DOI: 10.1111/jre.1990.25.issue-5
    DOI: 10.1111/j.1600-0765.1990.tb00914.x
    Language: English
    Publisher: Wiley
    Publication Date: 1990
    detail.hit.zdb_id: 390953-0
    detail.hit.zdb_id: 2025633-4
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  • 9
    Online Resource
    Online Resource
    Proteolytic processing of SDF-1α reveals a change in receptor specificity mediating HIV-associated neurodegeneration
    Proceedings of the National Academy of Sciences ; 2006
    In:  Proceedings of the National Academy of Sciences Vol. 103, No. 50 ( 2006-12-12), p. 19182-19187
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 103, No. 50 ( 2006-12-12), p. 19182-19187
    Abstract: Proteolytic cleavage of constitutively expressed proteins can generate peptides with novel bioactive properties. Matrix metalloproteinase (MMP)-2 cleaves the 4 amino-terminal residues of the chemokine, stromal cell-derived factor (SDF)-1α, yielding a highly neurotoxic molecule, SDF(5-67), which fails to bind to its cognate receptor, CXCR4. Herein, we detected SDF(5-67) in brain monocytoid cells of HIV-infected persons, particularly in those with HIV-associated dementia. SDF(5-67) activated cell type-specific expression of proinflammatory genes including IL-1β, TNFα, indoleamine 2′,3′-dioxygenase (IDO), and IL-10 in both astrocytic and monocytoid cells ( P 〈 0.05). Unlike SDF-1α, SDF(5-67) caused neuronal membrane perturbations with ensuing neurotoxicity and apoptosis ( P 〈 0.05) through engagement of an inducible receptor. CXCR3 antagonists and siRNA-mediated knockdown of CXCR3 inhibited SDF(5-67)-stimulated neurophysiological changes, neuronal death, and neuroimmune activation ( P 〈 0.05). Moreover SDF(5-67) bound directly to CXCR3 in a competitive manner, mediated by its amino terminus. In vivo neuroinflammation, neuronal loss, and neurobehavioral abnormalities caused by SDF(5-67) ( P 〈 0.05) were prevented by a CXCR3 antagonist. These studies reveal additive neuropathogenic properties exerted by a proteolytically cleaved chemokine as consequences of a change in receptor specificity, culminating in neurodegeneration.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.0604678103
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2006
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Matrix Metalloproteinase Activity Inactivates the CXC Chemokine Stromal Cell-derived Factor-1
    Elsevier BV ; 2001
    In:  Journal of Biological Chemistry Vol. 276, No. 47 ( 2001-11), p. 43503-43508
    Details
    In: Journal of Biological Chemistry, Elsevier BV, Vol. 276, No. 47 ( 2001-11), p. 43503-43508
    Type of Medium: Online Resource
    ISSN: 0021-9258
    URL: Article
    DOI: 10.1074/jbc.M107736200
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2001
    detail.hit.zdb_id: 2997-X
    SSG: 12
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