Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00750 (PLA)
 16,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In vitro effect of cisplatin and other biological response modifiers has been studied. It is observed that in vitro treatment of macrophage monolayers with cisplatin, rIFN Y, LPS or MDP either alone or in combination showed significantly increased activity of lysozyme, plasminogen activator and decreased activity of 5' nucleotidase. Priming of macrophages with rIFN Y had a significant effect in enhancing the activity of lysozyme and plasminogen activator when subsequently treated with cisplatin, MDP or LPS.
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PMID:Effect of cisplatin and other biological response modifiers on the activity of lysozyme, plasminogen activator and 5' nucleotidase by murine macrophages in vitro. 212 98

P388D1 is a murine macrophage cell line which spontaneously secretes plasminogen activator (PA; activated function) and lysozyme (LYS; constitutive function). Compounds which decrease PA secretion without affecting LYS secretion have potential as "down-regulators" of macrophage function and, hence, of the immune system. Glucocorticoids (e.g., dexamethasone, IC50 less than 0.01 microM) and auranofin (IC50 = 1 microM) are positive in this model. In contrast, cyclooxygenase inhibitors (indomethacin, ibuprofen and piroxicam, all at 1 microM) boost PA secretion; lipoxygenase inhibitors (REV-5901, NDGA and piriprost, all at 10 microM) have little or no effect. Dexamethasone, but not auranofin, induces a urokinase-inhibitory activity which elutes between 0.13 and 0.19 M NaCl upon anion exchange HPLC (TSK-DEAE-5-PW). Fibrin overlay following SDS-PAGE of the HPLC peak reveals a urokinase-inhibitory band at approximately 90 Kd.
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PMID:Pharmacological modulation of plasminogen activator secretion by P388D1 cell line. 312 May 14

The excretory duct of the lacrimal gland of rabbits and guinea pigs was cannulated in situ for collection of pure lacrimal gland fluid, not contaminated by secretions from the Harderian gland or contributions of desquamating cells of the conjunctival and corneal epithelium. Tears as well as lacrimal gland fluid of both species showed a species-specific and molecular weight-dependent pattern after sodium dodecylsulphate-polyacrylamide (SDS-PAA) gradient slab gel electrophoresis. The most striking difference in both species was a protein corresponding to serum albumin present in tears and almost lacking in lacrimal gland fluid. Likewise, a variety of enzymes, total protein and PGE2 were measured in tears and lacrimal gland fluid. For rabbit tears the lacrimal gland is the primary tissue source of lysozyme (LZM), beta-hexosaminidase (beta-hex), angiotensin-converting enzyme (ACE), plasminogen activator (PA) and total protein, while lactate dehydrogenase (LDH) and the greater part of prostaglandin E2 (PGE2) are present in rabbit tears mainly as products from other ocular tissue sources. In guinea pig tears peroxidase (POD), ACE, PA and less PGE2 are exceted by the lacrimal gland, amylase (AMY), LDH and a substantial amount of PGE2 are added to the guinea pig tears by other ocular tissue sources. Beta-hex and total protein are released from the lacrimal gland and from other ocular tissue sources as well.
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PMID:Comparison of tears and lacrimal gland fluid in the rabbit and guinea pig. 386 12

The secretory proteins of the mucosa of the cervix, uterus, and fallopian tubes were investigated by measuring the proteins that were released by isolated mucosal areas. Initial screening disclosed that the immunoglobulins IgG and IgA were released in measurable quantities, but that IgM and the secretory (T) piece of IgA were either absent or present only in trace amounts. Relatively low levels of diffusable total complement activity and the C3 component of complement were present, whereas the C1q, C1r, and C4 components were either absent or present only in trace quantities. No neutral proteinase activity was present, but lysozyme, plasminogen activator, alpha 1-antitrypsin, and alpha 1x-antichymotrypsin could be found in reasonable amounts. The site of secretion, concentration, and cyclic variation of the proteins that diffused from the mucosal sites in measurable quantities were studied. The types and amounts of protein secreted by a particular site in the cervix, uterus, or fallopian tube varied from those of protein from other sites, even within the same organ. During the menstrual cycle, variations occurred in the amount of protein secreted by each mucosal site. However, whether an increase or a decrease in the release of a particular protein took place varied with each protein, even at the same site. The mucosal sites also differed from each other in their response to the phase of the menstrual cycle, that is, whether more or less protein was released, even sites within the same organ. The conclusion is that each organ and even different sites within an organ can respond independently from each other to changes in hormone levels, producing different types and amounts of secretory proteins. The amount of diffusable protein produced by an individual site during the menstrual cycle depends on the type of protein as well as the mucosal site.
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PMID:Diffusable proteins of the mucosa of the human cervix, uterus, and fallopian tubes: distribution and variations during the menstrual cycle. 392 Sep 15

The injection of thioglycollate medium into the peritoneal cavity of the mouse induces high levels of macrophage fibrinolytic activity due to the production and secretion of a plasminogen activator, a trypsinlike serine protease, which is absent in unstimulated macrophages. Intraperitoneal injection of endotoxin or mineral oil can stimulate only a fraction (<10%) of the fibrinolytic activity of thioglycollate cells, similar to the partial stimulation (<10%) seen 1-2 days after phagocytosis of latex or SRBC by unstimulated macrophages. The endotoxin-stimulated macrophages contain and release relatively low levels of plasminogen activator, but these primed cells can be triggered to produce and secrete high levels of enzyme, by phagocytosis of latex. Under conditions where the plasminogen activator is induced and secreted, there are no effects on the production and/or release of lysozyme or intracellular acid hydrolases, Discovery of a two-stage procedure for inducing macrophage plasminogen activator made it possible to study the role of cell priming and phagocytosis separately. Endotoxin was a more effective priming agent, weight for weight, than lipid A:BSA complex. Secretion of the plasminogen activator was induced only by thioglycollate, or endotoxin and latex. In situ fibrinolysis was induced by these agents and mineral oil, BCG, and fetal calf serum, in decreasing order of effectiveness. Phagocytosis of latex in all cases except thioglycollate stimulation, increased fibrinolytic activity from three- to sixfold. Latex and a variety of other particles such as M. lysodeikticus, aggregated gamma-globulin and immune complexes showed dose-dependent stimulation of fibrinolysis by endotoxin-primed macrophages. Although the initial phagocytic trigger was not specific for the substance employed, the ability to induce a sustained response depended on the persistence of the phagocytized particle within the cell. Fibrinolysis and secretion of plasminogen activator continued at high levels for at least 9 days after uptake of latex, a nondigestible particle, whereas plasminogen activator was secreted only transiently after ingestion of rapidly digested M. lysodeikticus. The induction of plasminogen activator secretion provides a mechanism by which the activated macrophage can exert a selective effect on its extracellular environment.
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PMID:Induction of macrophage plasminogen activator by endotoxin stimulation and phagocytosis: evidence for a two-stage process. 442 92

Hydrolytic enzymes are major constituents of alveolar macrophages, which in recent years have been shown to be involved in many aspects of the inflammatory response in addition to their better-known role in bactericidal processes. This review summarizes the general properties, physiologic function, cellular physiology, and clinical associations of four important hydrolytic enzymes of alveolar macrophages--lysozyme, elastase, plasminogen activator, and collagenase--with particular attention to the relationship of these enzymes to the pathophysiology of lung disease. The information reviewed shows that much is known about the biochemistry of these enzymes, that each is produced in greater quantity when alveolar macrophages are stimulated, that each has a distinctive physiologic role in the inflammatory process, and that they function as part of the overall pulmonary antibacterial defense system. Studies of the pathophysiologic effects consequent to the elaboration of excess quantities of these enzymes by stimulated macrophages show that some hydrolytic enzymes injure the lung by attacking normal as well as inflammatory tissue sites that are susceptible to degradation. Such damage is normally limited by enzymatic inhibitors, like alpha-antitrypsin, but the inactivating capacity of the inhibitors can be overwhelmed and in these instances excess enzyme contributes to the development of emphysema. This newer understanding of the pathophysiologic role of hydrolytic enzymes may lead to therapeutically beneficial methods for modulating the pulmonary inflammatory response.
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PMID:Hydrolytic enzymes of alveolar macrophages. 631 90

We report here the ability of a murine macrophage-like cell line, J774.2, to present antigen to primed T cells in a genetically restricted manner. J774.2 is a subclone derived from the reticulum cell sarcoma cell line, J774. Like mature macrophages, J774.2 possesses Fc receptors for all immunoglobulin G (IgG) subclasses; it is capable of performing Fc-mediated phagocytosis, and it secretes both lysozyme and plasminogen activator.
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PMID:The J744.2 cell line presents antigen in an I region restricted manner. 634 73

Elicited peritoneal macrophages from Sprague-Dawley rats conventionally bred and housed failed, as we have reported, to produce detectable elastolytic activity in culture. They did produce lysozyme and plasminogen activator. We now show that in contrast to these cells, macrophages from pathogen-free, barrier-sustained rats produced readily demonstrable elastolytic activity. Rats raised pathogen-free and subsequently housed conventionally for 2-4 wk appeared to lose the capacity to afford macrophages producing elastase. At the same time they acquired infections with several rat pathogens including Spironucleus muris, Kilham rat virus, sialodacryoadinitis virus, and mycoplasma pulmonis. The acquisition by the rats of one or more of these infections, conditions conducive to infection, or both factors may have suppressed their capacity to yield elastolytic activity.
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PMID:Peritoneal macrophages of pathogen-free rats but not of conventional rats secrete elastolytic activity. 658 37

Human tear fluid has plasminogen activator activity. The type of plasminogen activator activity in unstimulated and stimulated tears was determined, using antibodies that specifically neutralize tissue plasminogen activator or urokinase. All plasminogen activator activity was tissue plasminogen activator-related in both types of tears. Correlations between activities of beta-hexosaminidase, lysozyme and lactate dehydrogenase with tissue plasminogen activator activity indicate that the contribution to plasminogen activator activity of conjunctival and corneal epithelium is more important in unstimulated tears than stimulated tears. In stimulated tears the tissue plasminogen activator activity originates mainly from the lacrimal gland. It is suggested that a constant concentration of plasminogen activator is released from the lacrimal gland and that this concentration is independent of the secretion rate of tear fluid and that the release from the conjunctiva is due to desquamation of cells.
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PMID:Immunological characterization and possible origin of plasminogen activator in human tear fluid. 668 45

Chrysotile fibers injected into the peritoneal cavity of mice elicit a cellular exudate. Macrophages appearing in this exudate produce high levels of the neutral protease, plasminogen activator, when compared with the resident peritoneal macrophage population. In contrast, the levels of lysozyme and two lysosomal enzymes are the same for the two macrophage types. The asbestos-induced macrophages producing the plasminogen activator appear to have descended from recently divided precursors. Low concentrations of anti-inflammatory glucocorticoids inhibit macrophage plasminogen activator synthesis. Preliminary experiments indicate that different asbestos types induce hyperemia in skin, and also shorten the partial thromboplastin time of plasma and generate the release of kinins. These observations could be interrelated and are suggested as representing some aspects of the inflammatory response of the host to asbestos exposure.
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PMID:Macrophage stimulation and the inflammatory response to asbestos. 677 Nov 31


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