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)

A reproducible method for isolation of mouse nasal lymphocytes was developed. The cells were released from tissue fragments of dissected mouse nose by enzyme extraction with collagenase and separated by a stepwise Percoll gradient centrifugation. The partially purified nasal lymphocyte fraction from normal BALB/c mice contained CD4+ T cells (18-23%), CD8+ T cells (7-10%) and B cells (20-38%), when analysed with a FACScan fluorescence analyser. The ratio of T to B cells and that of CD4+ to CD8+ T cells in the nasal cell fraction were about twice as high as those in Peyer's path lymphocytes. The nasal lymphocyte fraction from the mice infected with influenza virus was then characterized. The nasal lymphocytes contained a twice larger number of CD4+ and a three times larger number of CD8+ T cells than those of normal mice 7 days after infection. They produced IFN-gamma which increased after infection. They contained the cells secreting influenza virus-specific IgA and IgG antibodies 4 weeks after infection. Moreover, the nasal lymphocytes from infected C3H mice lysed the virus infected-target cells. These results suggest that this method can successfully be used for investigating cellular dynamics of mucosal immunity in the upper respiratory tract of experimental animals.
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PMID:Characterization of mouse nasal lymphocytes isolated by enzymatic extraction with collagenase. 749 Apr 57

Neutrophils contain on their surface a receptor for the Fc portion of IgA. Cross-linking of this receptor in the fluid phase induces superoxide production and release of granule constituents, but the response to surface associated IgA has not been previously studied. Neutrophils incubated with surface-associated IgA (SAIgA) release significant amounts of activated collagenase in addition to the granule proteins myeloperoxidase and lactoferrin. This activation is associated with release of superoxide as well as hydrogen peroxide and hypochlorous acid. Although neutrophils incubated with soluble aggregates of IgA also release granule proteins and produce superoxide, soluble aggregates of IgA do not trigger the release of activated collagenase and do not generate hydrogen peroxide or hypochlorous acid. In summary, neutrophils activated by surface associated IgA respond differently than when cells are activated by soluble aggregates of IgA. These differences may be important in understanding the mechanisms of tissue injury in patients with inflammatory disorders.
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PMID:Activation of human neutrophils by surface-associated IgA is associated with the release of activated collagenase. 755 45

Circulating IgG from a large subset of bullous pemphigoid (BP) patients reacted on immunoblot with a 120-kDa protein in conditioned keratinocyte culture medium and in keratinocyte cell extracts. A protein with a similar molecular weight was recognized by circulating IgA from a subset of patients with linear IgA dermatosis (LAD). Both affinity-purified 120-kDa-specific BP IgG and 120-kDa-specific LAD IgA bound to the roof of salt-split skin. Both proteins recognized are collagenous glycoproteins. Deglycosylation with N-glycosidase F resulted in an identical reduction in molecular weight for both the BP-IgG-recognized protein and the LAD-IgA-recognized protein. Both proteins were equally susceptible to digestion with type VII collagenase. Furthermore, both proteins were absent from conditioned culture medium of keratinocytes from patients with BP180-deficient general atrophic benign epidermolysis bullosa (GABEB). Immunodepletion studies showed that the 120-kDa LAD antigen could be removed from conditioned culture medium by anti-120-kDa BP IgG. Thus these results indicate that these proteins are either highly related or, most probably, identical. A strong antigenic relationship between the 120-kDa protein and the 180-kDa bullous pemphigoid antigen (BP180) was detected by cross-reaction of affinity-purified anti-120-kDa BP patient antibodies to BP180 and cross-reaction of monoclonal anti-180-kDa antibodies to the 120-kDa protein. Notwithstanding this cross-reactivity, the 120-kDa protein also exhibits unique epitopes demonstrated by the nonreactivity of individual anti-120-kDa BP and LAD patient serum with the 180-kDa antigen.
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PMID:Bullous pemphigoid and linear IgA dermatosis sera recognize a similar 120-kDa keratinocyte collagenous glycoprotein with antigenic cross-reactivity to BP180. 907 69

Glomerular IgA deposits were eluted from biopsied kidney tissues of patients with IgA nephritis and the antibody specificity was analyzed. The IgA was successfully eluted with combined use of citrate buffer and collagenase. The elution procedure did not attenuate antibody activity which was confirmed by the preliminary experiment that mouse IgA monoclonal anti-DNP antibody similarly treated did not cause any decline of antigen-binding ability. Because of the limited amounts ranging from 80-800 ng/ml, the eluted IgA did not react with respective lysates of the kidney tissues from which the IgA had derived. Moreover, kidney tissues from 9 biopsies yielded 5 micrograms/ml of IgA, when mixed together as source of IgA; nevertheless, the eluted IgA did not react with the kidney lysates, either. The eluted IgA, however, did react with several bacterial antigens, among which the 34-kDa antigen from Haemophilus influenzae (34-kDa H. influenzae) was most clearly detected with IgA eluted from pooled 10 kidney samples of IgA nephritis, which was confirming by Western blot analysis. The reactivity of the eluted IgA with the 34-kDa H. influenzae antigen was seen in 3/5 of IgA nephritis and 3/9 of non IgA nephritis patients with glomerular IgA deposits, respectively. The reactivity of serum IgA with the bacterial antigen was also investigated, which revealed that the serum IgA reacted with the 34-kDa antigen in 2/12 of IgA nephritis, 4/10 of liver cirrhosis patients and 3/10 of healthy control individuals, respectively. The surerum IgA from the IgA nephritis patients appeared to react with 34-kDa antigen more intensively than did healthy control IgAs. These results suggest that the 34-kDa H. influenzae plays an important role in the pathogenesis of at least certain IgA nephritis cases.
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PMID:[Isolation of glomerular IgA deposits from biopsied kidney tissues of patients with IgA nephritis and analysis of the antibody specificity of IgA]. 1042 65

Collagen XVII/BP180, an epidermal adhesion molecule, exists as a full-length transmembrane protein and as a soluble 120-kd ectodomain that is shed from the keratinocyte surface by furin-mediated proteolysis. Despite a number of studies on autoantibody targets in blistering skin diseases, it has remained unclear whether the physiologically shed ectodomain of collagen XVII plays a role as an autoantigen. Here we isolated the authentic, soluble form of human collagen XVII and showed that it is an autoantigen recognized by IgG and IgA autoantibodies in different blistering skin diseases and is, in some cases, the preferential target. The ectodomain was isolated from the epidermis, keratinocyte media, amniotic fluid, and pemphigoid blister fluid, and autoantibodies affinity-purified with this ectodomain bound to the proximal surface of the epidermis in normal skin but not in collagen XVII-deficient skin. The antibody reactivity was not dependent on the native conformation or the N-glycosylation of the soluble ectodomain, but was abolished by collagenase treatment. Sera of 81 patients with a clinically active blistering skin disease were reacted with full-length collagen XVII, the authentic soluble ectodomain, and recombinant fragments. In bullous and cicatricial pemphigoid, IgG reactive with full-length collagen XVII also recognized the soluble ectodomain. In linear IgA dermatosis and chronic bullous dermatosis of childhood, IgA targeted the soluble ectodomain more efficiently than the full-length protein. The use of recombinant fragments demonstrated that epitopes were present in several noncollagenous and collagenous subdomains of the molecule, and that a significant portion of the sera targeted Col15 domain, a hitherto unrecognized epitope region.
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PMID:The shed ectodomain of collagen XVII/BP180 is targeted by autoantibodies in different blistering skin diseases. 1066 97

When synovial effusion is the only symptom, it is often difficult to make an exact diagnosis of the arthritic disease. To distinguish various types of arthritis with synovial effusion, we measured the levels of matrix metalloproteinase-3 (MMP-3, Stromelysin), tissue inhibitor of metalloproteinase-1 (TIMP-1) and rheumatoid factor (RF) isotypes in synovial fluid (SF) from patients with rheumatoid arthritis (RA), osteoarthritis (OA), pyogenic arthritis (PA), pseudogouty arthritis (PG), gouty arthritis (GA) and traumatic arthritis (TA). SF was aspirated from the knee joint or the ankle joint. Levels of IgG-, IgM- and IgA-RF isotypes were measured by ELISA. Levels of MMP-3 and TIMP-1 in SF were simultaneously determined by a one-step EIA system. Levels of IgG-RF, IgM-RF and MMP-3 in SF from RA patients were significantly higher than those in OA, PA, PG, GA and TA. However, IgA-RF in SF from RA patients, when compared with PA and GA, did not show a significantly increased level. In addition, TIMP-1 in SF from RA, when compared with PA and TA, also has not shown a significantly increased level. Therefore, in addition to analysing clinical data, measurements of IgG-RF, IgM-RF and MMP-3 in SF may contribute in distinguishing RA from other arthritic diseases.
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PMID:Levels of rheumatoid factor isotypes, metalloproteinase-3 and tissue inhibitor of metalloproteinase-1 in synovial fluid from various arthritides. 1075 93

We have shown that two of the matrix metalloproteinases (MMPs), matrilysin and stromelysin-1, are capable of cleaving all of the human IgG subclasses. The cleavage occurs at a conserved site in the CH(2) domain of the heavy chain of IgG, releasing a single chain Fc-like fragment. We have not been able to demonstrate cleavage of IgA, IgD, IgM or IgE classes, which lack the cleavage site, nor could we show cleavage of IgG by collagenase, gelatinase, macrophage metalloelastase or membrane-type (MT)-MMP. This cleavage of IgG, by separating the antigen-binding (Fabprime prime or minute)(2) from the Fc portion, will remove much of the immunoglobulins' functionality, e.g. complement fixation, Fc receptor binding. In the context of a tumour producing matrilysin or stromelysin, this may represent a way in which the tumour protects itself from ADCC. In inflamed or damaged tissues where plasma protein leakage occurs, degradation by MMPs may be a mechanism for clearance of IgG.
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PMID:Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin. 1184 44

Glomerular IgA deposits were eluted from renal biopsy specimens exhibiting IgA nephropathy (IgAN) by using a combination of citrate buffer and collagenase. Collagenase predigestion of the kidney tissues resulted in increased amounts of IgA eluted by citrate buffer, and the elusion procedure did not attenuate the antigen-binding ability of IgA antibody. When reactivity of the eluted IgA with bacteria components was examined by Western blotting, the most notable reaction was observed for Haemophilus influenzae lysates in the form of a 34 kD-band. The reactivity of IgA eluted from the kidney tissues against the H. influenzae 34 kD antigen was evident in 3 of 5 IgAN cases. However, similar reactivity was also evident in 2 of 6 non-IgAN hepatic diseases exhibiting a glomerular IgA deposition. These findings suggest that antibody specificity of IgA against H. influenzae itself may not be directly associated with glomerular injury, although anti-H. influenzae 34 kD IgA was deposited in the kidney, at least in part, by IgAN. Further investigations into the properties of IgA deposited in the glomerulus are needed. Our improved method for IgA elution from kidney tissues would be useful for analysing the pathogenesis of IgAN.
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PMID:Elution of IgA from kidney tissues exhibiting glomerular IgA deposition and analysis of antibody specificity. 1247 35

Phenytoin (diphenylhydantoin or Dilantin) is a highly effective and widely prescribed anticonvulsant agent used in the treatment of grand mal and psychomotor epilepsy. In dermatology, phenytoin has been used to treat ulcers, epidermolysis bullosa, and inflammatory conditions. Its mechanism appears to involve its ability to inhibit collagenase. Its topical use for the promotion of wound healing seems promising but requires further trials. The side effects of phenytoin continue to create significant morbidity. Common side effects include gingival hyperplasia, coarsening of the facies, and hirsutism. Rarer cutaneous side effects include drug-induced lupus, purple-hand syndrome, pigmentary alterations, and IgA bullous dermatosis. It can cause generalized cutaneous eruptions that include a maculopapular exanthem, Stevens-Johnson syndrome, generalized exfoliative dermatitis, toxic epidermal necrolysis, vasculitis, and fixed-drug eruptions. Phenytoin is linked to a hypersensitivity syndrome manifested by fever, rash, and lymphadenopathy. Patients receiving phenytoin may develop pseudolymphoma or, rarely, malignant lymphoma and mycosis-fungoides-like lesions. Phenytoin can effect clotting function. Phenytoin can alter vitamin and mineral levels. Prenatal exposure to phenytoin may result in a spectrum of structural, developmental, and behavioral changes known as the fetal hydantoin syndrome. After 60 years of use, phenytoin uses and mechanisms of action have yet to be fully defined; the drug remains a useful tool and an important subject for additional research.
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PMID:Phenytoin in cutaneous medicine: its uses, mechanisms and side effects. 1295 53

Goodpasture's disease is characterized by crescentic glomerulonephritis and lung hemorrhage in the presence of anti-glomerular basement membrane (anti-GBM) antibodies. This disease usually is mediated by IgG autoantibodies directed against the noncollagenous domain of the alpha3(IV) collagen chain, the Goodpasture autoantigen. In rare cases, anti-GBM antibodies of IgA or IgM class are involved, but their specificity has not been determined, and their target antigen remains unknown. The authors present the case of a 62-year-old man with anti-GBM disease mediated by a monoclonal IgA-kappa antibody, which progressed to end-stage renal disease despite intensive immunosuppression. The patient underwent living-related kidney transplantation, but lung hemorrhage and crescentic glomerulonephritis recurred, causing the loss of the allograft 2 years later. Indirect immunofluorescence found the presence of circulating IgA antibodies reactive with a basement membrane component, identified by enzyme-linked immunoabsorbent assay and Western blot as the alpha1/alpha2(IV) collagen chains. Sensitivity to digestion with collagenase indicated that IgA bound to epitopes located in the collagenous domain. This is the first case of recurrent Goodpasture's disease secondary to an autoreactive IgA antibody. The specificity of an IgA antibody implicated in the pathogenesis of anti-GBM disease has been investigated for the first time, identifying the alpha1/alpha2(IV) collagen chains as a novel target for nephritogenic antibodies.
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PMID:Recurrent Goodpasture's disease secondary to a monoclonal IgA1-kappa antibody autoreactive with the alpha1/alpha2 chains of type IV collagen. 1568 19


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