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)

Involved psoriatic epidermis maintains its histologic appearance, increased labeling index, and increased level of plasminogen activator after grafting onto athymic nude mice. Epidermis from clinically uninvolved psoriatic skin develops an increase in plasminogen activator activity after grafting for 6 weeks on nude mice and demonstrates an increased labeling index. Normal control skin maintains its low level of plasminogen activator and labeling index after grafting. These results indicate that psoriatic skin can maintain and develop markers of psoriatic skin independent of the host.
J Invest Dermatol 1983 Jun
PMID:Transplantation of psoriatic skin onto nude mice. 634 18

Human epidermal cells were cultured with pemphigus antibody in the presence of hydrocortisone, methylprednisolone sodium succinate, dapsone and gold. Hydrocortisone and methylprednisolone reduced the production of the enzyme plasminogen activator but dapsone and gold had no effect. These results support the hypothesis that corticosteroids have dual effects on pemphigus through inhibition of plasminogen activator production by epidermal cells and suppression of pemphigus antibody production by B lymphocytes.
Br J Dermatol 1984 Mar
PMID:The effect of corticosteroids, dapsone and gold upon plasminogen activator synthesis and secretion by human epidermal cells cultured with pemphigus antibody. 642 6

The incubation of cultured epidermal cells with IgG obtained from a 56-year-old man with penicillamine-induced pemphigus resulted in an increase in extracellular and intracellular plasminogen activator. This suggests that penicillamine-induced pemphigus and spontaneously occurring pemphigus share common pathophysiologic processes in the induction of blister formation.
Arch Dermatol 1984 Jun
PMID:Penicillamine-induced pemphigus. Immunoglobulin from this patient induces plasminogen activator synthesis by human epidermal cells in culture: mechanism for acantholysis in pemphigus. 653 2

Primary cultures of human epidermal cells produce plasminogen activator (PA) as demonstrated by the ability of conditioned medium or cell lysates to hydrolyze fibrin in the presence of plasminogen, and to cleave [125I]plasminogen to characteristic fragments. The major molecular species of PA in human epidermal cells was inhibited by diisopropylfluorophosphate and comigrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with the high molecular weight band of human urokinase (Mr 55,000). Production of PA by human epidermal cells was inhibited by cycloheximide, stimulated by colchicine, and not affected by cytochalasin B or the tumor promoter 12-O-tetradecanoyl-phorbol-13-acetate. Both cholera toxin and epidermal growth factor stimulated PA activity in human epidermal cells, and PA activity was maximal at concentrations that best support in vitro growth of human epidermal cells. Examination of individual cells indicated that at least 15% of cells within a culture produced detectable amounts of PA.
J Invest Dermatol 1983 Nov
PMID:Plasminogen activator in cultured human epidermal cells. 660 91

The activity of the serine protease plasminogen activator (PA) was measured in cell lysates from primary mouse keratinocyte cultures as well as from a number of established mouse keratinocyte lines. Enzyme activity was generally higher in the transformed lines than in the primary cultures; however, among the lines tested, those that expressed the highest degree of morphologic differentiation had the highest levels of cell-associated PA. In both the normal (primary) and transformed (established) keratinocyte cultures, PA activity increased when cultures reached confluence and morphologic evidence of differentiation was noted. The highest specific activity of the enzyme was found in cells shed from differentiating cultures, which consisted predominantly of detergent-resistant cornified envelopes. As the cultures differentiated and these cells were shed from the culture surface, the total cell-associated PA activity of the culture decreased accordingly. In both the normal and transformed keratinocyte cultures, peak PA activity occurred at a time when DNA synthesis was declining. These findings indicate that as keratinocytes differentiate, their intracellular levels of PA increase. The modulation of this endogenous keratinocyte enzyme may play an important, although as yet undefined, role in the normal maturation and terminal differentiation of these cells.
J Invest Dermatol 1983 Apr
PMID:Plasminogen activator in differentiating mouse keratinocytes. 668 29

The molecular sizes of secreted and cell-associated plasminogen activators from four cultured cell types were determined using an SDS-PAGE technique in which plasminogen and casein were included during polymerization of the polyacrylamide gel. The major bands of plasminogen activators secreted by human neonatal epidermal cells, human adult epidermal cells and transformed human squamous cells migrated the same distance as the high molecular weight band of authentic urokinase, indicating that the apparent molecular weight of these plasminogen activators was approximately 55,000 daltons. Plasminogen activator extracted from normal adult human epidermis also migrated with this major band of plasminogen activator, and a minor higher molecular weight band was also detected. In contrast, plasminogen activators secreted by transformed mouse squamous cells migrated between the high molecular weight band (approximately 55K) and the low molecular weight band of urokinase (approximately 32K), indicating that plasminogen activators of mouse epidermal cells differ from those of human epidermal cells. The mobility of the major bands of plasminogen activators detected in cell lysates of the four cell types was identical to that of secreted plasminogen activators.
Br J Dermatol 1983 Jul
PMID:Molecular size of secreted and cell-associated plasminogen activators from cultured epidermal cells. 668

A tissue plasminogen activator was extracted from skin lesions with allergic vasculitis and purified by successive column chromatography on Sephadex G-200, DEAE-cellulose, Hydroxyaptite-cellulose and polyacrylamide gel electrophoresis. By these procedures, 160 micrograms of enzyme with a specific activity of 843.8 international units/mg protein was obtained from 5 g of original skin. The purified material was homogeneous as ascertained by sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 110,000 as measured by gel filtration on Sephadex G-200. Its identity with human urokinase was investigated and was found to possess the same plasminogen activator activity as that of urokinase. It had high amindolytic activity, but only slight N-alpha-acetyl-glycyl-L-lysine methyl ester esterolytic activity. This tissue plasminogen activator was confirmed to be immunologically identical to human urokinase.
J Invest Dermatol 1982 Jan
PMID:Isolation of tissue plasminogen activator from skin lesions with allergic vasculitis. 719 68

The precise mechanism for acantholysis after pemphigus IgG binds to the cell surface is as yet unknown, although involvement of proteinases such as plasminogen activator (PA) has been suggested. We previously reported that pemphigus IgG, but not normal nor bullous pemphigoid IgGs, caused a transient increase in intracellular calcium ([Ca++]i) and inositol 1,4,5-trisphosphate (IP3) concentration in cultured DJM-1 cells (a squamous cell carcinoma line). To clarify whether phospholipase C is involved in this process after the antibody binds to the cell surface, we examined the effects of a specific phospholipase C inhibitor (U73122) on the pemphigus IgG-induced increase in [Ca++]i, IP3, PA secretion, and cell-cell detachment in DJM-1 cells. [Ca+2]i and IP3 contents were determined with or without 30-min pre-incubation with U73122 or an inactive analogue (U73343) with fura-2 acetoxymethylester and a specific IP3 binding protein, respectively. PA activity in the culture medium was measured after various incubation periods with pemphigus IgG by two-step amidolytic assay. The detachment of cell-cell contacts was examined by detecting the retraction of keratin filament bundle from cell-cell contact points to the perinuclear region by immunofluorescence microscopy using anti-keratin antibody. Pemphigus IgG immediately increased [Ca++]i and IP3 content. PA activity in the culture medium has also been increased at 24 h after pemphigus IgG was added in association with cell-cell detachment. However, pre-incubation with U73122 (1-10 microM), but not with U73343 (10 microM), dramatically reduced the pemphigus IgG-induced increases in [Ca++]i, IP3, and PA activity and inhibited the pemphigus IgG-induced cell-cell detachment. Both U73122 and U73343 caused no effects on cell viability and IgG binding to the cell surface. These results suggest that phospholipase C plays an important role in transmembrane signaling leading to cell-cell detachment exerted by pemphigus IgG binding to the cell surface.
J Invest Dermatol 1995 Sep
PMID:Pharmacologic evidence for involvement of phospholipase C in pemphigus IgG-induced inositol 1,4,5-trisphosphate generation, intracellular calcium increase, and plasminogen activator secretion in DJM-1 cells, a squamous cell carcinoma line. 766 7

Zymographic and immunological studies revealed that primarily tissue-type plasminogen activator and to a lesser extent urokinase-type plasminogen activator were present in fluids of pemphigus vulgaris (type Neumann) skin blisters. Furthermore, plasmin activity was detected in pemphigus blister fluids using chromogenic peptide substrate assays. In pemphigus, but not in control, suction blister fluids plasmin/alpha 2-antiplasmin and plasmin/alpha 2-macroglobulin complexes were found by immunoprecipitation or by testing in immunoassays after fractionation by molecular-sieve chromatography. Plasmin activity, detected by a low molecular weight chromogenic peptide assay, was ascribed to plasmin/alpha 2-macroglobulin complexes. Since formation of plasmin/inhibitor complexes requires active plasmin, the finding indicates previous activation of plasminogen in pemphigus lesions.
Arch Dermatol Res 1993
PMID:Plasminogen activation in lesional skin of Pemphigus vulgaris type Neumann. 768 51

Hepatocyte growth factor/scatter factor (HGF/SF) and keratinocyte growth factor (KGF, also designated FGF-7) are paracrine growth factors secreted by mesenchymal cells and active on a variety of epithelial cell types. In this study, the biologic responses of keratinocytes to these paracrine growth factors were compared. Stimulation of mitogenesis, migration, plasminogen activator (PA) activity, and fibronectin production were examined using human foreskin keratinocytes cultured in serum-free MCDB 153 medium. Although the two factors stimulated a similar level of proliferation when cells were maintained for 5 d in 1.8 mM Ca++, the peak effect of KGF, observed at 10 ng/ml, was approximately threefold higher than that of HGF/SF when cells were in medium containing 0.15 mM Ca++. Both agents promoted the migration of cells in low-calcium medium (0.08 mM Ca++). However, the magnitude of the response was approximately twofold greater for HGF/SF at 10 ng/ml than KGF at the same concentration. None of the matrix proteins such as type I collagen, type IV collagen, laminin, or fibronectin either stimulated or suppressed HGF/SF- or KGF-stimulated keratinocyte migration. Both factors stimulated PA activity of the cell extracts, especially urokinase-type, with similar potencies. Promoted PA activity was maximal with the addition of 10 ng/ml of either factor. Neither factor increased the production of fibronectin under conditions in which transforming growth factor-beta 1 was active. These results indicate that HGF/SF and KGF, both recognized as paracrine growth factors, elicit distinctive patterns of response by keratinocytes, implying that they have different roles in epidermal physiology.
J Invest Dermatol 1995 Jun
PMID:Comparative study of hepatocyte growth factor/scatter factor and keratinocyte growth factor effects on human keratinocytes. 776 66


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