Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The extracts of granules of human polymorphonuclear leukocytes hydrolyzed a variety of proteins including human and bovine hemoglobin, human fibrinogen, human and bovine serum albumin, bovine elastin, and casein. The hydrolysis of all the proteins except fibrinogen and elastin was increased by addition of urea. Various inhibitors of trypsin, kallikrein, plasmin, Clr, Cls, and other proteolytic enzymes had no inhibitory effect. Slight inhibition was observed with polyanethol sulfonate and strong inhibition with normal human serum. Serum of patients with hereditary angioneurotic edema having no functional C1-esterase inhibitor was as effective in inhibiting the proteolysis as normal serum. The inhibitor was localized in 4S fractions of normal serum fractionated on Sephadex G-200. Fractionation of normal serum by ammonium sulfate precipitation, Sephadex G-200 filtration, and CM-Sephadex chromatography did not result in appearance of inhibitory activity in more than one protein peak, suggesting the possibility that only one inhibitor might be responsible. Since all fractions which contained the inhibitor of proteolysis also contained alpha1-antitrypsin, since sera of patients having low alpha1-antitrypsin levels contained less inhibitory activity, and since antibodies against alpha1-antitrypsin reversed the inhibition obtained from normal serum, the inhibition of proteolysis may be attributed to alpha1-antitrypsin.
J Invest Dermatol 1976 Feb
PMID:Some properties of proteolysis by polymorphonuclear leukocyte-granule extracts. 0 49

Two acid proteases, one hydrolysing hemoglobin and the other hydrolysing benzoyl arginine naphthyamide (BANA), were separated and partially purified from human skin buffer extract. The acid protease hydrolysing hemoglobin was purified about 190 fold by Sephadex G-100 gel filtration and DEAE-cellulose chromatography. It hydrolysed hemoglobin at pH 3.5, casein at pH 5.8 and skin protein substrate at pH 6.0. It did not markedly hydrolyse synthetic protease substrates. The molecular size of this protease was 38000. The protease was insensitive to common protease modifiers and closely resembles cathepsin D purified from other organs. The BANA-hydrolysing acid protease was purified about 760 fold by Sephadex G-100 gel filtration and affinity chromatography on organomercurial Sepharose 4B gel. It preferentially hydrolysed BAEE, BANA and BAA with an optimum at pH 5.8. The hydrolysis of BAPA, LeuNA and protein substrates was very low. This acid protease was found to be highly dependent on reducing agents, as DTT, and chelating agents, as EDTA, and was inhibited by pCMB and TLCK. The molecular size of the enzyme was 28000. This protease closely resembles cathepsin B1 purified from other organs. Human skin was also shown to contain a low activity of benzoyl arginine amide (BAA) hydrolysing acid protease with a molecular size of about 50000 and resembling cathepsin B2. Human skin contained an inhibitor with a molecular size of about 13000 against human skin cathepsin B1. This inhibitor did not inhibit trypsin, chymotrypsin or skin proteases other than cathepsin B1.
Arch Dermatol Res 1976 Jun 21
PMID:Human skin proteases. Separation and characterization of two acid proteases resembling cathepsin B1 and cathepsin D and of an inhibitor of cathepsin B1. 0 17

Psoriatic scale proteases were found to be extracted effectively in salt solution (1 mol/l) containing Triton X-100 (5 g/l). The extraction in dilute buffer or sucrose yielded low activities. The acid (0.25 N H2SO4) and KSCN (2 mol/l) solutions effectively extracted plasminogen activator. Fibrinolysin was most active in salt (1 mol/l KCl) and in KSCN (2 mol/l) extracts. Psoriatic scale proteases were fractionated by Sephadex G-100 gel filtration and further by DEAE cellulose chromatography. Five different enzyme preparations were obtained. The first preparation, resembling cathepsin D, effectively hydrolysed hemoglobin at pH 3.5 and casein at pH 5.8 and was insensitive to protease modifiers. The second preparation effectively hydrolysed trypsin substrates (AGLME, TAME, BAEE and BANA) and also histone and casein at pH 7.2 and was inhibited by protease inhibitors, TLCK and E-600. The third preparation hydrolysed histone and casein at pH 10.2 and was effectively inhibited by E-600 and partially by protease inhibitors and TPCK. The fourth preparation, resembling cathepsin B1, hydrolysed BANA and BAEE at pH 5.8 and was activated by SH-reagents and EDTA. The fifth enzyme preparation hydrolysed ATEE and was inhibited by E-600 and TPCK. Plasminogen activator was found mainly in the second enzyme preparation and fibrinolysin activity in the third and fifth enzyme preparations. The second, third and fifth enzyme preparations were different from the enzymes found in healthy human skin. The proteases of psoriatic scale resemble those of tissue and cell cultures undergoing rapid cell division. The possible role of proteases in the increased cell division in psoriasis plaque is discussed.
Arch Dermatol Res 1976 Aug 27
PMID:Human skin proteases. Fractionation of psoriasis scale proteases and separation of a plasminogen activator and a histone hydrolysing protease. 0 31

A method for preparing isolated epidermal cells using trypsin is described. The isolated cells retain the ability to bind antibody from patients with pemphigus or with pemphigoid in a disease-specific.
Br J Dermatol 1975 Oct
PMID:The differential binding of antibody from the sera of patients with pemphigus and pemphigoid to isolated guinea-pig epidermal cells. 5 62

The hypothesis that deficiencies of plasma protease inhibitors might play a role in the pathogenesis of chronic urticaria was evaluated. Plasma levels were measured in patients with urticaria and a matched control group for alpha1-antitrypsin, alpha2-macroglobulin, total trypsin-inhibiting capacity, kallikrein-inhibiting capacity, and the complement factors C1 esterase inhibitor, C3, and C4. A total of 92 patients with chronic urticaria or more than three months' duration was studied. Patients with acquired cold urticaria had significantly decreased levels of alpha1-antitrypsin and total antitrypsin activity. In patients with acquired angioneurotic edema, alpha1-antitrypsin levels and antichymotrypsin activities were lowered, with less significant decreases in anti-trypsin and antikallikrein activities. Levels of C1 esterase inhibitor , C3, and C4 were normal in all groups. There was no correlation between the increased sensitivity to intracutaneously administered kallikrein injection and deficiencies of of protease inhibitors.
Arch Dermatol 1975 Aug
PMID:Protease inhibitors in plasma of patients with chronic urticaria. 6 Sep 15

Anti-epidermal cell sera (AES) were obtained by immunizing rabbits with enzymatically dispersed, viable guinea-pig epidermal cells followed by absorption with guinea-pig red blood cells, spleen and thymus cells, and liver powders. Complement-mediated cytotoxicity and immunofluorescence demonstrated that AES were towards cell surface antigen specific for stratified squamous epithelia of guinea pigs, and cross reacted with the corresponding tissues of humans and monkeys. Immunofluorescence revealed that AES reacted with Hassall's corpuscles and surrounding epithelial cells of the guinea-pig thympus which seemed to share common antigens with the epidermis; AES gave no reaction with other organs. While antigens reactive with pemphigus antibodies (PA) were demonstrated by membrane immunofluorescence to be present on the epidermal cell surface, PA showed no cytotoxicity to guinea-pig and human epidermal cells. Re-treatment of isolated epidermal cells with trypsin showed that antigens ractive with PA were more susceptible to the enzyme than those reactive with AES. These findings suggest that the cell surface antigens binding AES are different from the antigens which bind PA.
J Invest Dermatol 1977 May
PMID:Experimental production of rabbit anti-guinea-pig epidermal cell sera. Comparison to pemphigus antibodies. 6 55

Contact sensitivity to dinitrochlorobenzene (DNCB) in guinea pigs could be rapidly suppressed by intravenous injection of dinitrobenzene sulfonic acid sodium salt (DNBSO3). This suppression is transient and antigen-specific. Macrophages from desensitized animals are not inactivated as shown by their ability to react, both in vivo and in vitro to lymphokines produced in a separate system. Therefore, effector lymphocytes are considered the target for the desensitizing antigen. Using an adoptive transfer system it was demonstrated that effector lymphocytes are inactivated by a direct effect of the hapten. Since this inactivation can be reversed by trypsin treatment, a receptor blockade of effector lymphocytes is proposed as the mechanism of desensitization of DNCB-contact sensitive guinea pigs. This does not exclude the possibility that additional mechanisms such as suppressor cells, compartmentalization or endogenous proliferation of lymph node lymphocytes may play an additional role.
J Invest Dermatol 1978 Feb
PMID:Mechanism of densensitization in DNCB-contact sensitive guinea pigs. 7 98

Modifications in the distribution of the binding sites for concanavalin A (Con A) were studied on trypsin isolated living guinea pig keratinocytes. Fluorescein-labelled Con A was used and the in vitro procedure has included short-term cultures, experiments at 37 degrees C and 4 degrees C, the study of colchicine and vincaleucoblastine effects. It was possible to induce different patterns of staining corresponding to distinct redistribution of Con A binding sites; the distinct redistribution was correlated to the effects of Con A, colchicine and vincaleucoblastine. These findings demonstrated that the system used was appropriate to the study of some dynamic events on the keratinocytes membranes.
Arch Dermatol Res 1979 May 29
PMID:Dynamic redistribution of concanavalin A binding sites on isolated guinea pig keratinocytes. 8 36

To obtain pure culture of epidermal cells from small human biopsies, two different techniques were tested and compared, i.e. separation of epidermis from corium before cultivation by trypsin and suction, and after cultivation by trypsin and collagenase. The most active growth of epidermal cells was obtained by the third technique, since short-term trypsin treatment released only fibroblasts from the culture. Crude collagenase (type I) was less effective than trypsin. Collagenase type II, III and IV had no effect on fibroblast release. Neither trypsin nor collagenases dispersed epidermal cells.
Arch Dermatol Forsch 1975
PMID:Separation of human epidermal cells from fibroblasts in primary skin culture. 16 87

Guinea-pig melanocytes in mixed epidermal cell cultures bind melanocyte-stimulating hormone in a distinct focal surface area in their perinuclear field and thus follow the same pattern previously described for Cloudman melanoma cells. The labeling index ranged from 18 to 34%. Pretreatment of cultures with trypsin leads to destruction of melanocyte-stimulating hormone receptors whereas neuraminidase has no such effect.
J Invest Dermatol 1976 Oct
PMID:Melanocyte-stimulating hormone receptors on cultured guinea-pig melanocytes. 18 12


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