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M Järvinen

Publications and source records attributed to M Järvinen.

At least 19 recordsLinked to original sources
PubMed1979

Localization of the rat epidermal SH-protease inhibitor in proventricular and vaginal squamous epithelium. An immunofluorescence study.

The rat epidermal SH-protease inhibitor was localized with the indirect immunofluorescence method in the rat proventricle and vagina fixed in cold phosphate-buffered formalin. Bright fluorescence was seen in the cytoplasms of the superficial layers of these squamous epithelia only when a highly specific antiinhibitor serum was used. The fluorescence diminished when normal rabbit serum or a rabbit antiserum againts bovine serum albumin was used instead of the anti-inhibitor serum. When the anti-inhibitor serum was neutralized with the purified epidermal inhibitor, the fluorescence was again markedly weakened. The results confirm our previous observations showing that the epidermal SH-protease inhibitor also occurs in other squamous epithelia, especially in the cytoplasms of the cells in their upper layers.

Animals↗
PubMed1979

Localization of the rat epidermal SH-protease inhibitor in the proventricular squamous epithelium using the peroxidase-antiperoxidase (PAP) method.

The rat epidermal SH-protease inhibitor was localized by the PAP method in the squamous epithelium of rat proventricle. Brown accumulation due to the peroxidase reaction was seen in the superficial and middle layers of squamous epithelia. The localization of the inhibitor in squamous epithelium is the same as we have demonstrated with immunofluorescence staining.

Animals↗
PubMed1979

The main neutral protease of rat skin is a mast cell enzyme. Immunohistochemical localization of the enzyme in rat skin with the peroxidase-antiperoxidase (PAP) complex method.

The highly sensitive PAP immunoperoxidase method was used to localize the main neutral protease of rat skin. The use of the neutral detergent, Triton X-100, in the reagent and washing solutions was observed to effectively decrease the nonspecific staining. The specific staining was localized to the mast cell granules.

Animals↗
PubMed1978

A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat.

The occurence of the human and rat epidermal SH-protease inhibitors in various human and rat tissues was studied by double radial immunodiffusion against specific antisera to the inhibitors. An immunoreactive protein was found in the extracts prepared from human and rat epidermis and from eosophageal and vaginal squamous epithelia, and from rat pro-ventricular squamous epithelium. No immunoreactive protein was found in man or rat in any other of their tissues, studied by us. The results strongly suggest that a protein reminiscent of the human or rat epidermal SH-protease inhibitor is present in squamous epithelia but not in other tissues. The identity of the epidermal inhibitor and the immunoreactive protein in the other squamous epithelia was confirmed by immunodiffusion, immunoelectrophoresis and gel chromatography, and by immunoinhibition of the papain inhibiting activity of the human epidermal and oesophageal inhibitors by gammaglobulins separated from antiserum to the human epidermal inhibitor.

Animals↗
PubMed1978

Localization of the human SH-protease inhibitor in the epidermis. Immunofluorescent studies.

Human epidermis contains a low molecular weight SH-protease inhibitor (Human Epidermal Inhibitor = HEI), whose epidermal localization was performed with the indirect immunofluorescence method. The fluorescence was most intensive in the cytoplasms of epidermal cells, often occurring perinuclearly. The fluorescent material in the frozen sections was often finely granular and occasionally extended outside the cytoplasm, while the fluorescence in fixed sections was more uniform, but weaker. Stratum basale generally stained poorly or not at all, as did also stratum lucidum. Stratum corneum stained fairly intensively throughout. In addition to fixation, the outcome of staining was also affected by the thickness of the epidermis, particularly stratum corneum. The significance of this inhibitor for the differentiation of epidermal cells and the keratinization of epidermis has therefore been discussed, and the authors assume it to be of considerable significance in these processes.

Cytoplasm↗
PubMed1978

Purification and some characteristics of the human epidermal SH-protease inhibitor.

An inhibitor of papain and other SH-proteases was purified 520-fold from human epidermis extracts by acetone fractionation, heat treatment, papain-Sepharose affinity chromatography, and Sephadex G-50 chromatography. The purified inhibitor had a molecular weight of 12,600 and contained no hexose, as tested by the anthrone reaction. The inhibitor survived in a boiling water bath, in 5% trichloroacetic acid, 20 mM Na3PO4 (pH 12.1) and 4 M NH4OH (pH 11.9). By isoelectric focusing 2 major activity peaks with pI's of 4.6 and 4.8, and a minor peak with a pI of 4.9 was fractioned, and 3 corresponding protein bands were seen after analytical isoelectric focusing. Immunization of rabbits with the purified inhibitor yielded a highly specific anti-inhibitor serum. The purified inhibitor inhibited papain, ficin, human cathepsins B and C, and slightly inhibited bromelain. No inhibition of serine proteases (bovine trypsin and chymotrypsin A, porcine elastase) or an acid protease (human cathepsin D) was observed. Evidence was obtained that the inhibitor formed a complex with both dithiothreitol-activated papain and enzymatically inactive mercuripapain.

Epidermis↗
PubMed1978

The low-molecular-weight SH-protease inhibitor in rat skin is epidermal.

The epidermis and dermis of rat skin were separated and the presence of the high-molecular-weight SH-protease inhibitor I1 and the low-molecular-weight inhibitor I2 in both was studied. Gel filtrations of the extracts revealed that 97% of the epidermal inhibitor activity was due to I2 and 89% of the dermal activity to I1. The presence of I2 mainly in the epidermis extract was confirmed by immunodiffusion of specific rabbit anti-I2 serum against purified I2, epidermis and dermis extracts, and rat serum. Most of the immunoreactive protein was seen in the epidermis extract, traces in the dermis extract and none in the rat serum. I2 was localized in rat skin by indirect immunofluorescence using rabbit anti-I2 serum and fluorescein isothiocyanate conjugate of goat anti-rabbit immunoglobulins. Intense fluorescence, much brighter than in the controls treated with rabbit non-immune serum, was seen in the epidermis, being most pronounced in the cytoplasms of cells in the granular layer. The weak fluorescence of the hair follicles, sebaceous glands, connective tissue cells and fibres was unspecific and was also seen in the controls. In view of its epidermal location, the name epidermal SH-protease inhibitor is suggested for I2.

Animals↗
PubMed1978

Effect of sport stress on lymphocyte transformation and antibody formation.

The effect of a heavy (marathon, 2.5 hr) and moderate (35 min of running) sport stress on the number and function of lymphocytes, and on the plasma cortisol and leucocyte levels was investigated. Marathon running had a profound effect on the lymphocytes. Though the total number of lymphocytes did not change, their responsiveness to PHA and Con A, especially to PPD, was clearly depressed. The suppression of lymphocyte transformation was transient, the recovery occurring in 24 hr. The marathon running had no effect on antibody-forming capacity when the antigen was given immediately after the performance of the marathon, i.e. at the time when the response of lymphocytes to PHA, Con A and PPD stimulation was impaired. A clear-cut granulocytosis and elevation of plasma cortisol was seen in all the marathon runners. The 35 min of running also resulted in granulocytosis and an increase of plasma cortisol, but it did not cause any impairment of the lymphocyte function.

Adult↗
PubMed1977

Immobilization effect on the tensile properties of striated muscle: an experimental study in the rat.

To investigate the effect of immobilization on the tensile properties of atrophied gastrocnemius muscle, the left hind legs of 40 rats were fixed with padded plaster casts for three weeks. Seven to 42 days after starting the immobilization, load-deformation curves were registered from both gastrocnemius muscles of each rat and several parameters assessed from the curves. The rupture always occurred at the muscle belly. The decrease in breaking strength and energy absorption capacity following immobilization for one week averaged 20% and 34%, respectively, and the values fell further to about 32% and 46% at the end of the immobilization (21 days), when compared to the contralateral control muscles of the same animals. The elastic stiffness of the immobilized muscles was markedly decreased but rose nearly to the level of the controls after removal of the casts. The tensile properties of the previously immobilized muscles had not yet reached the control levels three weeks after removal of the casts.

Animals↗
PubMed1976

Alpha-N-Benzoylarginine-2-naphthylamide hydrolase (cathepsin BI?) from rat skin. III. Substrate specificity, modifier characteristics, and transformation of the enzyme at acidic pH.

Some properties of rat skin benzoylarginine-2-naphthylamide hydrolase types I (preparations I and AI) and II (preparations II and NII) were studied. Both types were activated by dithiothreitol and EDTA, but responded differently to 1 mM KCN, when benzoylarginine-2-naphthylamide (BANA) was used as a substrate: type I was inhibited, while type II was activated. When leucine-2-naphthylamide was used as a substrate, both types were activated by KCN. Thiol proteinase inhibiting substances, like heavy metals, iodoacetic acid, 4-chloromercuribenzoic acid, and tosyllysine chloromethylketone, inhibited the enzymes. Diisopropylfluorophosphate, phenylmethylsulfonyfluoride, 4-aminobenzamidine, and high-molecular-weight trypsin inhibitors were without effect. The substrate specificity of rat skin BANA hydrolase resembled that of an amino acid naphthylamidase, naphthylamides of methionine, lysine, arginine, and alanine being hydrolyzed most rapidly. The rate of hydrolysis of BANA was only 11% of that of methionine naphthylamide. Amino acid esters with a free alpha-amino group were also good substrates. The transformation of type II to type I at acidic pH was studied. During the transformation amino acids or peptides were formed and probably some inhibitor present in type II was destroyed proteolytically.

Animals↗
PubMed1976

Purification and properties of two protease inhibitors from rat skin inhibiting papain and other SH-proteases.

Two papain inhibitors, I1 and I2, from rat skin extract were purified by affinity chromatography on KSCN-modified papain-agarose gel and by gel filtration on Sephadex G-100. I1 had a molecular weight of 74 000, a pI of 4.6, and it contained 4% of carbohydrates. I1 inhibited papain, ficin, bromelain, rat skin benzoylarginine-2-naphthylamide hydrolase, and to a minor extent, rat skin cathepsin C and bovine trypsin. Bovine chymotrypsin or rat skin cathepsin D were not inhibited and benzoylarginine-2-naphthylamide hydrolase was inhibited only at alkaline pH. An inhibitor corresponding to I1 was present in various rat tissues and also in serum. A similar inhibitor was present in the skin of cat, rabbit, guinea pig, and man. I2 had a molecular weight of 13 400, a pI of 4.9 and it contained no carbohydrates. I2 inhibited all thiol proteases tested, but not trypsin, chymotrypsin, or rat skin cathepsin D. I2 formed an equimolar complex with papain and benzoylarginine-2-naphthylamide hydrolase. I2 was present in rat skin, muscle, lung, and small intestine, but not in kidney, liver, or serum. A similar inhibitor was found in skin extracts of cat, rabbit, guinea pig, and man.

Animals↗
PubMed1975

Purification and biochemical characterization of rat skin cathepsin D.

The hemoglobin-hydrolyzing, acidic proteinase activity of rat skin was purified by using ammonium sulfate precipitation. Sephadex G-100 gel column chromatography, acid treatment, and DEAE-cellulose column chromatography, giving a purification coefficient of 182. The pH optimum, molecular size, substrate specificity, as well as inhibitor and activator sensitivity of the enzyme preparation, corresponded closely to those of cathepsin D. The enzyme activity was separated from cathepsin B1. The present status of the knowledge of skin cathespins is reviewed.

Ammonium Sulfate↗
PubMed1975

Binding of folic acid to serum proteins. V. Tritiated folic acid in the liver.

Sephadex G-200 chromatographies of the liver cell sap of rabbits, 1, 3 and 6 days after an injection of 3H-folic acid activity (FAA) into the circulation, were used in an attempt to study the binding of this labelled FAA to liver proteins. The labelled FAA was quickly accumulated in the liver, and in the cell sap it was grouped chromatographically to two maxima, which corresponded to the two maxima of microbiological FAA (L. casei). The maxima were eluated in the chromatography together with cell sap proteins. The possible coupling of FAA to proteins in the liver is discussed.

Animals↗