Biomedical subjects

H Yokozeki

Publications and source records attributed to H Yokozeki.

105 records · Page 6Linked to original sources

PubMed1991

In situ expression of messenger RNA of interleukin-1 and interleukin-6 in psoriasis: interleukin-6 involved in formation of psoriatic lesions.

Psoriasis is a disease of abnormal proliferation and differentiation of epidermal cells. Several cytokines released by keratinocytes are implicated as factors responsible for this pathological condition of the epidermis. In order to elucidate the role of these cytokines in psoriasis, messenger RNA (mRNA) expression of interleukin-1 (IL-1) and IL-6 in psoriatic epidermis was investigated using biotin-labelled complementary DNA (cDNA) of the cytokines. Messenger RNA of IL-1 alpha was weakly detected in some normal healthy epidermis specimens and more strongly in all the perilesional uninvolved psoriatic epidermis specimens. It was also expressed in the transitional zone between uninvolved and fully developed psoriatic skin, but was not expressed in lesional skin. In contrast, IL-6 mRNA was rarely expressed in normal healthy epidermis, but was expressed in perilesional uninvolved psoriatic epidermis, in the transitional zone and in the fully developed lesional epidermis, with the maximum intensity in the transitional zone. Expression of mRNA of IL-6 receptor showed a similar tendency to that of IL-6. It was expressed in psoriatic epidermis, most strongly in the transitional zone, but not in normal healthy epidermis. IL-6 was demonstrated immunohistochemically in psoriatic epidermis, but IL-6 receptor was demonstrated only in the transitional zone. Thus IL-6 and its receptor expression correlated well with the formation of psoriatic lesions where IL-1 may initiate their expression. IL-6 may play an important role in the pathogenesis of psoriasis.

Adult↗

PubMed1991

Cysteine proteinase inhibitor in eccrine sweat is derived from sweat gland.

Although cysteine proteinases have been reported to be present in human eccrine sweat, their endogenous inhibitors, cysteine proteinase inhibitors (CPIs), have remained unstudied. We now present evidence that CPIs are indeed a true ingredient of human eccrine sweat. Sweat induced in sauna was collected over a Vaseline barrier placed on the skin to minimize epidermal contamination. The absence of major epidermal contamination of the sweat was further ensured by monitoring an epidermal marker, high-molecular-mass aminopeptidase. Sweat CPI was purified sequentially by chromatography with Sephacryl S-200, carboxymethylated papain-Sepharose, and anion-exchange Mono Q fast-protein liquid chromatography columns. Sweat CPI has a molecular mass of approximately 15 kDa, is stable for temperature (up to 80 degrees C) and pH (from 3 to 10), and inhibits papain, ficin, and sweat cathepsin B- and H-like enzymes. Sweat CPI may be of sweat gland origin because 1) the rate of CPI output in sweat (CPI concentration x sweat rate) is constant over 45 min; 2) antibody against epidermal CPI, which cross-reacts with sweat CPI, localized immunoreactivity in the sweat duct; 3) CPI activity was present in the glandular extracts of control and methacholine-stimulated (for 1 h in vitro) human sweat glands; and 4) the peaks of CPI activity in the glandular extract and sweat CPI were both eluted (by high-pressure liquid chromatography) at around 15 kDa. Sweat CPI may be very similar to epidermal CPI (which belongs to the stefin family of CPIs) because of many shared characteristics. The identity and function of sweat CPI remain to be studied.

Cysteine Proteinase Inhibitors↗

PubMed1991

[A case of systemic lupus erythematosus with the central nervous system manifestations (CNS-lupus) mimicking herpes simplex encephalitis (HSE)].

A 21-year-old male with SLE developed seizure, loss of consciousness and focal signs referable to involvement of the front-temporal brain regions. MRI (magnetic response imaging) image revealed high signal areas in the temporal lobes. By these findings, herpes simplex encephalitis (HSE) was suspected at first. But neither isolation of herpes simplex virus nor HSV specific IgM by ELISA was detected. Acyclovir administration by intravenous infusion was'nt effective but corticosteroid pulse therapy was effective. The level of anticardiolipin antibody was very high. Finally, the diagnosis of CNS-lupus with HSE-like characteristics was made in this case.

Adult↗

PubMed1990

Human epidermal T cells predominantly belong to the lineage expressing alpha/beta T cell receptor.

The epidermis of clinically normal-appearing human skin harbors a phenotypically heterogeneous population of T lymphocytes (TCs), the majority of which are CD2+/CD3+/CD5+ "memory" cells, but in an unactivated state, and express the TCR-alpha/beta. In contrast to murine skin, only a very minor subpopulation of CD3+ cells in the human epidermis bears the TCR-gamma/delta. Epidermal TCs primarily are distributed along the rete ridges in the basal keratinocyte layer and are often in close apposition to Langerhans cells (LCs). These TCs were propagated from epidermal cell suspensions after stimulation with TC activating agents (Con A, rIL-1, rIL-2), then evaluated for phenotypic features and TCR diversity. Similar to the in situ situation, most were CD4-/CD8+/TCR-alpha/beta+. In addition, two cultures contained TCR-gamma/delta+ cells; one of these determined to be an adherent CD4-/CD8+ population. Epidermal TCs were significantly (p less than 0.0001) more abundant in the sole than in the other body regions examined (i.e., 40 vs. 7 CD3+ cells/linear centimeter of epidermis) and seemed to have a particular affinity for the acrosyringial epithelium of eccrine sweat ducts. Moreover, the sole usually contained a greater number of CD8+ relative to CD4+ TCs, whereas the epidermal CD4/CD8 ratio in the trunk and extremities was quite variable, although the trend also was towards a slightly larger percentage of CD8+ cells. Collectively, our data suggest that the volar epidermis has a unique microenvironment which is responsible for both the higher density of TCs, preferentially CD8+, and lower number of LCs. This study has not only provided evidence for significant regional variability in the human epidermal TC population of normal skin, but also strengthens the concept for skin-associated lymphoid tissues (SALT), whereby memory TCs recirculate back to the epidermis and interact with resident antigen-presenting cells (i.e., LC).

Antibodies, Monoclonal↗

PubMed1990

Pharmacological responsiveness of dissociated native and cultured eccrine secretory coil cells.

Methacholine (MCh)- and isoproterenol (Iso)-stimulated 14CO2 production was compared between freshly dissociated rhesus sweat secretory coil cells (mainly clear cells) and cultured cells (grown on a collagen-coated plastic plate) derived from native cells. 14CO2 production was enhanced by MCh and by Iso in native coil cells (but not in ductal cells) in a pharmacologically specific and dose-dependent manner. 14CO2 production in subcultured coil cells (19-45 days in culture) was only one-third to one-fifth that of native cells. MCh-stimulated 14CO2 production was inhibited by ouabain and furosemide in both native and cultured coil cells. A decrease in 14CO2 production, of about one-half, was already evident in primary cells cultured for less than 1 wk. The decreased pharmacological responsiveness of the cultured coil cells was seen, although the cultured cells showed the typical epithelioid appearance, abundant mitochondria, the occasional presence of intercellular lacunae resembling intercellular canaliculi, and the persistence of immunoreactive keratin. We conclude that 1) a primary culture of sweat gland cells can be initiated from dissociated cells; 2) cultured sweat secretory coil cells qualitatively, but not quantitatively, retain the pharmacological responsiveness and transport activity of the native cells as determined by 14CO2 production; 3) collagenase-dissociated cells represent an excellent in vitro system for the study of glandular function at the cellular level; and 4) the decrease in pharmacological responsiveness is not simply due to trypsin treatment during harvesting of cultured cells, because that of organ-cultured, intact, secretory coils also declines with time of culture.

Animals↗

PubMed1990

Induction of eczematous skin reaction in experimentally induced hyperplastic skin of Balb/C mice by monoclonal anti-DNP IgE antibody: possible implications for skin lesion formation in atopic dermatitis.

Biphasic skin reaction with peak response at 1 and 24 h with prominent mast cell degranulation was induced by intravenous application of a monoclonal anti-DNP IgE antibody and subsequent skin test. This reaction was hapten-specific and mast-cell-dependent because no reaction was observed when oxasolone was used as an elicitation antigen or skin test was elicited in genetically mast-cell-deficient mice (W/Wvv). A partial spongiotic reaction and mononuclear cell infiltration into the epidermis were observed in mice with hyperplastic epidermis induced by topical retinoic acid. Cotransfer of DNFB-sensitized lymph node cells with anti-DNP IgE antibodies failed to enhance the skin test reaction in unsensitized mice. These results suggest that, to some degree, IgE antibody may play some role in the development of eczematous skin lesions in the rodent system without the involvement of cellular hypersensitivity.

Animals↗

PubMed1989

Drug-induced chronic pigmented purpura.

A close correlation between purpuric reaction and drugs was observed in seven cases of chronic pigmented purpura. The patients developed purpuric lesions after taking certain drugs for more than 3 years, were thiamine propyldisulfide in 2 cases, and chlordiazepoxide in 1 case. The purpuric lesions stopped recurring after removal of the drugs in the rest of the cases. It is suggested that drugs are among the etiological factors in chronic pigmented purpura.

Aged↗

PubMed1987

Partial purification and characterization of cysteine proteinases in eccrine sweat.

Attempts were made to purify and characterize cysteine proteinases in human eccrine sweat and further clarify their origin. Benzoyl-DL-arginine-beta-naphthylamide (BANA) and L-leucine beta-naphthylamide (LeuNA) hydrolases in thermally induced sweat were sequentially purified by Sephacryl S-200 chromatography and chromatofocusing, which yielded two major peaks of BANA hydrolase activity, BANA-I and BANA-II. Both enzymes are cysteine proteinases as evidenced by stimulation of enzymic activity by dithiothreitol and ethylenediaminetetraacetic acid and its inhibition by iodoacetic acid, (PCMB), and trans-epoxysuccinyl-L-leucylamido-(4-guanidino)-butane (E-64). Unlike BANA-II, BANA-I showed an additional aminopeptidase activity, an affinity to concanavalin A-Sepharose but no affinity to organomercurial sepharose and failed to hydrolyze benzyloxycarbonyl-phenylalanyl-arginine 4-methyl 7-coumarylamide (Z-Phe-Arg-NMec), a specific substrate for cathepsin B, which is poorly sensitive to leupeptin [inhibitor constant (Ki) = 1 X 10(-5) M] and relatively heat resistant. These and other characteristics such as its isoelectric points (PI) (= 5.8) and the Km for Arg-NMec (0.1 mM) and BANA (0.71 mM) all support the possibility that BANA-I is closely related to cathepsin H. In contrast, BANA-II is sensitive to Zn2+, leupeptin (Ki = 5.5 X 10(-9) M), is not adsorbed by concanavalin A- (Con-A)Sepharose, but is bound to organomercurial sepharose. It has a specificity to Z-Phe-Arg-NMec but not to Arg-NMec, has the molecular weight of 27, PI of 5.2, the pH optima for BANA (6.0), and the Km for BANA of 3.3 mM and the Km for Z-Phe-Arg-NMec of 0.1 mM. These features resemble those of liver cathepsin B. Leupeptin-sensitive BANA hydrolase was observed in the glandular extract of isolated sweat glands, which was increased after stimulation with methacholine and isoproterenol in vitro. The data are consistent with the notion that cathepsins B- and H-like enzymes are present in eccrine sweat and the former may be derived from the sweat gland.

Benzoylarginine-2-Naphthylamide↗

PubMed1987

Thiol-dependent aminopeptidase (350,000 mol wt) as a marker of epidermal contamination in sweat.

L-Leucine 2-naphthylamide (Leu-NA) hydrolytic activity is increased 20-fold in eccrine sweat collected by simple scraping (SS) compared with sweat collected over the white petrolatum (Vaseline) barrier (clean sweat, CS) [Am. J. Physiol. 250 (Regulatory Integrative Comp. Physiol. 19): R691-R698, 1986]. Sephadex G-200 chromatography of SS but not that of CS showed a single peak of Leu-NA hydrolytic activity (at pH 8) at 350,000 mol wt. An enzyme with similar molecular weight was eluted from tape-stripped stratum corneum and from stripped skin in situ. Anion-exchange FPLC of the 350,000 fractions yielded a single Leu-NA hydrolase peak at pH 8 (pool IV), which also showed hydrolytic activity for benzoyl-L-arginine-2-naphthylamide (BANA). Both Leu-NA and BANA hydrolytic activities of pool IV were thiol dependent, inhibited by heavy metals, and activated by ethylenediaminetetraacetic acid. The pool IV enzyme also hydrolyzed L-lysine- and L-arginine-2-naphthylamide. The most prominent BANA hydrolase activity was seen in both SS and CS at pH 5.0 at 33,000, which was not associated with Leu-NA hydrolytic activity. Diethylaminoethyl cellulose chromatography of the 33,000 fractions yielded three peaks of BANA hydrolytic activity in SS but only one in CS, suggesting that this thiol-dependent BANA hydrolyzing enzyme in CS may be of sweat gland origin. We conclude that the 350,000 thiol-dependent Leu-NA-hydrolyzing aminopeptidase is one of the most prominent epidermal contaminants and thus is a useful marker of epidermal contamination in sweat samples.

Adult↗

PubMed1987

[A case of intrascrotal rhabdomyosarcoma].

We report a case of intrascrotal rhabdomyosarcoma. A 15-year-old boy visited our clinic with the chief complaint of swelling of the right hemiscrotum. He had a history of fever and right hemiscrotal pain. With the initial diagnosis of acute epididymitis, the patient underwent medical therapy with antibiotics. One month later, because the mass had not responded to medical therapy, a right inguinal orchiectomy was done. Histologic examination revealed rhabdomyosarcoma. The patient received retroperitoneal lymph node dissection and combined chemotherapy with cyclophosphamide, bleomycin, actinomycin-D, adriamycin and vinblastine. He was well 5 years and 10 months postoperatively with no evidence of tumor recurrence or metastasis.

Combined Modality Therapy↗

PubMed1986

Proteolytic enzymes in human eccrine sweat: a screening study.

Thermally induced human eccrine sweat was collected both by simple scraping (SS) and by a polyethylene sweat collector that covered the Vaseline-coated skin of the back to minimize epidermal contamination (CS, clean sweat). Using synthetic chromogenic Kabi S-series substrates, we demonstrated a variety of proteases in both SS and CS, the former being higher than the latter to varying extents. The higher enzyme activity in SS is mainly due to epidermal contamination because abundant protease activity was eluted from the nonperspiring stripped and unstripped skin in vivo and from the stripped stratum corneum itself. The electrophoretic separation of sweat protein has shown that CS contains at least 7 and SS 15 gelatinolytic proteinases. Although some CS proteinases could be derived from the sweat duct, the sweat secretory coil itself is responsible for at least two proteinases at 78 and 25 kilodaltons. The identity and function of these enzymes remain to be studied.

Caseins↗

PubMed1986

Origin of periodic acid-Schiff-reactive glycoprotein in human eccrine sweat.

To evaluate the possible involvement of ductal blockade with periodic acid-Schiff (PAS)-positive materials in the mechanism of hidromeiosis in humans, skin slices were incubated with methacholine for 2 h and PAS-positive materials localized histologically in the ductal lumen. In 20% of the glands complete ductal blockade with PAS-positive materials was noted. The characteristics and origin of such PAS-positive glycoproteins in human sweat were then studied using various electrophoretic techniques. One-dimensional sodium dodecylsulfate-polyacrylamide gel electrophoresis (1-D SDS-PAGE) demonstrated considerable individual variation in the electrophoretic pattern; however, four major bands at 45, 28, 20, and 18K shared by different individuals, were PAS positive. Further studies using two-dimensional SDS-PAGE, immunodiffusion and immunoaffinity chromatography demonstrated that the PAS-positive glycoproteins are not derived directly from serum because they are electrophoretically and antigenically distinct from serum proteins, including alpha 1-glycoprotein, alpha 2-HS-glycoprotein, and alpha 1-antitrypsin. Since only dark cell granules are densely stained in the histochemical PAS staining, and because antiserum produced against the PAS-positive band selectively stained cells facing the secretory coil lumen (which are most likely dark cells), it is suggested that PAS-positive sweat glycoproteins are derived predominantly from the dark cells.

Adult↗

PubMed1985

Induction and suppression of contact sensitivity by liposomes carrying molecules from haptenated epidermal cells.

Liposomes carrying molecules from trinitrophenylated epidermal cells (TNP-EC) liposomes stimulated the hapten-specific proliferation of lymphocytes in vitro in our previous study. In order to analyze the role of TNP-EC liposomes in vivo, they were injected into naive mice. TNP-EC liposomes induced contact sensitivity effectively when injected either s.c. or i.p. Contact sensitivity induced by TNP-EC liposomes was a long-lived T cell-mediated reaction. A s.c. injection of liposomes with molecules from TNP-Ia antigen-depleted epidermal cells [TNP-EC (Ia-) liposomes] failed to induce contact sensitivity and developed unresponsiveness. This unresponsiveness was transferred by T cells, i.e., suppressor T cells. Therefore, it is suggested that Ia antigens in epidermal cells play a critical role for induction and suppression of contact sensitivity.

Animals↗

PubMed1984

Induction of hapten-specific lymphoid cell proliferation by liposome-carrying molecules from haptenated epidermal cells in contact sensitivity.

Liposomes containing the extract of trinitrophenylated (TNP) epidermal cells stimulated lymph node cells from TNCB-sensitized mice effectively. Optimal stimulation was achieved by the liposome containing 0.06 microgram of the extract of TNP epidermal cells/microgram of phospholipid at a concentration of 20 micrograms phospholipid/ml. The response was hapten-specific and macrophage-dependent. UV irradiation of the epidermal cells abolished their ability to stimulate the lymph node cells. Furthermore, the liposomes containing the extract of TNP epidermal cells treated with anti-Ia and complement failed to stimulate the lymph node cells. The liposomes recovered their reactivity when nonhaptenated Ia antigen-rich epidermal extract was added. Taken together, it is likely that haptenated molecules and Ia antigen on the liposome stimulated T-lymphocytes in the presence of macrophages.

Animals↗

PubMedDate not supplied

Acute exanthematous pustular drug eruption induced by mexiletine.

A 56-year-old man developed infiltrated erythemas on the trunk, extremities, and face with marked facial edema, one month after taking mexiletine hydrochloride for his arrhythmia. A number of pustules were also noted on the surface of erythemas on his chest and face. Laboratory examination showed liver dysfunction and hypereosinophilia. The culture from pustules was sterile. Histological examination of the biopsied skin from a pustular lesion revealed a subcorneal abscess, and perivascular infiltration of lymphocytes, mononuclear cells and eosinophils in the upper dermis. The skin lesions and facial edema as well were improved within three weeks by withdrawal of mexiletine hydrochloride. Patch tests with 10% and 20% mexiletine hydrochloride in petrolatum showed positive reaction, however, pustules were not provoked on the tested site. We conclude that pustules, infiltrated erythema and facial edema were the signs of acute exanthematous pustular drug eruption induced by mexiletine hydrochloride.

Acute Disease↗