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M Manabe

Publications and source records attributed to M Manabe.

At least 19 recordsLinked to original sources
PubMed1992

Characterization of a keratinocyte-specific extracellular epitope of desmoglein. Implications for desmoglein heterogeneity and function.

Despite the presumed importance of desmoglein, a 160-kDa glycoprotein, in desmosome formation and its possible involvement in certain blistering skin diseases, the precise location and function of this protein have not yet been firmly established. We describe here the characterization of a new monoclonal antibody, AE23, against an extracellular epitope of desmoglein. Both the AE23 epitope and another epitope, defined by the previously characterized DG3.4 antibody, reside on a 160-kDa human epidermal desmoglein as evidenced by their identical solubility profile, their coexistence in a 130-kDa desmoglein degradative product, their coadsorption by an AE23 immunoaffinity column, and the identical changes in the two antigens' electrophoretic mobility after air oxidation and deglycosylation. The AE23 epitope is resistant to various endoglycosidases, suggesting that sugar moieties are not involved. Characterization of several proteolytic fragments of this epidermal desmoglein enabled us to map the DG3.4 epitope to a 96-kDa intracellular domain and the AE23 epitope to an extracellular domain flanked by the plasma membrane and the distal N-glycosylation site(s). However, these two epitopes do not always coexist on the same desmoglein molecule. For example, tissue surveys showed that although the DG3.4 epitope is present in the desmogleins of all epithelial cell types, the AE23 epitope is limited to normal keratinocytes. Moreover, electron microscopic localization data indicate that whereas the DG3.4 epitope is detected in the submembranous plaques of desmosomes, the AE23 epitope is present in the intercellular space of both desmosomal and nondesmosomal areas. These results raise the possibility that there exist several biochemically closely related isoforms of desmoglein, one (AE23+/DG3.4+) restricted to epidermal desmosomes, one (AE23+/DG3.4-) uniformly distributed along the keratinocyte cell surface, and another (AE23-/DG3.4+) present in desmosomes of simple epithelia and basal cells of cultured keratinocytes. The uniform distribution of at least one desmoglein-related antigen in the intercellular space of keratinocytes coupled with the realization that different isoforms of desmogleins form a subfamily of cadherins suggest that desmoglein(s) may play a more general role in keratinocyte adhesion than previously appreciated.

Animals↗
PubMed1992

Separation of oligogalacturonic acids by high-performance gel filtration chromatography on silica gel with diol radical.

Oligogalacturonic acids (OLGAs) ranging from two to nineteen residues in length were separated using high-performance gel filtration chromatography on a silica gel with diol radical. The optimum conditions (eluent, column temperature) for separation of OLGAs by high-performance gel filtration chromatography were investigated. The column used in this experiment allowed a high pressure of 4900 p.s.i. and a flow-rate of 2 ml/min. The stationary phase of silica gel stabilized the separation of OLGAs. The peaks of OLGAs separated using this column were assigned by comparing retention times with standards, and the molecular weights of the corresponding OLGAs were determined by fast atom bombardment mass spectrometry.

Chromatography, Gel↗
PubMed1992

Interaction of trichohyalin with intermediate filaments: three immunologically defined stages of trichohyalin maturation.

"Trichohyalin" is a 220-kD protein found in trichohyalin granules that are present as major differentiation products in the medulla and inner root sheath cells of human hair follicles. It was unclear whether this protein served as an intermediate filament precursor in the inner root sheath or as an intermediate-filament-associated (matrix) protein. We have produced a panel of monoclonal antibodies (AE15-17) to this protein and used them to trace its fate during inner root sheath differentiation. These studies have allowed us to define three immunologically distinct forms of this trichohyalin protein. They are 1) the AE15-positive form, which is found throughout all trichohyalin granules; 2) the AE16-positive form, which is localized as discrete punctae on the surface of trichohyalin granules; and 3) the AE17-positive, intermediate-filament-bound form, which associates with the inner root sheath filaments with a regular, 400-nm periodicity. From these results we suggest that the 220-kD trichohyalin protein is an intermediate-filament-associated protein that may play a role in the lateral aggregation, precise alignment, and stabilization of inner root sheath filament bundles.

Animals↗
PubMed1992

Keratohyalin, trichohyalin and keratohyalin-trichohyalin hybrid granules: an overview.

Filaggrin and trichohyalin are the two major intermediate filament associated proteins which interact with keratin filaments in the skin. These two proteins initially accumulate in cytoplasmic granules called keratohyalin or trichohyalin granules which provide prominent morphological hallmarks of differentiation in the epidermis and the inner root sheath of hair follicles, respectively. The contents of each of these granules are modified and subsequently released into the cytoplasm of the fully mature cells where they function in the role of aggregating keratin filament bundles. We are beginning to identify several important aspects relative to the unique biological functions of both filaggrin and trichohyalin during the late stages of keratinocyte differentiation. This overview summarizes recent work on these proteins and will also highlight the existence of novel cytoplasmic granules, keratohyalin-trichohyalin hybrid granules, in dorsal tongue epithelia.

Animals↗
PubMed1992

Characterization of sciellin, a precursor to the cornified envelope of human keratinocytes.

The cornified envelope, located beneath the plasma membrane of terminally differentiated keratinocytes, is formed as protein precursors are cross-linked by a membrane associated transglutaminase. This report characterizes a new precursor to the cornified envelope. A monoclonal antibody derived from mice immunized with cornified envelopes of human cultured keratinocytes stained the periphery of more differentiated cells in epidermis and other stratified squamous epithelia including hair and nails. The epitope was widely conserved among mammals as determined by immunohistochemical and Western analysis. Immunoelectron microscopy localized the epitope to the cell periphery in the upper stratum spinosum and granulosum of epidermis. In the hair follicle, the epitope was present in the internal root sheath and in the infundibulum, the innermost aspect of the external root sheath. The antibody recognized a protein of relative mobility (M(r)) 82,000, pI 7.8. The protein was a transglutaminase substrate as shown by a dansylcadaverine incorporation assay. Purified cornified envelopes absorbed the reactivity of the antibody to the partially purified protein and cleavage of envelopes by cyanogen bromide resulted in release of immunoreactive fragments. The protein was soluble only in denaturing buffers such as 8 M urea or 2% sodium dodecyl-sulfate (SDS). Partial solubility could be achieved in 50 mM TRIS pH 8.3 plus 0.3 M NaCl (high salt buffer); the presence of a reducing agent did not affect solubility. Extraction of cultured keratinocytes in 8 M urea and subsequent dialysis against 50 mM TRIS pH 8.3 buffer resulted in precipitation of the protein with the keratin filaments. Dialysis against high salt buffer prevented precipitation of the protein. The unique solubility properties of this protein suggest that it aggregates with itself and/or with keratin filaments. The possible role of the protein in cornified envelope assembly is discussed. We have named this protein Sciellin (from the old english "sciell" for shell).

Animals↗
PubMed1992

Identification of an 85-100 kDa glycoprotein as a cell surface marker for an advanced stage of urothelial differentiation: association with the inter-plaque ('hinge') area.

Although bladder cancers account for almost 5% of all human cancer deaths, little is known about the biochemistry of urothelial differentiation. We have recently identified three major protein subunits ('uroplakins') of asymmetric unit membranes (AUM), which form rigid-looking plaques covering up to 70% of the apical surface of urothelial superficial (umbrella) cells. The ordinary-looking plasma membranes that interconnect these plaques are believed to be functionally specialized, serving as flexible but durable 'hinges'. Whether these hinge membranes are biochemically unique is unknown. Using a new monoclonal antibody (AE32) we have identified an 85-100 kDa glycoprotein (UGP85) which appears to be urothelium-specific. In both normal urothelium and cultured urothelial colonies this cell surface protein is associated mainly with superficial cells, suggesting that its expression is differentiation dependent. Results from in vitro translation experiments indicated that this glycoprotein contains a core polypeptide of about 55 kDa. Using immunogold localization techniques, we showed that in cultured urothelial colonies--which are known to lack mature AUM plaques--UGP85 is distributed relatively uniformly on the apical surface of some differentiated cells. However, in superficial cells of normal urothelium UGP85 is mainly associated with the hinge areas. These results raise the possibility that UGP85 is a plasma membrane component which can be excluded, to varying extents, from the plaque region as 12 nm protein particles are assembled into a tightly packed paracrystalline AUM structure. The identification of UGP85 provides the first evidence that the hinge areas interconnecting the urothelial plaques are biochemically distinguishable from the plasma membranes of the relatively undifferentiated urothelial cells of the lower cell layers.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1992

[Effect of halothane on the peripheral cutaneous vasoconstriction and shivering induced by internal body cooling in rabbits].

Although suppression of thermoregulatory mechanisms by anesthetics is generally assumed, the extent to which thermoregulatory responses are active during general anesthesia is not known. To evaluate the effect of anesthetics on thermoregulation, we investigated the threshold body core temperatures to induce peripheral cutaneous vasoconstriction and shivering in spontaneously breathing rabbits. Rabbits are anesthetized with halothane at 0.05, 0.2 and 0.4 MAC (minimum alveolar concentration). Internal whole body cooling was performed by perfusing the cool water through an intestinal U-shaped thermode placed in the colon. Core (esophagus) and peripheral (ear) temperatures were measured with thermistors. The esophageal temperatures at the beginning of peripheral cutaneous vasoconstriction and shivering induced by internal whole body cooling were determined. Peripheral cutaneous vasoconstriction was not significantly affected by halothane. However, the incidence of shivering was significantly decreased by halothane dose-dependently. Threshold of shivering (37.3 +/- 0.8 degrees C) was significantly lower than that of peripheral cutaneous vasoconstriction (38.9 +/- 1.1 degrees C). We conclude that the halothane can exert an influence on shivering.

Animals↗
PubMed1992

[Usefulness of 0.02 percent epinephrine solution to widen the nasal cavity].

There are many reports describing how to use epinephrine solution before nasal intubation, but there are few reports showing how much of the nasal cavity is widened by using epinephrine solution. The purpose of this study is to examine the usefulness of epinephrine solution to widen the nasal cavity before nasal intubation by measuring the decrease of the nasal concha. Twenty patients who were scheduled for nasal intubation were divided into two groups: 0.02 percent (1:5000) epinephrine solution (0.02 group, n = 10). 0.033 percent (1:3000) epinephrine solution (0.033 group, n = 10). The solutions were instilled on long cotton-tipped applicators that were slowly inserted until they reached posterior wall of the nasopharynx. We examined the area of the inferior nasal concha on X-P before and after inserting applicators in two groups. The area of the inferior nasal concha on X-P decreased 25 percent and 27 percent after using epinephrine solution in 0.02 group and 0.033 group, respectively and the decreases of the area were significant. But there was no significant difference between two groups. We conclude that 0.02 percent epinephrine solution is useful and adequate to widen the nasal cavity before nasal intubation.

Adolescent↗
PubMed1991

Effects of sodium pentothal and sufentanil on serotonin induced constriction of canine coronary artery rings without endothelium.

1. The individual and combined effects of sufentanil and sodium pentothal on canine coronary artery vasomotor responses to 5-HT were studied in an isolated vascular ring preparation. 2. Clinical concentrations of sufentanil have little effect on basal coronary tension or constriction induced by either 5-HT or sodium pentothal individually, until very high doses greater than 0.26 microM are reached. 3. Sodium pentothal causes coronary constriction at clinical concentrations and this effect is additive and possibly potentiated when combined with 5-HT. 4. Sufentanil inhibits coronary constriction induced by the combination of sodium pentothal and 5-HT.

Anesthetics↗
PubMed1991

Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in ichthyosis vulgaris.

Filaggrin is a histidine-rich, basic protein whose name was first proposed based on its ability to aggregate intermediate filaments in vitro. Based on this in vitro observation, it has generally been assumed that filaggrin functions in vivo as a matrix protein which causes keratin filaments to become densely packed in the terminally differentiated cornified cells. Inconsistent with this view however, is the well-known observation that keratin aggregation appears to proceed normally in the affected epidermis of ichthyosis vulgaris patients despite a greatly reduced quantity of filaggrin. To address this issue, we used immuno-electron microscopy to localize filaggrin and its cross-reactive precursor, profilaggrin, in human and mouse epidermis, as well as in ichthyosis vulgaris epidermis. We found that the localization of filaggrin in lower cornified cells correlates precisely with the formation of aggregated keratin filaments, and the disappearance of filaggrin in upper cornified cells correlates precisely with the loosening of keratin filaments. Furthermore, we showed that, even in ichthyosis vulgaris, small amounts of filaggrin/profilaggrin are present as electron-dense deposits associated with keratin filaments in the granular cells, and that the localization of this small amount of antigen again correlates with the aggregation state of keratin filaments. These data strongly suggest that filaggrin is indeed involved in filament aggregation in vivo.

Animals↗
PubMed1991

[Separation of high density lipoprotein (HDL) using anti-apo A-I, apo A-II immuno-affinity chromatography to evaluate the effects of probucol].

An assessment has been made regarding the changes of the particles of lipoprotein A-I without A-II (Lp A-I) and lipoprotein A-I with A-II (LpA-I/A-II) which correspond to HDL subfraction isolated by the use of anti-apo A-I and A-II antibody affinity columns in order to quantitatively and qualitatively investigate the change of HDL caused by administration of probucol and pravastatin which are therapeutic drugs for hypercholesterolemia. Probucol caused significant decreases of HDL-cholesterol, plasma apo A-I/apo A-II ratio and particles larger in diameter than 10.4 nm. Comparing Lp A-I and A-I/A-II ratios with those in normolipidemic controls and the ratios before and after administration of probucol, the decrease of LpA-I ratio was found to be remarkable after prolonged administration of probucol, and it was presumed that the decrease of HDL cholesterol by prolonged administration reflects the decrease of LpA-I particles more than the decrease of LpA-I/A-II. On the other hand, no significant change was seen in HDL cholesterol, plasma apo A-I/apo A-II ratio or HDL particle size in the pravastatin group. It is considered essential to observe HDL from the aspect of apoprotein, which plays an important role in the metabolism of lipoprotein, in the assessment of the anti-atherogenic activity of HDL cholesterol in future. In other words, it is necessary to analyze the change of HDL from the aspect of Lp A-I and Lp A-I/AII and investigate their respective metabolisms and roles.

Adult↗
PubMed1991

[The effect of prostaglandin E1 (PGE1) on body temperature and on postoperative shivering under high dose epidural fentanyl].

Ninety-nine elective abdominal surgeries were performed under high dose epidural fentanyl anesthesia. PGE1 (0.02 microgram.kg-1.min-1 = 0.02 gamma) was administered to 34 patients (0.02 gamma group), and PGE1 (0.05 gamma) was administered to 16 patients (0.05 gamma group). PGE1 was not administered to 49 patients (control group). The effect of PGE1 on body temperature and on postoperative shivering was compared within three groups. In the 0.02 gamma group, the temperature of the fingertip was significantly higher and the rectum-fingertip temperature gradient was significantly lower than in the other groups. The forearm-fingertip temperature gradient was lower in the 0.02 gamma and 0.05 gamma groups than in the control group. The incidence of postanesthetic shivering was significantly lower in the 0.05 gamma group than in the other groups. These results suggest that; 1) PGE1 (0.02 gamma and 0.05 gamma groups) affects the peripheral blood flow and peripheral temperature, and 2) PGE1 (0.05 gamma group) significantly affects the incidence of postanesthetic shivering.

Abdomen↗
PubMed1991

[Epidural anesthesia with high dose fentanyl for thoracic surgeries].

Twenty-two elective thoracic surgeries were performed under epidural high dose fentanyl anesthesia. These included 11 mastectomies, 3 lung lobectomies, and 8 operations for esophageal carcinoma. Through an epidural catheter, 10 micrograms.kg-1 fentanyl with [E (+)] or without [E (-)] epinephrine (1: 100,000) was given. N2O (66%) and enflurane (0.2-0.8%) were also administered, and muscle relaxants were given as needed. The onset and duration of the action were approximately 20 minutes and 3 hours, respectively. Anesthesia was maintained with enflurane (up to 0.4%) in 17 patients (77.3%). There were no differences between the E (+) group and the E (-) group. Systolic pressure, diastolic pressure and heart rate during operations were about 30% lower than those observed before the operations. Patients recovered from anesthesia rapidly. Naloxone was administered intravenously in 6 patients after mastectomies or lung lobectomies (42.9%), whose respiratory rate was below 10.min-1. The patients with short operating time (shorter than 2 hours) needed more naloxone. Troubles did not occur either in the recovery room or in the ward with both naloxone and non-naloxone groups.

Adult↗
PubMed1991

[Interaction between diltiazem and sevoflurane in the canine blood-perfused papillary muscle and sinoatrial node preparations].

Experiments were carried out on 17 canine isolated cardiac tissue preparations perfused by arterial blood from donor dogs. Diltiazem was continuously infused i.v. into the conscious (10 dogs) and the sevoflurane anesthetized (2.36%, 7 dogs) donor dogs at a rate of 20 micrograms.kg-1.min-1 for 60 minutes. The changes induced by diltiazem were normalized by the values at the start of diltiazem infusion, and the comparison was made between the two groups. 1) The decrease in heart rate and increase in PQ interval were smaller in conscious dogs than in the anesthetized dogs. 2) Decrease in developed tension in conscious state was smaller than that during sevoflurane anesthesia. 3) There was no significant difference in the decrease in blood pressure or sinoatrial rate between the conscious group and the anesthetized group. These results indicate that sevoflurane anesthesia removes the compensatory reflex which is present in the conscious state and also increases cardiovascular depressant effects of diltiazem.

Anesthetics↗
PubMed1990

Desmoglein shows extensive homology to the cadherin family of cell adhesion molecules.

Desmoglein is a major adhesive component of the desmosome. It is also at least one of the antigenic targets of pathogenic antibodies circulating in the sera of patients with the blistering disease Pemphigus foliaceus. To examine the molecular basis of desmosomal adhesion and to further our understanding of its disruption in various bullous disorders we have cloned cDNAs encoding four of the extracellular domains of desmoglein. The predicted amino acid sequence of these clones shows extensive homology with the cadherin class of calcium-dependent cell adhesion molecules. Desmoglein represents a novel subtype of this family.

Amino Acid Sequence↗
PubMed1990

Medullary projection of nonaugmenting inspiratory neurons of the ventrolateral medulla in the cat.

In Nembutal-anesthetized, immobilized, and artificially ventilated cats, we studied the morphological characteristics of inspiratory neurons with nonaugmenting firing patterns. HRP was injected intracellularly into a total of 22 neurons of the Bötzinger complex (BOT) and the ventral respiratory group (VRG). In 20 cases somata with their axonal trajectories were stained, and in two cases only axons were stained. None of the neurons stained could be antidromically activated by stimulation of the cervical cord. The somata of 20 neurons were located in the vicinity of the nucleus ambiguus or the retrofacial nucleus (RFN) between 600 microns and 2,800 microns caudal to the rostral end of the RFN. Their axons could be traced for a distance of several millimeters on the side of the somata, and showed various projection patterns. According to these projection patterns, the 20 neurons were tentatively classified into four groups: A (8/20), B (4/20), C (6/20), and motoneurons (2/20). Group A neurons gave off extensive axon collaterals that arborized and distributed boutons predominantly in the BOT and the VRG areas. Group B neurons had less extensive axon collaterals with various projection patterns, projecting rarely to the BOT or the VRG area. Group C neurons sent their stem axons, without issuing any axonal collaterals, to the contralateral side in five cases and to the ipsilateral pons in one case. The two motoneurons had axons leaving the brainstem without any intramedullary collaterals. Thus, the nonaugmenting inspiratory neurons showed morphological variations, which may play different roles in neural control of respiration.

Animals↗
PubMed1990

Large scale purification and immunolocalization of bovine uroplakins I, II, and III. Molecular markers of urothelial differentiation.

The differentiation of mammalian urothelium culminates in the formation of asymmetrical unit membrane (AUM). Using gradient centrifugation and detergent wash, we purified milligram quantities of AUMs which, interestingly, contained three major proteins (15, 27, and 47 kDa) that appeared to be identical to the three immunoaffinity purified, putatively AUM-associated proteins that we described earlier (Yu, J., Manabe, M., Wu, X.-R., Xu, C., Surya, B., and Sun, T.-T. (1990) J. Cell Biol., 111, 1207-1216). Peptide mapping and immunoblotting established that these three proteins were distinct molecules. Using monospecific antibodies to these three proteins, we showed that they were all restricted to the superficial urothelial cells and were AUM-associated. The 27- and 15-kDa proteins were detected exclusively on the luminal side of mature, apical AUMs. In contrast, epitopes of the 47-kDa protein were detected on both sides of apical AUMs suggesting a transmembranous configuration. These results (i) provide the strongest evidence thus far that AUM contains three major proteins (the 27-kDa uroplakin I, 15-kDa uroplakin II, and 47-kDa uroplakin III) which form an extremely insoluble complex, (ii) suggest that uroplakin II, like uroplakin I (Yu, J., Manabe, M., Wu, X.-R., Xu, C., Surya, B., and Sun, T.-T. (1990) J. Cell. Biol. 111, 1207-1216), translocates from one side of the membrane to another during AUM maturation, (iii) indicate that uroplakin III may play a different structural role than uroplakins I and II in AUM formation, and (iv) establish the three uroplakins as markers for an advanced stage of urothelial differentiation.

Animals↗