Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 20 de 31
Filter
Add more filters

Country/Region as subject
Publication year range
1.
Geriatr Nurs ; 43: 91-96, 2022.
Article in English | MEDLINE | ID: mdl-34844130

ABSTRACT

The functional, interactive, and critical domains of health literacy are associated with health. However, studies examining the relationship between health literacy subdomains and health in the Chinese-speaking context are still limited. Thus, we aimed to examine the association of functional, interactive, and critical health literacy with self-rated health among older Taiwanese adults. A total of 1,072 participants aged 60 or older were included in the analysis. Health literacy was measured by the 11-item short-form Mandarin Health Literacy Scale and validated tools. Self-rated health was categorized into good (good/very good), fair, and poor (poor/very poor) status. Multinomial logistic regression revealed that only interactive health literacy was associated with reporting good health status (OR = 2.30; 95% CI = 1.65 to 3.21). Conversely, all health literacy subdomains were not associated with reporting poor health. This study suggested that interactive health literacy was the key determinant of good self-rated health status for community-dwelling older adults.


Subject(s)
Health Literacy , Aged , Asian People , Health Status , Humans , Independent Living
2.
PLoS Pathog ; 11(10): e1005203, 2015 Oct.
Article in English | MEDLINE | ID: mdl-26491970

ABSTRACT

Betanodaviruses cause massive mortality in marine fish species with viral nervous necrosis. The structure of a T = 3 Grouper nervous necrosis virus-like particle (GNNV-LP) is determined by the ab initio method with non-crystallographic symmetry averaging at 3.6 Å resolution. Each capsid protein (CP) shows three major domains: (i) the N-terminal arm, an inter-subunit extension at the inner surface; (ii) the shell domain (S-domain), a jelly-roll structure; and (iii) the protrusion domain (P-domain) formed by three-fold trimeric protrusions. In addition, we have determined structures of the T = 1 subviral particles (SVPs) of (i) the delta-P-domain mutant (residues 35-217) at 3.1 Å resolution; and (ii) the N-ARM deletion mutant (residues 35-338) at 7 Å resolution; and (iii) the structure of the individual P-domain (residues 214-338) at 1.2 Å resolution. The P-domain reveals a novel DxD motif asymmetrically coordinating two Ca2+ ions, and seems to play a prominent role in the calcium-mediated trimerization of the GNNV CPs during the initial capsid assembly process. The flexible N-ARM (N-terminal arginine-rich motif) appears to serve as a molecular switch for T = 1 or T = 3 assembly. Finally, we find that polyethylene glycol, which is incorporated into the P-domain during the crystallization process, enhances GNNV infection. The present structural studies together with the biological assays enhance our understanding of the role of the P-domain of GNNV in the capsid assembly and viral infection by this betanodavirus.


Subject(s)
Capsid Proteins/chemistry , Nodaviridae/chemistry , Virus Assembly , Calcium/metabolism , Crystallography, X-Ray , Polyethylene Glycols/pharmacology , Protein Structure, Tertiary , Virion/chemistry
3.
Nano Lett ; 15(2): 974-80, 2015 Feb 11.
Article in English | MEDLINE | ID: mdl-25602598

ABSTRACT

Single crystalline p-type CdTe:Sb nanobelts were fabricated using an Au-catalyzed chemical vapor deposition method. Low carrier concentration and low mobility even at high Sb incorporation manifest compensation in the system. From cross examination of temperature-dependent charge transport and photoluminescence measurements, two major acceptor levels induced by Sb doping are determined: a shallow level attributed to substitutional Sb dopants without lattice relaxation and an associated deeper level resulted from large lattice relaxation-AX centers. Persistent photoconductivity and hysteresis photoconductance under the thermal cycle elucidate the nature of AX centers. This comprehensive investigation of the impurity levels in the material system is essential for the design and development of nanoelectronic devices based on the CdTe nanostructures.

4.
Acta Crystallogr D Biol Crystallogr ; 71(Pt 4): 1006-21, 2015 Apr.
Article in English | MEDLINE | ID: mdl-25849409

ABSTRACT

10-Formyltetrahydrofolate dehydrogenase (FDH), which is composed of a small N-terminal domain (Nt-FDH) and a large C-terminal domain, is an abundant folate enzyme in the liver and converts 10-formyltetrahydrofolate (10-FTHF) to tetrahydrofolate (THF) and CO2. Nt-FDH alone possesses a hydrolase activity, which converts 10-FTHF to THF and formate in the presence of ß-mercaptoethanol. To elucidate the catalytic mechanism of Nt-FDH, crystal structures of apo-form zNt-FDH from zebrafish and its complexes with the substrate analogue 10-formyl-5,8-dideazafolate (10-FDDF) and with the products THF and formate have been determined. The structures reveal that the conformations of three loops (residues 86-90, 135-143 and 200-203) are altered upon ligand (10-FDDF or THF) binding in the active site. The orientations and geometries of key residues, including Phe89, His106, Arg114, Asp142 and Tyr200, are adjusted for substrate binding and product release during catalysis. Among them, Tyr200 is especially crucial for product release. An additional potential THF binding site is identified in the cavity between two zNt-FDH molecules, which might contribute to the properties of product inhibition and THF storage reported for FDH. Together with mutagenesis studies and activity assays, the structures of zNt-FDH and its complexes provide a coherent picture of the active site and a potential THF binding site of zNt-FDH along with the substrate and product specificity, lending new insights into the molecular mechanism underlying the enzymatic properties of Nt-FDH.


Subject(s)
Oxidoreductases Acting on CH-NH Group Donors/chemistry , Zebrafish/metabolism , Amino Acid Sequence , Animals , Binding Sites , Catalytic Domain , Crystallography, X-Ray , Folic Acid/analogs & derivatives , Formates/metabolism , Hydrolysis , Models, Molecular , Molecular Sequence Data , Oxidoreductases Acting on CH-NH Group Donors/metabolism , Protein Conformation , Protein Structure, Tertiary , Sequence Alignment , Tetrahydrofolates/metabolism
5.
JACS Au ; 4(6): 2130-2150, 2024 Jun 24.
Article in English | MEDLINE | ID: mdl-38938812

ABSTRACT

Monoclonal antibodies (mAbs) have gradually dominated the drug markets for various diseases. Improvement of the therapeutic activities of mAbs has become a critical issue in the pharmaceutical industry. A novel endo-ß-N-acetylglucosaminidase, EndoSz, from Streptococcus equisubsp. zooepidemicus Sz105 is discovered and applied to enhance the activities of mAbs. Our studies demonstrate that the mutant EndoSz-D234M possesses an excellent transglycosylation activity to generate diverse glycoconjugates on mAbs. We prove that EndoSz-D234M can be applied to various marketed therapeutic antibodies and those in development for antibody remodeling. The remodeled homogeneous antibodies (mAb-G2S2) produced by EndoSz-D234M increase the relative ADCC activities by 3-26-fold. We further report the high-resolution crystal structures of EndoSz-D234M in the apo-form at 2.15 Å and the complex form with a bound G2S2-oxazoline intermediate at 2.25 Å. A novel pH-jump method was utilized to obtain the complex structure with a high resolution. The detailed interactions of EndoSz-D234M and the carried G2S2-oxazoline are hence delineated. The oxazoline sits in a hole, named the oxa-hole, which stabilizes the G2S2-oxazoline in transit and catalyzes the further transglycosylation reaction while targeting Asn-GlcNAc (+1) of Fc. In the oxa-hole, the H-bonding network involved with oxazoline dominates the transglycosylation activity. A mobile loop2 (a.a. 152-159) of EndoSz-D234M reshapes the binding grooves for the accommodation of G2S2-oxazoline upon binding, at which Trp154 forms a hydrogen bond with Man (-2). The long loop4 (a.a. 236-248) followed by helix3 is capable of dominating the substrate selectivity of EndoSz-D234M. In addition, the stepwise transglycosylation behavior of EndoSz-D234M is elucidated. Based on the high-resolution structures of the apo-form and the bound form with G2S2-oxazoline as well as a systematic mutagenesis study of the relative transglycosylation activity, the transglycosylation mechanism of EndoSz-D234M is revealed.

6.
Nat Commun ; 14(1): 545, 2023 02 01.
Article in English | MEDLINE | ID: mdl-36726015

ABSTRACT

Understanding the structural diversity of honeybee-infecting viruses is critical to maintain pollinator health and manage the spread of diseases in ecology and agriculture. We determine cryo-EM structures of T = 4 and T = 3 capsids of virus-like particles (VLPs) of Lake Sinai virus (LSV) 2 and delta-N48 LSV1, belonging to tetraviruses, at resolutions of 2.3-2.6 Å in various pH environments. Structural analysis shows that the LSV2 capsid protein (CP) structural features, particularly the protruding domain and C-arm, differ from those of other tetraviruses. The anchor loop on the central ß-barrel domain interacts with the neighboring subunit to stabilize homo-trimeric capsomeres during assembly. Delta-N48 LSV1 CP interacts with ssRNA via the rigid helix α1', α1'-α1 loop, ß-barrel domain, and C-arm. Cryo-EM reconstructions, combined with X-ray crystallographic and small-angle scattering analyses, indicate that pH affects capsid conformations by regulating reversible dynamic particle motions and sizes of LSV2 VLPs. C-arms exist in all LSV2 and delta-N48 LSV1 VLPs across varied pH conditions, indicating that autoproteolysis cleavage is not required for LSV maturation. The observed linear domino-scaffold structures of various lengths, made up of trapezoid-shape capsomeres, provide a basis for icosahedral T = 4 and T = 3 architecture assemblies. These findings advance understanding of honeybee-infecting viruses that can cause Colony Collapse Disorder.


Subject(s)
Capsid Proteins , RNA Viruses , Bees , Animals , Capsid Proteins/metabolism , Capsid/metabolism , Cryoelectron Microscopy , Molecular Conformation , Virus Assembly
7.
J Biol Chem ; 285(5): 3245-52, 2010 Jan 29.
Article in English | MEDLINE | ID: mdl-19948735

ABSTRACT

Tubulointerstitial nephritis is a cardinal renal manifestation of leptospirosis. LipL32, a major lipoprotein and a virulence factor, locates on the outer membrane of the pathogen Leptospira. It evades immune response by recognizing and adhering to extracellular matrix components of the host cell. The crystal structure of Ca(2+)-bound LipL32 was determined at 2.3 A resolution. LipL32 has a novel polyD sequence of seven aspartates that forms a continuous acidic surface patch for Ca(2+) binding. A significant conformational change was observed for the Ca(2+)-bound form of LipL32. Calcium binding to LipL32 was determined by isothermal titration calorimetry. The binding of fibronectin to LipL32 was observed by Stains-all CD and enzyme-linked immunosorbent assay experiments. The interaction between LipL32 and fibronectin might be associated with Ca(2+) binding. Based on the crystal structure of Ca(2+)-bound LipL32 and the Stains-all results, fibronectin probably binds near the polyD region on LipL32. Ca(2+) binding to LipL32 might be important for Leptospira to interact with the extracellular matrix of the host cell.


Subject(s)
Bacterial Outer Membrane Proteins/physiology , Calcium/chemistry , Fibronectins/chemistry , Leptospira/metabolism , Lipoproteins/physiology , Amino Acid Sequence , Bacterial Outer Membrane Proteins/chemistry , Calorimetry/methods , Circular Dichroism/methods , Crystallography, X-Ray/methods , Enzyme-Linked Immunosorbent Assay , Lipoproteins/chemistry , Molecular Sequence Data , Protein Binding , Protein Structure, Secondary , Surface Properties
8.
Sci Rep ; 10(1): 5553, 2020 03 27.
Article in English | MEDLINE | ID: mdl-32221413

ABSTRACT

Most studies focusing on only one directional effect among cognitive health, physical function, and incontinence may miss potential paths. This study aimed to determine the pathway by analyzing the bidirectional effects of exposure (X) on outcome (Y) and explore the mediating effect (M) between X and Y. Secondary data analyses were performed in this study. The original data were collected from August to October 2013 in one VH in Tainan, Taiwan, and the final sample size was 144 older male veterans. Path analysis was performed to test the pathway sequence X → M → Y among the three outcome variables. Approximately 80% of the veterans were aged 81 or older, approximately 42% had a functional disability, 26% had cognitive impairment, and 20% had incontinence. The relationships between functional disability and incontinence and between functional disability and cognition impairment were bidirectional, and functional disability played a key mediating role in the relationship between cognitive impairment and incontinence. Physical more than cognitive training in order to improve or at least stabilize functional performance could be a way to prevent or reduce the process of developing incontinence.


Subject(s)
Cognitive Dysfunction/epidemiology , Disabled Persons/statistics & numerical data , Fecal Incontinence/epidemiology , Homes for the Aged , Institutionalization/statistics & numerical data , Urinary Incontinence/epidemiology , Veterans/statistics & numerical data , Activities of Daily Living , Aged , Causality , Comorbidity , Cross-Sectional Studies , Disabled Persons/psychology , Drug Utilization/statistics & numerical data , Fecal Incontinence/etiology , Geriatric Assessment , Humans , Male , Mental Status and Dementia Tests , Middle Aged , Models, Theoretical , Population Dynamics , Quality of Life , Socioeconomic Factors , Taiwan/epidemiology , Urinary Incontinence/etiology , Veterans/psychology
9.
Acta Crystallogr D Struct Biol ; 76(Pt 2): 147-154, 2020 Feb 01.
Article in English | MEDLINE | ID: mdl-32038045

ABSTRACT

Noncrystallographic symmetry (NCS) averaging following molecular-replacement phasing is generally the major technique used to solve a structure with several molecules in one asymmetric unit, such as a spherical icosahedral viral particle. As an alternative method to NCS averaging, a new approach to optimize or to refine the electron density directly under NCS constraints is proposed. This method has the same effect as the conventional NCS-averaging method but does not include the process of Fourier synthesis to generate the electron density from amplitudes and the corresponding phases. It has great merit for the solution of structures with limited data that are either twinned or incomplete at low resolution. This method was applied to the case of the T = 1 shell-domain subviral particle of Penaeus vannamei nodavirus with data affected by twinning using the REFMAC5 refinement software.


Subject(s)
Models, Molecular , Software , Animals , Crystallography, X-Ray/methods , Penaeidae/virology , Virion/chemistry
10.
ACS Omega ; 5(7): 3428-3443, 2020 Feb 25.
Article in English | MEDLINE | ID: mdl-32118157

ABSTRACT

The protrusion domain (P-domain; MrNVPd) of Macrobrachium rosenbergii nodavirus (MrNV) exists in two conformations, parallel and X-shaped. We have performed a theoretical study to gain insight into the nature of the dimeric interactions involving the dimeric interfaces within parallel and X-shaped conformations of MrNVPd by applying the quantum theory of atoms in molecules (QTAIM) and natural bond orbital (NBO) analyses in the framework of the density functional theory (DFT) approach. The results reveal that the dimer-dimer interfaces of MrNVPd have hydrogen bonds of common types. Leu255-Lys287, Tyr257-Lys287, Lys287-Ser253, Met294-Cys328, Asp295-Lys327, Ser298-Ser324, Ile326-Asp295, and Cys328-Met294 are the key residue pairs of the dimer-dimer interfaces to maintain the dimer-dimer structures of MrNVPd through charge-charge, charge-dipole, dipole-dipole, hydrophobic, and hydrogen bonding interactions. The strengths of these intermolecular dimer-dimer interactions in the parallel conformation are much greater than those in the X-shaped conformation. The parallel trimeric interface is held basically by electrostatic and hydrophobic interactions. The electrostatic interactions accompanying a strong hydrogen bond of Oγ1-Hγ1···Oγ1 in the Thr276 A-Thr276 D pair maintain the intermolecular interface of two X-shaped MrNVPd dimers.

11.
IUCrJ ; 7(Pt 5): 934-948, 2020 Sep 01.
Article in English | MEDLINE | ID: mdl-32939285

ABSTRACT

In Pseudomonas aeruginosa, an important opportunistic pathogen that causes numerous acute and chronic infections, the hybrid two-component system (TCS) regulates the swarming ability and biofilm formation with a multistep phospho-relay, and consists of hybrid-sensor histidine kinase (HK), histidine-containing phospho-transfer protein (Hpt) and response regulator (RR). In this work, two crystal structures of HptB and the receiver domain of HK PA1611 (PA1611REC) of P. aeruginosa have been determined in order to elucidate their interactions for the transfer of the phospho-ryl group. The structure of HptB folds into an elongated four-helix bundle - helices α2, α3, α4 and α5, covered by the short N-terminal helix α1. The imidazole side chain of the conserved active-site histidine residue His57, located near the middle of helix α3, protrudes from the bundle and is exposed to solvent. The structure of PA1611REC possesses a conventional (ß/α)5 topology with five-stranded parallel ß-sheets folded in the central region, surrounded by five α-helices. The divalent Mg2+ ion is located in the negatively charged active-site cleft and interacts with Asp522, Asp565 and Arg567. The HptB-PA1611REC complex is further modeled to analyze the binding surface and interactions between the two proteins. The model shows a shape complementarity between the convex surface of PA1611REC and the kidney-shaped HptB with fewer residues and a different network involved in interactions compared with other TCS complexes, such as SLN1-R1/YPD1 from Saccharomyces cerevisiae and AHK5RD/AHP1 from Arabidopsis thaliana. These structural results provide a better understanding of the TCS in P. aeruginosa and could potentially lead to the discovery of a new treatment for infection.

12.
J Surg Res ; 153(2): 268-73, 2009 May 15.
Article in English | MEDLINE | ID: mdl-18708190

ABSTRACT

OBJECTIVE: Partial face composite tissue allotransplantation was recently achieved in a human subject. However, the side effects of long-term immunosuppression and chronic rejection area still need concerning. This preliminary study investigated the reproducibility of swine hemi-facial transplantation for preclinical studies. MATERIALS AND METHODS: Eleven out-bred miniature swine underwent hemi-facial transplant. The hemi-facial orthotopic transplant consisted of ear cartilage, auricular nerve, parotid gland and lymphoid tissue, muscle with surrounding hemi-facial skin paddle supplied by the carotid artery, and external jugular vein transplanted to recipient swine. Three different experimental designs were studied, as follows: group I (n = 4): autologous hemi-facial transplantation as a normal control; group II (n = 4): hemi-facial allotransplantation without treatment; group III (n = 3): hemi-facial allotransplantation with cyclosporine-A treatment for 4 wk. The transplanted face was observed daily for signs of rejection. Biopsy of donor skin, gland lymphoid tissue, and cartilage were obtained at specified predetermined time (d 7, 14, 28), or at the time of clinically evident rejection. RESULTS: The results indicated the survival of group I following autologous hemi-facial transplant was 100% and indefinite until sacrifice. Group II without treatment as the controls revealed allograft rejection by d 7 to 28. The allograft with short-term cyclosporine-A treatment revealed delayed rejection by d 38 to 49 postoperatively. The histological examination in group I revealed abundant lymphocyte infiltration, especially in lymphoid gland and alloskin at 1 wk and sacrifice. In contrast, the cyclosporine treatment group showed no significant rejection signs in 4 wk posttransplants. These results demonstrated that lymphoid tissue and alloskin are both susceptible to early rejection. CONCLUSION: The experimental results revealed this model is suitable to investigate the new strategies for preclinical facial allotransplantation studies. Monitoring and modulation of early rejection in alloskin and gland lymphoid tissue is a useful strategy to evaluate composite tissue allotransplantation survival.


Subject(s)
Disease Models, Animal , Facial Transplantation , Graft Rejection , Animals , Cyclosporine/pharmacology , Cyclosporine/therapeutic use , Face/pathology , Face/surgery , Graft Rejection/pathology , Graft Rejection/prevention & control , Graft Survival/drug effects , Immunosuppressive Agents/pharmacology , Immunosuppressive Agents/therapeutic use , Swine , Swine, Miniature , Transplantation, Homologous
13.
Commun Biol ; 2: 72, 2019.
Article in English | MEDLINE | ID: mdl-30820467

ABSTRACT

Shrimp nodaviruses, including Penaeus vannamei (PvNV) and Macrobrachium rosenbergii nodaviruses (MrNV), cause white-tail disease in shrimps, with high mortality. The viral capsid structure determines viral assembly and host specificity during infections. Here, we show cryo-EM structures of T = 3 and T = 1 PvNV-like particles (PvNV-LPs), crystal structures of the protrusion-domains (P-domains) of PvNV and MrNV, and the crystal structure of the ∆N-ARM-PvNV shell-domain (S-domain) in T = 1 subviral particles. The capsid protein of PvNV reveals five domains: the P-domain with a new jelly-roll structure forming cuboid-like spikes; the jelly-roll S-domain with two calcium ions; the linker between the S- and P-domains exhibiting new cross and parallel conformations; the N-arm interacting with nucleotides organized along icosahedral two-fold axes; and a disordered region comprising the basic N-terminal arginine-rich motif (N-ARM) interacting with RNA. The N-ARM controls T = 3 and T = 1 assemblies. Increasing the N/C-termini flexibility leads to particle polymorphism. Linker flexibility may influence the dimeric-spike arrangement.


Subject(s)
Capsid Proteins/chemistry , Capsid/metabolism , Nodaviridae/physiology , Palaemonidae/virology , Penaeidae/virology , Virion/metabolism , Amino Acid Sequence , Animals , Capsid/ultrastructure , Capsid Proteins/genetics , Capsid Proteins/metabolism , Cryoelectron Microscopy , Models, Molecular , Nodaviridae/genetics , Nodaviridae/ultrastructure , Protein Domains , Protein Multimerization , Sequence Homology, Amino Acid , Virion/ultrastructure , Virus Assembly
14.
Sci Rep ; 8(1): 14935, 2018 10 08.
Article in English | MEDLINE | ID: mdl-30297797

ABSTRACT

The membrane-embedded quinol:fumarate reductase (QFR) in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain. The electron/proton-transfer pathways in QFRs remain controversial. Here we report the crystal structure of QFR from the anaerobic sulphate-reducing bacterium Desulfovibrio gigas (D. gigas) at 3.6 Å resolution. The structure of the D. gigas QFR is a homo-dimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. This location of the menaquinone-binding site differs from the menaquinol-binding cavity proposed previously for QFR from Wolinella succinogenes. The observed bound menaquinone might serve as an additional redox cofactor to mediate the proton-coupled electron transport across the membrane. Armed with these structural insights, we propose electron/proton-transfer pathways in the quinol reduction of fumarate to succinate in the D. gigas QFR.


Subject(s)
Bacterial Proteins/metabolism , Desulfovibrio gigas/metabolism , Oxidoreductases/metabolism , Bacterial Proteins/chemistry , Crystallography, X-Ray , Desulfovibrio gigas/chemistry , Desulfovibrionaceae Infections/microbiology , Electron Transport , Humans , Models, Molecular , Oxidoreductases/chemistry , Protein Binding , Protein Conformation , Protons , Substrate Specificity , Vitamin K 2/metabolism
15.
J Mol Graph Model ; 78: 61-73, 2017 11.
Article in English | MEDLINE | ID: mdl-29032052

ABSTRACT

Crystal structure of the protrusion domain (P-domain) of the grouper nervous necrosis virus (GNNV) shows the presence of three-fold trimeric protrusions with two asymmetrical calcium cations along the non-crystallographic three-fold axis. The trimeric interaction natures of the interacting residues and the calcium cations with the neighboring residues within the trimeric interface have been studied by the quantum theory of atoms in molecules (QTAIM) and natural bond orbital (NBO) analyses in the framework of the density-functional theory (DFT) approach. The results revealed that residues Leu259, Val274, Trp280, and Gln322 of subunit A, Arg261, Asp275, Ala277, and Gln322 of subunit B, Leu259, Asp260, Arg261, Ala277, Val278, and Leu324 of subunit C are the main residues involved in the trimeric interactions. Charge-dipole, dipole-dipole, and hydrogen bonding interactions make the significant contributions to these trimeric interactions. Among different interacting residues within trimeric interface, residue pair Arg261 B-Leu259C forms the strongest hydrogen bond inside the interface between subunits B and C. It was also found that calcium cations interact with residues Asp273, Val274, and Asp275 of subunits A, B, and C through charge-charge and charge transfer interactions.


Subject(s)
Calcium/chemistry , Molecular Conformation , Orthoreovirus/chemistry , Viral Proteins/chemistry , Amino Acids/chemistry , Cations , Crystallography, X-Ray , Hydrogen Bonding , Models, Molecular , Orthoreovirus/genetics , Quantum Theory
16.
Surg Neurol ; 66(4): 377-80; discussion 380-1, 2006 Oct.
Article in English | MEDLINE | ID: mdl-17015114

ABSTRACT

BACKGROUND: Although the determination of the correct ganglion under direct vision through thoracoscopy by an experienced surgeon is almost unerring, there is still a 4.3% rate of clipping at the unintended level. METHODS: Through the review of the most recent patients (N = 117) with various sympathetic disorders undergoing thoracoscopic sympathetic interruption over different ganglions by clipping, we found that 5 cases were clipped at the unplanned level. The immediate manifestations were the different outcomes between both sides of the face, trunk, and extremities. The postoperative chest radiographs demonstrated the error. RESULTS: All patients received a second operation in which the unintended clip was removed, and a new one was applied to the appropriate ganglion. The results were satisfactory. CONCLUSIONS: Although the authors in this study have the experience of more than 1000 cases of hyperhidrosis, such an error is still inevitable. Luckily, by using the clipping method, the error is detectable and amendable.


Subject(s)
Ganglia, Sympathetic/surgery , Hyperhidrosis/surgery , Postoperative Complications/etiology , Postoperative Complications/prevention & control , Surgical Instruments/standards , Thoracoscopy/methods , Denervation/adverse effects , Denervation/instrumentation , Denervation/methods , Female , Functional Laterality/physiology , Ganglia, Sympathetic/physiopathology , Humans , Hyperhidrosis/etiology , Hyperhidrosis/physiopathology , Male , Postoperative Complications/physiopathology , Reoperation/instrumentation , Reoperation/methods , Reoperation/statistics & numerical data , Retrospective Studies , Surgical Instruments/adverse effects , Surgical Instruments/statistics & numerical data , Thoracic Cavity/anatomy & histology , Thoracic Cavity/surgery , Thoracoscopy/adverse effects , Thoracoscopy/standards , Treatment Outcome
17.
Ann Biomed Eng ; 44(11): 3384-3397, 2016 Nov.
Article in English | MEDLINE | ID: mdl-27216824

ABSTRACT

Based on plastically compressed cell-seeded collagen gels, we fabricated a small-diameter tubular construct that withstands arterial pressure without prolonged culture in vitro. Specifically, to mimic the microstructure of vascular media, the cell-seeded collagen gel was uniaxially stretched prior to plastic compression to align collagen fibers and hence cells in the gel. The resulting gel sheet was then wrapped around a custom-made multi-layered braided tube to form aligned tubular constructs whereas the gel sheet prepared similarly but without uniaxial stretching formed control constructs. With the braided tube, fluid in the gel construct was further removed by vacuum suction aiming to consolidate the concentric layers of the construct. The construct was finally treated with transglutaminase. Both SEM and histology confirmed the absence of gaps in the wall of the construct. Particularly, cells in the wall of the aligned tubular construct were circumferentially aligned. The enzyme-mediated crosslinking increased burst pressure of both the constructs significantly; the extent of the increase of burst pressure for the aligned tubular construct was greater than that for the control counterpart. Increasing crosslinking left the compliance of the aligned tubular construct unchanged but reduced that of the control construct. Cells remained viable in transglutaminase-treated plastically compressed gels after 6 days in culture. This study demonstrated that by combining stretch-induced fiber alignment, plastic compression, and enzyme-mediated crosslinking, a cell-seeded collagen gel-based tubular construct with potential to be used as vascular media can be made within 3 days.


Subject(s)
Bioprosthesis , Blood Pressure , Blood Vessel Prosthesis , Collagen/chemistry , Models, Cardiovascular , Myocytes, Smooth Muscle/metabolism , Cell Line , Collagen/metabolism , Gels , Humans , Myocytes, Smooth Muscle/cytology , Time Factors
18.
Acta Crystallogr D Struct Biol ; 72(Pt 7): 830-40, 2016 07.
Article in English | MEDLINE | ID: mdl-27377380

ABSTRACT

Molecular averaging, including noncrystallographic symmetry (NCS) averaging, is a powerful method for ab initio phase determination and phase improvement. Applications of the cross-crystal averaging (CCA) method have been shown to be effective for phase improvement after initial phasing by molecular replacement, isomorphous replacement, anomalous dispersion or combinations of these methods. Here, a two-step process for phase determination in the X-ray structural analysis of a new coat protein from a betanodavirus, Grouper nervous necrosis virus, is described in detail. The first step is ab initio structure determination of the T = 3 icosahedral virus-like particle using NCS averaging (NCSA). The second step involves structure determination of the protrusion domain of the viral molecule using cross-crystal averaging. In this method, molecular averaging and solvent flattening constrain the electron density in real space. To quantify these constraints, a new, simple and general indicator, free fraction (ff), is introduced, where ff is defined as the ratio of the volume of the electron density that is freely changed to the total volume of the crystal unit cell. This indicator is useful and effective to evaluate the strengths of both NCSA and CCA. Under the condition that a mask (envelope) covers the target molecule well, an ff value of less than 0.1, as a new rule of thumb, gives sufficient phasing power for the successful construction of new structures.


Subject(s)
Capsid Proteins/chemistry , Crystallography, X-Ray/methods , Nodaviridae/chemistry , Models, Molecular , Protein Conformation , Protein Domains
19.
Hypertens Res ; 28(5): 409-14, 2005 May.
Article in English | MEDLINE | ID: mdl-16156504

ABSTRACT

Poorly controlled hypertension was incidentally cured after performing an endoscopic sympathetic block (ESB) in a patient with hyperhidrosis craniofacialis (HHC). A survey of the literature indicated that 30% to 40% of essential hypertension is of sympathetic origin. Patients with facial sweating associated with hypertension were then studied to determine whether blood pressure is lowered after performing ESB. Between November 2002 and July 2003, 17 hypertensive patients (13 males and 4 females) ranging in age from 22 to 62 years underwent ESB solely for HHC at the Department of Surgery of Kaohsiung Medical University, Taiwan. Their preoperative systolic blood pressure (SBP) values ranged from 170 +/- 6 to 200.7 +/- 7.6 mmHg, and their diastolic blood pressure (DBP) values ranged from 94.7 +/- 6.1 to 120.3 +/- 5.7 mmHg. Their heart rates were between 92.67 +/- 2.28 and 119.67 +/- 5.13 beats per minute (bpm). They were refractory to aggressive medical treatment, including lifestyle modifications and antihypertensive medications. Their postoperative blood pressure, heart rate and surgical outcomes were recorded. After performing ESB, HHC was cured in all 17 patients. Based on the reductions in blood pressure and heart rate, the patients could be divided into two groups, one showing high-level reductions (Group T) and one showing low-level reductions (Group S). The blood pressure of Group T (ten patients) was reduced to the range of 120.2 +/- 6.9 to 131.6 +/- 3.5 mmHg SBP and 74.8 +/- 3.1 to 85.4 +/- 4.5 DBP, and the heart rate of this group was reduced to the range of 65.36 +/- 4.63 to 85 +/- 3.60 bpm, while the blood pressure and heart rate of Group S (seven other patients) were reduced to the ranges of 145.9 +/- 5.7 to 160.5 +/- 5.5 mmHg SBP, 90 +/- 4 to 100.7 +/- 3.2 mmHg DBP, and 80 +/- 4 to 90.83 +/- 3.53 bpm, respectively. The patients in Group S were well controlled at 119.8 +/- 5.5 to 130.6 +/- 8.0 mmHg SBP and 70.1 +/- 3.8 to 84.5 +/- 5.7 mmHg DBP with a daily low-dose of calcium channel blocker. The average follow-up periods of the two groups were 17.00 +/- 2.906 and 17.43 +/- 2.37 months, respectively. We named this surgically curable form of hypertension "Sympathetic Hypertensive Syndrome" (SHS), which we define by the presence of all three of the following: 1) stage II hypertension; 2) HHC or other sympathetic disorders; and 3) heart rate > or = 100 bpm. If the patient is male the reductions of blood pressure after the surgery will be better, which might be due to the link with Y chromosome. Finally, we recommend that ESB should be performed in patients with SHS, although the female would respond less satisfactorily in terms of the blood pressure.


Subject(s)
Autonomic Nervous System Diseases/complications , Autonomic Nervous System Diseases/surgery , Hypertension/etiology , Hypertension/surgery , Sympathectomy , Adult , Blood Pressure , Female , Ganglia, Sympathetic/surgery , Heart Rate , Humans , Hyperhidrosis/etiology , Hyperhidrosis/surgery , Male , Middle Aged , Treatment Outcome
20.
Kaohsiung J Med Sci ; 21(7): 310-3, 2005 Jul.
Article in English | MEDLINE | ID: mdl-16089308

ABSTRACT

Compensatory hyperhidrosis (CH) is the most troublesome side effect after T2 sympathectomy for palmar hyperhidrosis (PH). The aim of this study was to evaluate whether T4 ganglion interruption for PH is an effective approach that can simultaneously minimize the rate of CH. Between July 2001 and July 2003, 84 PH patients undergoing bilateral thoracoscopic T4 sympathectomy were followed up in the outpatient clinic and by telephone questionnaire. Rates of success, regret, CH, recurrence, and complications were recorded. The follow-up period ranged from 18 to 42 months. All excessive hand sweating was stopped. Only two patients had mild CH that did not affect their daily activities. No patients had recurrence or regret. The only other complication was that four patients had postoperative minimal residual pneumothorax, which needed no treatment. All patients were satisfied with the outcome. T4 sympathectomy was an effective method to cure PH. The success rate was 100%. The rate of CH was remarkably low compared with T2 sympathetic ganglionic interruption.


Subject(s)
Hyperhidrosis/surgery , Postoperative Complications/prevention & control , Sympathectomy/methods , Adolescent , Adult , Female , Humans , Male , Sympathectomy/adverse effects
SELECTION OF CITATIONS
SEARCH DETAIL