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Biomedical subjects

M Li

Publications and source records attributed to M Li.

At least 865 records · Page 48Linked to original sources
PubMed1996

[Clinical analysis of diagnosis and treatment of 44 cases with intraspinal lipoma].

44 cases of intraspinal lipoma were confirmed by pathologic examination. We excised the lipomas totally or partly. After surgery, 8 cases improved greatly, 19 cases improved, 18 not improved. CT scan and MRI are the key methods for diagnosis of intraspinal lipoma, most of intraspinal lipomas are adherent to the spine and root of nerves tightly and difficult to be dissected. So it's not easy to excise the lipoma entirely. But if we use microsurgery we can get better results.

Adolescent↗
PubMed1996

[Topographic stereoscopic measurements of optic disc in early primary open angle glaucoma].

OBJECTIVE: To search a sensitive parameter for the early diagnosis of primary open angle glaucoma (POAG). METHOD: A system of computerized image analysis was used to acquire images of the optic nerve head of patients with POAG, suspect glaucoma (SG) and of normal persons. Each of these groups contained 31 eyes of 31 cases. The mean relative depths of disc rim and cup at different areas in the optic nerve head were measured. All these patients were followed up for four to six months, and the changes of the mean depths of every sector were compared between each pair of the three groups with statistic analysis. RESULTS: The mean depth of the neural rim and cup of each sector and that of total rim and total cup of POAG and SG patients were all deeper than that of normal controls. The mean depths of neural rim of the superior sector, inferior sector and the total rim area of POAG were deeper than that of SG patients. Compared to their first measurements, the changes of mean depths of neural rim of superior sector and total neural rim area of POAG patients were more prominent than that of normal controls and SG. We also compared the relative depth of the total rim area in the different areas in the optic nerve head with other two dimensional optic disc parameters such as cup/disc ratio, etc. CONCLUSION: Our study suggests that three-dimensional stereoscopic measurement of the surface of optic nerve head and follow-up be of paramount importance in the early diagnosis of POAG patients.

Adult↗
PubMed1996

[The structure and type of neuroglia in human eye lamina cribrosa].

OBJECTIVE: To investigate the morpho-structure of neuroglia in the lamina cribrosa of human eyes, its cell type, physiological characteristics and role in the pathological process of optic nerve damage. METHODS: Histochemical and immunocytochemical staining, and transmission electron microscopic techniques were uses. RESULTS: The neuroglial tissue is distributed in the interspaces between the laminar sheets, on the internal wall of scleral canal and in optic nerve fiber bundles. Its cell is of fibrillary neuroglial astrocyte type. CONCLUSION: The fibrillary neuroglial astrocytes constitute a spatial net-work like architecture within the lamina cribrosa, provide mechanical support for optic nerve fibers as their main function and have higher resistance to pressure insults than optic nerve fibers.

Astrocytes↗
PubMed1996

[24 patients with aneurysm of membranous ventricular septumi: clinical analysis].

24 patients with aneurysm of the membranous ventricular septum were confirmed by operatively in our hospital. Four patients had true aneurysm of the membranous ventricular septum, and 20 false. According to the difference of membranous aneurysm (true or false) and the size of the defect, different methods of the operation were adopted. Postoperation intracardiac residual shunt was avoided. There was no death in the group. Follow-up for 9 years to 6 months showed excellent long-term results. The authors consider that the diagnosis of this disease before operation is difficult.

Adolescent↗
PubMed1996

Signal transduction pathways in guinea pig sperm.

Trifluoperazine (TFP), the antagonist of calmodulin (CaM), significantly stimulated the capacitation and acrosome reaction of guinea pig spermatozoa at the concentration of 10-100 mumol/L, independent of the external Ca2+. Forskolin, dbcAMP and caffeine evidently promoted the occurrence of acrosome reaction of spermatozoa at early capacitation stage (5 h) in nonsynchronous system but not in synchronous system. If the spermatozoa were capacitated for 15 h in synchronous system, the above three drugs significantly stimulated acrosome reaction in a Ca(2+)-independent manner. Protein kinase C activators, i.e. phorbol 12-myristate 13-acetate (PMA) and phorbol 12,13-dibutyrate (PDB) did not influence the occurrence of acrosome reaction of spermatozoa at early capacitation stage, but significantly increased the acrosome reaction rate in capacitated spermatozoa in a Ca(2+)-independent manner. In contrast, PKC inhibitor staurosporine significantly inhibited the occurrence of acrosome reaction.

Acrosome↗
PubMed1995

HNF3 binds and activates the second enhancer, ENII, of hepatitis B virus.

The basic functional unit of hepatitus B virus (HBV) enhancer II (ENII) is located within nt 1687-1774, which is defined as the B fragment in our previous papers. A major trans-acting factor binding site has been identified within the B fragment. The sequence corresponding to this binding site was named B2. In this paper, several point mutations were introduced into the B2 subunit by PCR-mediated site-directed mutagenesis. CAT analysis indicated that the TGTTTGTTT motif within the B2 subunit was critical for the activity of ENII. Mutations of individual nucleotides within this motif could decrease the activity of ENII. Electrophoresis mobility shift assay revealed that the liver-enriched transcription factors hepatocyte nuclear factor (HNF) 3 alpha and HNF3 beta bound to the B2 subunit specifically and the TGTTTGTTT motif was essential for DNA-protein interaction. Anti-HNF3 alpha and anti-HNF3 beta antisera could block such binding ability. Moreover, HNF3 beta could switch on the activity of ENII in HeLa cells and the activity of ENII could be suppressed by antisense HNF3 alpha and antisense HNF3 beta mRNA in HepG2 cells. These results prompted the conclusion that HNF3 was crucial for the liver-specific activity of ENII, which in turn contributed significantly to the liver specificity of HBV.

Base Sequence↗
PubMed1995

Essential function of LIF receptor in motor neurons.

Development and maintenance of the mammalian nervous system is dependent upon neurotrophic cytokines. One class of neurotrophic factor acts through receptor complexes involving the low-affinity leukaemia inhibitory factor receptor subunit (LIF-R). Members of this family of cytokines, such as ciliary neurotrophic factor (CNTF) and leukaemia inhibitory factor (LIF), have profound effects on the survival and maintenance of motor neurons. Recently it was reported that mice lacking LIF-R die shortly after birth unlike mice lacking CNTF or LIF which are viable. Here we describe histopathological analyses of lifr mutants that reveal a loss > 35% of facial motor neurons, 40% of spinal motor neurons and 50% of neurons in the nucleus ambiguus. These findings point to the existence of a ligand for LIF-R that is required for the normal development of motor neurons in both brainstem nuclei and spinal cord.

Animals↗
PubMed1995

Prelabeling of chimeric monoclonal antibody L6 with 90yttrium- and 111indium-1,4,7,10-tetraazacyclododecane-N,N',N",N"'-tetraacetic acid (DOTA) chelates for radioimmunodiagnosis and therapy.

90Y and 111In have been attached to chimeric monoclonal antibody L6 with a bifunctional chelating agent (DOTA-peptide isothiocyanate). The bifunctional chelating agent was prelabeled with either radiometal and then conjugated to the antibody. Studies in human patients showed excellent 111In single-photon emission computed tomography images of breast cancer lesions 24 h after injection.

Animals↗
PubMed1995

In vitro phosphorylation of the polyomavirus major capsid protein VP1 on serine 66 by casein kinase II.

Phosphorylation of the polyomavirus major capsid protein VP1 plays a role in virus assembly and may function in virus-cell recognition. Previous mapping of the in vivo phosphorylation sites on VP1 identified phosphorylation of threonine residues Thr-63 and Thr-156 (Li, M., and Garcea, R. L. (1994) J. Virol. 68, 320-327). Phosphoserine was detected in a tryptic phosphopeptide encompassing residues 58-78. Because of consensus casein kinase II (CK II) sites in this peptide, we examined the in vitro phosphorylation of the purified recombinant VP1 protein by CK II. CK II phosphorylated VP1 on serine, and the resulting tryptic phosphopeptide eluted in a 30-31 min high performance liquid chromatography fraction corresponding to residues 58-78. The VP1 tryptic phosphopeptide also co-migrated in two-dimensional peptide analysis with one of the tryptic peptides obtained from VP1 isolated after in vivo 32P labeling of virus-infected cells. A site-directed mutant VP1 protein, Ser-66 to Ala, was phosphorylated poorly by CK II in vitro. As determined by electron microscopy, all of the mutant proteins were isolated in pentameric form similar to the wild-type protein, although the Ala-66 pentamers had a tendency to self-assemble in vitro into tubular as well as capsid-like structures. These findings identify Ser-66 as a site of VP1 phosphorylation in vitro, and suggest that VP1 may serve as a substrate for CK II in vivo.

3T3 Cells↗
PubMed1995

Assembly of voltage-gated potassium channels. Conserved hydrophilic motifs determine subfamily-specific interactions between the alpha-subunits.

Voltage-gated potassium (K+) channels are assembled by four identical or homologous alpha-subunits to form a tetrameric complex with a central conduction pore for potassium ions. Most of the cloned genes for the alpha-subunits are classified into four subfamilies: Kv1 (Shaker), Kv2 (Shab), Kv3 (Shaw), and Kv4 (Shal). Subfamily-specific assembly of heteromeric K+ channel complexes has been observed in vitro and in vivo, which contributes to the diversity of K+ currents. However, the molecular codes that mediate the subfamily-specific association remain unknown. To understand the molecular basis of the subfamily-specific assembly, we tested the protein-protein interactions of different regions of alpha-subunits. We report here that the cytoplasmic NH2-terminal domains of Kv1, Kv2, Kv3, and Kv4 subfamilies each associate to form homomultimers. Using the yeast two-hybrid system and eight K+ channel genes, two genes (one isolated from rat and one from Drosophila) from each subfamily, we demonstrated that the associations to form heteromultimers by the NH2-terminal domains are strictly subfamily-specific. These subfamily-specific associations suggest a molecular basis for the selective formation of heteromultimeric channels in vivo.

Amino Acid Sequence↗
PubMed1995

The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin.

Domain III of Pseudomonas aeruginosa exotoxin A catalyses the transfer of ADP-ribose from NAD to a modified histidine residue of elongation factor 2 in eukaryotic cells, thus inactivating elongation factor 2. This domain III is inactive in the intact toxin but is active in the isolated form. We report here the 2.5-A crystal structure of this isolated domain crystallized in the presence of NAD and compare it with the corresponding structure in the intact Pseudomonas aeruginosa exotoxin A. We observe a significant conformational difference in the active site region from Arg-458 to Asp-463. Contacts with part of domain II in the intact toxin prevent the adoption of the isolated domain conformation and provide a structural explanation for the observed inactivity. Additional electron density in the active site region corresponds to separate AMP and nicotinamide and indicates that the NAD has been hydrolyzed. The structure has been compared with the catalytic domain of the diphtheria toxin, which was crystallized with ApUp.

ADP Ribose Transferases↗
PubMed1995

Inhibition of alpha-chymotrypsin with an enzyme-activated n-nitrosoamide: active-site labeling by the naphthylmethyl cation.

alpha-Chymotrypsin was irreversibly inhibited with an enzyme-activated N-nitrosamide inhibitor, N-nitroso-N-(1-naphthylmethyl)-N'-isobutyrylalanine; alkylation of the active-site residues by the naphthylmethyl cation produced in the enzymatic reaction occurred. The inhibited enzyme was reduced and aminoethylated and then subjected to tryptic and chymotryptic digestion. Separation of the digest by reversed-phase HPLC revealed one major new peak relative to that of a control run from the native enzyme. Subsequent amino acid analysis and sequencing along with fast atom bombardment-mass spectrometry measurements indicated that this new peak stemmed from an active-site peptide, Met-192-Leu-199, and that the naphthylmethyl label was attached to the side-chain oxygen of Ser-195. The general approach employed can be applied to labeling active sites of a variety of hydrolytic enzymes.

Alanine↗
PubMed1995

Polyomavirus VP1 phosphorylation: coexpression with the VP2 capsid protein modulates VP1 phosphorylation in Sf9 insect cells.

The polyomavirus virion has an outer capsid comprised of 72 pentamers of the VP1 protein associated with the minor virion proteins, VP2 and VP3, and the viral minichromosome. To investigate the interaction between VP1 and VP2/VP3, we mapped VP1 phosphorylation sites and assayed VP1 recognition by anti-peptide antibodies after coexpression of VP1 with VP2 or VP3 by using recombinant baculovirus vectors. VP1, expressed either alone or with VP3, was phosphorylated on serine residues, which are not modified during polyomavirus infection of mouse cells. When VP1 was coexpressed with VP2, the nonphysiologic serine phosphorylation of VP1 was decreased, and a tryptic peptide containing Thr-63, a site modified during virus infection of mouse cells, was phosphorylated. An anti-peptide antibody directed against the VP1 BC loop domain containing Thr-63 recognized VP1 expressed alone but not VP1 coexpressed with VP2 or VP3. The change in phosphorylation resulting from coexpression of two structural proteins identifies the potential of the baculovirus system for studying protein-protein interactions and defines a functional role for the VP1-VP2 interaction.

Amino Acid Sequence↗
PubMed1995

Phosphorylation of eukaryotic protein synthesis initiation factor 4E by insulin-stimulated protamine kinase.

Insulin-stimulated protamine kinase (cPK) and protein kinase C (PKC) phosphorylated eukaryotic protein synthesis initiation factor 4E (eIF-4E) on serine and threonine residues located on an identical tryptic fragment as judged by two-dimensional phosphopeptide mapping. With cPK and PKC, the apparent Km for eIF-4E was about 1.2 and 50 microM, respectively. Relative to recombinant human eIF-4E, cPK exhibited about 100% and < or = 5% activity with eIF-4ES209A and eIF-4ET210A, respectively, and eIF-4ES209A was phosphorylated exclusively on threonines. Bovine kidney eIF-4E enhanced up to 1.8-fold globin synthesis in m7GTP-Sepharose-treated reticulocyte lysates. In contrast, following incubation with cPK, these eIF-4E preparations stimulated globin synthesis up to 6-fold. Compared to the dephosphorylation of the cPK-modified serine on eIF-4E, reticulocyte lysates and highly purified protein phosphatase 2A exhibited marked preference for the cPK-modified threonine. The results indicate that cPK phosphorylates eIF-4E on Ser209 and Thr210, that the hydroxyl group or phosphorylation of Thr210 is necessary for cPK to act on Ser209, and that Ser209 phosphorylation activates reticulocyte globin synthesis. The results suggest that cPK could contribute to the insulin-stimulated phosphorylation of eIF-4E, but that protein phosphatase 2A may confer the site specificity of this response.

Animals↗
PubMed1995

Photoaffinity labelling of cyanomethaemoglobin with derivatives of tryptophan and 5-bromotryptophan.

Tryptophan and 5-bromotryptophan (5-BrTrp) are relatively potent inhibitors of sickle-haemoglobin polymerization. The binding sites of these compounds to normal and sickle haemoglobin (HBA and HBS) have been suggested, but not firmly established, through the use of spin-labelled derivatives and/or computer modeling. In the present study we approached the problem by utilizing the technique of photoaffinity labelling. The cyanomet forms of HBA and HBS were subjected to photoaffinity labelling with N alpha-(4-azidotetrafluorobenzoyl)tryptophan and N alpha-(1-ethyl-2-diazomalonyl)-5-bromotryptophan respectively. Both irradiated samples of HBA and HBS were denatured, digested with trypsin, and then separated by reversed-phase HPLC. A labelled tryptic peptide was isolated from the photolabelling of HBS with N alpha-(1-ethyl-2-diazomalonyl)-5-bromotryptophan. The peptide was identified to be Val1(alpha)-Lys7(alpha), with the label attached to Val1(alpha), by virtue of amino acid analysis and sequencing, in conjunction with fast-atom-bombardment MS. The binding mode of N alpha-(1-ethyl-2-diazomalonyl)-5-bromotryptophan is proposed and its relevance to the potency of the 5-BrTrp-based anti-sickling agents is discussed.

Affinity Labels↗