[A case of esophageal and duodenal varices treated with Hassab's procedure and ligation of the duodenal varix].
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Duodenum↗
Biomedical subjects
M Fukasawa
Publications and source records attributed to M Fukasawa.
Tissue distribution of placenta-type 6-phosphofructo- 2-kinase/fructose-2,6-bisphosphatase.
Several isozymes of 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase have been characterized from mammalian tissues and, based on tissue origin, they are classified as liver, skeletal muscle, heart, testis, and placenta isozymes. In this paper, we examined the tissue distribution of placenta-type isozyme in rat tissues at the levels of transcription and translation. Analysis by Northern blotting showed that placenta, brain, testis, liver, kidney, and skeletal muscle expressed mRNA of placenta-type isozyme. Western blot analysis of fractions from POROS-HQ column chromatography of extracts from various rat tissues showed that proteins of placenta-type isozyme are expressed in placenta, brain, testis, liver, spleen, heart and lung, but not in kidney and skeletal muscle. An immunohistochemical study showed that, in liver, placenta-type isozyme is localized in Kupffer cells. These results indicate that isozymes of this particular enzyme may occur in particular cell types within each tissue.
Animals↗
Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in Chinese hamster ovary cells.
LY-A strain is a Chinese hamster ovary cell mutant resistant to sphingomyelin (SM)-directed cytolysin and has a defect in de novo SM synthesis. Metabolic labeling experiments with radioactive serine, sphingosine, and choline showed that LY-A cells were defective in synthesis of SM from these precursors, but not syntheses of ceramide (Cer), glycosphingolipids, or phosphatidylcholine, indicating a specific defect in the conversion of Cer to SM in LY-A cells. In vitro experiments showed that the specific defect of SM formation in LY-A cells was not due to alterations in enzymatic activities responsible for SM synthesis or degradation. When cells were treated with brefeldin A, which causes fusion of the Golgi apparatus with the endoplasmic reticulum (ER), de novo SM synthesis in LY-A cells was restored to the wild-type level. Pulse-chase experiments with a fluorescent Cer analogue, N-(4,4-difluoro-5,7-dimethyl-4-bora-3a, 4a-diaza-s-indacene-3-pentanoyl)-D-erythro-sphingosine (C5-DMB-Cer), revealed that in wild-type cells C5-DMB-Cer was redistributed from intracellular membranes to the Golgi apparatus in an intracellular ATP-dependent manner, and that LY-A cells were defective in the energy-dependent redistribution of C5-DMB-Cer. Under ATP-depleted conditions, conversion of C5-DMB-Cer to C5-DMB-SM and of [3H]sphingosine to [3H]SM in wild-type cells decreased to the levels in LY-A cells, which were not affected by ATP depletion. ER-to-Golgi apparatus trafficking of glycosylphosphatidylinositol-anchored or membrane-spanning proteins in LY-A cells appeared to be normal. These results indicate that the predominant pathway of ER-to-Golgi apparatus trafficking of Cer for de novo SM synthesis is ATP dependent and that this pathway is almost completely impaired in LY-A cells. In addition, the specific defect of SM synthesis in LY-A cells suggests different pathways of Cer transport for glycosphingolipids versus SM synthesis.
Adenosine Triphosphate↗
[Dermoid cyst with thyroid follicle perforated into bladder and ileum: a case report].
A 64-year-old woman was admitted to our hospital on August 19, 1996 with the chief complaint of microscopichematuria. A solid mass was found in her lower abdomen. An abdominal CT scan suggested a large intrapelvic cystic mass and the existence of a fistulous connection between the mass and the small intestine. The existence of a fistula was confirmed by a preoperative barium enema and a cystscopic study. On September 25, 1996, a suprapubic partial cystectomy and total hysterectomy were performed since an intrapelvic abscess was suspected. The cystic mass was observed to adhere to the hollow viscus (uterus, rectum, appendix, ileum and bladder). As a result a part of the ileum and bladder were also removed with the mass. The contents of the cyst included a foul smelling gas and white-green pus. Using a probe, we found two fistulous openings to the ileum and bladder. The histopathological findings indicated a dermoid cyst of the left ovary with thyroid follicles, which are known as "Struma ovarii".
Abscess↗
[Biosynthesis and intracellular trafficking of sphingolipids in mammalian cells].
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Animals↗
[Biosynthesis and intracellular trafficking of ceramide].
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Animals↗
Liposome oligomannose-coated with neoglycolipid, a new candidate for a safe adjuvant for induction of CD8+ cytotoxic T lymphocytes.
The cytotoxic T lymphocyte (CTL) response has recently been shown to play a role in protection against human immunodeficiency virus (HIV) and it is therefore thought that a vaccine against HIV must be able to elicit a CTL response. The development of a safe, effective adjuvant is very important because alum, the only adjuvant available for use in humans at present, can barely induce a response of this type. We demonstrate here that liposomes that contain an immunodominant peptide (15 amino acids) of the envelope glycoprotein gp120 of HIV-1 and that are coated with mannopentaose-dipalmitoylphosphatidylethanolamine conjugate induce a major histocompatibility complex class I-restricted CD8+ CTL response in mice with a single subcutaneous immunization, whereas non-coated liposomes do not. Since no damage to the skin at the injection site was caused by the liposomes, and since the oligomannose-coated liposomes consist of innocuous materials ubiquitously distributed throughout the human body, they may be highly suitable for use as a safe adjuvant in vaccines inducing a CTL response against HIV.
Adjuvants, Immunologic↗
Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase.
Lysenin, a hemolytic protein derived from the earthworm Eisenia foetida, has a high affinity for sphingomyelin. Chinese hamster ovary (CHO) cells exhibited a high cytolytic sensitivity to lysenin, but treatment with sphingomyelinase rendered the cells resistant to lysenin. Temperature-sensitive CHO mutant cells defective in sphingolipid synthesis were resistant to lysenin, and this lysenin resistance was suppressed by metabolic complementation of sphingolipids. Selection of lysenin-resistant variants from mutagenized CHO cells yielded two types of sphingomyelin-deficient mutants, both of which showed less lysenin binding capability than wild-type cells. One mutant strain was severely defective in sphingomyelin synthesis but not glycosphingolipid synthesis, and another strain (designated LY-B) was incapable of de novo synthesis of any sphingolipid species and had no activity of serine palmitoyltransferase (SPT; EC 2.3.1.50) catalyzing the first step of sphingolipid biosynthesis. LY-B cells lacked the LCB1 protein, a component of SPT, and transfection of LY-B cells with the hamster LCB1 cDNA restored both SPT activity and sphingolipid synthesis to the cells. Expression of an affinity peptide-tagged LCB1 protein in LY-B cells caused the endogenous LCB2 protein to adsorb to a tag affinity matrix. In addition, an anti-hamster LCB2 protein antibody co-immunoprecipitated both SPT activity and the wild-type LCB1 protein with the LCB2 protein. Thus, cell surface sphingomyelin is essential for lysenin-induced cytolysis, and lysenin is a useful tool for isolation of sphingomyelin-deficient mutants. Moreover, these results demonstrate that the SPT enzyme comprises both the LCB1 and LCB2 proteins.
Acyltransferases↗
Expression of human placental-type 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase in various cells and cell lines.
The expression of the human placental-type 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (HP2K) in various human cells and cell lines was investigated at the levels of transcription and translation. Analyses by both Northern blotting and a reverse transcription-polymerase chain reaction (RT-PCR) showed that BeWo, U-937, SupT1, H9, HeLa, HepG2, and human mononuclear cells, as well as human placental chorionic cells, expressed HP2K mRNA. All the nucleotide sequences of RT-PCR products from these cell lines were identical to that of HP2K. The expression of HP2K protein was determined by Western blot analysis of fractions from POROS-HQ column chromatography of the cell extracts from U-937 cells, which was used as an example of HP2K-mRNA positive cell lines. As with the 6-phosphofructo-2-kinase activity of HP2K, the activity of 6-phosphofructo-2-kinase in extracts of U-937 cells was not inhibited by glycerol 3-phosphate, a known 6-phosphofructo-2-kinase inhibitor of liver- and testis-type isozymes. These results strongly suggested that various cell lines, in particular U-937 cells, express functional HP2K enzyme. Furthermore, 6-phosphofructo-2-kinase in U-937 cells was found to be activated by treatments with isoproterenol and phorbol 12-myristate 13-acetate, indicating regulation of 6-phosphofructo-2-kinase activity in U-937 cells by protein kinases A and C.
Blotting, Northern↗
cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity.
Chicken aminopeptidase H is a cysteine protease possessing endopeptidase as well as aminopeptidase activity [Rhyu, M. R., Nishimura, T., Kato, Y., Okitani, A. & Kato, H. (1992) Eur. J. Biochem. 208, 53-59]. This enzyme exhibits molecular masses of 400 kDa on gel filtration and 52 kDa on SDS/PAGE, indicating that it consists of eight subunits with the same molecular mass. In the current study, we cloned the cDNA for the catalytic subunit of chicken aminopeptidase H. The open reading frame of the aminopeptidase H gene consists of 1362 base pairs encoding a 52-kDa protein consistent with the molecular mass determined on SDS/PAGE; the deduced amino acid sequence contains all the partial sequences determined for the purified enzyme. The sequence is similar to that of the bleomycin hydrolase of rabbit lung, which has been partially determined. The recombinant 52-kDa protein expressed in COS7 cells exhibited both aminopeptidase and endopeptidase activities, which were inhibited by monoiodoacetic acid. Furthermore, the expression of aminopeptidase H in COS7 cells was also recognized on immunoblotting. This gene is the first one for aminopeptidase H in an animal tissue whose sequence has been completely determined.
Amino Acid Sequence↗
Involvement of heparan sulfate proteoglycans in the binding step for phagocytosis of latex beads by Chinese hamster ovary cells.
Chinese hamster ovary (CHO) K1 cells, typical nonprofessional phagocytes, exhibited intense phagocytosis of latex beads when incubated under serum-free conditions. Under the serum-free conditions, the recognition mechanism of latex beads by cells was investigated. Exogenous heparin and heparan sulfate but not chondroitin sulfate effectively inhibited the binding of latex beads to cells. The binding of latex beads to cells was also inhibited by treatment of cells with heparitinase more effectively than by treatment of cells with chondroitinase. Furthermore, CHO mutant cells defective in biosyntheses of both heparan sulfate and chondroitin sulfate proteoglycans almost completely lacked binding activity of latex beads. Another mutant, which is deficient in heparan sulfate proteoglycans but rather overproduces chondroitin sulfate proteoglycans, also showed lower binding activity, compared with wild-type cells. Coculture of these proteoglycan-less mutants and the wild-type cells did not restore the binding activity of the mutant cells, suggesting that membrane-bound rather than secretory proteoglycans were responsible for the binding of latex beads. These results indicated that heparan sulfate proteoglycans at the cell surface were involved in the binding step for phagocytosis of latex beads by CHO cells.
Animals↗
Characterization of a human placental fructose-6-phosphate, 2-kinase/fructose-2,6-bisphosphatase.
A full-length cDNA, which encodes a human placental fructose-6-phosphate,2-kinase/ fructose-2,6-bisphosphatase, was constructed and expressed in Escherichia coli. The expressed protein, purified to homogeneity, showed a molecular weight of 58,000 by gel electrophoresis under denaturing conditions, compared to the deduced molecular weight of 59,410. The N-terminal sequence of 15 amino acids coincided with that of the deduced sequence. The active enzyme was a dimer as judged by molecular sieve filtration. The expressed enzyme was bifunctional with Vmax values of 142 and 0.2 milliunits/mg for the kinase and phosphatase activities, respectively. The phosphatase activity was extremely low, because one phosphatase active site residue was mutated, and consequently the kinase/phosphatase ratio was the highest among the known isozymes. Furthermore, the enzyme was phosphorylated by cAMP-dependent protein kinase, protein kinase C and also by [2-32P]fructose-2,6-bisphosphate. Phosphorylation by cAMP-dependent protein kinase and protein kinase C increased the maximal Fru-6-P,2-kinase activities by 1.8- and 1.1-fold, respectively. These results suggested that placental fructose-6-phosphate,2-kinase/ fructose-2,6-bisphosphatase is important in maintaining and regulating a relatively high rate of glycolysis in placenta.
Cyclic AMP-Dependent Protein Kinases↗
Replication of feline syncytial virus in feline T-lymphoblastoid cells and induction of apoptosis in the cells.
Feline syncytial virus (FSV) was isolated from feline peripheral blood mononuclear cells of FSV-seropositive cats. When the susceptibility of feline T-lymphocytes to FSV was examined using three strains of FSV, FSV antigens were detected in the FSV-infected T-lymphoblastoid cells. Further, a diversity of biological properties, including replication kinetics and syncytia formation, was noted among the strains, and condensation of chromatin and the fragmentation of cellular DNA were observed in the infected cells. From these data, we conclude that FSV is lymphotropic and can induce apoptosis in the lymphocytes.
Animals↗
[A case of congenital hepatic fibrosis successfully performed by esophageal transection for esophago-gastric varices].
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Adult↗
[A Rastelli operation with a reconstruction of the central pulmonary artery for a pulmonary atresia with an absent left pulmonary artery].
A Rastelli procedure was successfully performed on a 6-year-old girl with an absence of the intrapericardial pulmonary artery and the left pulmonary artery (PA), following a right B-T shunt. The central PA was reconstructed with an 18 mm diameter xenopericardial roll behind the ascending aorta and the superior vena cava. After intracardial repair, the Rastelli operation was performed using an 18 mm diameter composite graft which consisted of a valved xenopericardial roll and a knitted Dacron graft. Since the size of the right PA was large enough to undergo this surgical procedure (the preoperative right PA index was 300 mm2/m2), the postoperative peak systolic pressure ratio of the right ventricle to the left ventricle declined from 1.0 to 0.64. Although the patient showed slight signs of right ventricular failure on the operative day, the postoperative course was uneventful.
Bioprosthesis↗
In vitro immortalization of Old World monkey T lymphocytes with Herpesvirus saimiri: its susceptibility to infection with simian immunodeficiency viruses.
Peripheral blood T lymphocytes of Old World monkeys, rhesus and cynomolgus monkey (Macaca mulatta and Macaca fascicularis, respectively), were successfully immortalized by infection with Herpesvirus saimiri subtype C. The T cell lines were stably cultured without addition of exogenous IL-2. The STP-C488 protein, the oncogene product of subtype C strain 488-77, was detected in these cells by Western blotting. They also expressed some markers of activated or matured T cell phenotypes such as CD2+, monkey Pan-T+, CD25+,CD29+ and MHC-II DR+. Interestingly, not only CD4+CD8- or CD4-CD8+ single positive subpopulations but also CD4+CD8+ double positive ones were present in all of them. Furthermore, they were productively infected with both SIVmac and SIVagm. The levels of the viral replication were comparable to those in human T cell lines. Thus, Herpes Virus Saimiri-immortalized Old World monkey T lymphocytes will be suitable for further studies of immune system in Old World monkeys and cell-virus interactions in SIV infection.
Animals↗
SRB1, a class B scavenger receptor, recognizes both negatively charged liposomes and apoptotic cells.
Scavenger receptors mediate the recognition of a wide range of negatively charged macromolecules such as acetylated low-density lipoproteins (AcLDL). We previously reported the isolation of CHO cell variants expressing a novel type of scavenger receptor, distinct from type I and II macrophage scavenger receptors, that recognize both AcLDL and negatively charged liposomes. In the present study, we found that these isolated CHO cells express class B scavenger receptors (SRB1), which have recently been identified as a new member of the CD36 family of membrane proteins. The isolated CHO cells and CHO transfectants constitutively expressing SRB1 recognized and mediated the endocytosis of cells undergoing apoptosis as well as that of negatively charged liposomes. In contrast, CHO cells constitutively expressing type I or II scavenger receptors were unable to take up these ligands.
Animals↗
Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta.
Two independent cDNA clones encoding fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase were isolated from a human placental cDNA library. The deduced amino acid sequences showed that one of the clones, 2K-1, was almost identical to the rat testis isozyme and the other, 2K-3, was different from any known isozymes expressed in mammalian tissues. The results of Southern blot analysis suggested that clones 2K-1 and 2K-3 were encoded as single copy genes and located in different parts of the genome. Since open reading frames of the cDNA clones were not complete, we obtained the 5'-end of the clone 2K-3 cDNA using the 5'-rapid amplification of cDNA end method. The entire cDNA (HP; 1,756 bp) had a coding capacity of 519 amino acids (M(r) = 59,410), and putative phosphorylation sites for protein kinases A and C on the C terminus. Northern blot analysis using a fragment of the HP as a probe showed that a major band of 5.4 kb, significantly different in size from known isozyme mRNAs such as liver (2.1 kb), muscle (1.9 kb), heart (4.0 kb), and testis (2.0 kb), was present in poly(A)+RNA preparations of human first trimester and term placentae. These results strongly suggested that this 5.4 kb mRNA codes a novel isozyme of fructose 6-phosphate,2-kinase/fructose 2,6-bisphosphatase.
Amino Acid Sequence↗