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Biomedical subjects

A Oohira

Publications and source records attributed to A Oohira.

At least 55 records · Page 3Linked to original sources
PubMed1995

[Incidence of acute idiopathic optic neuritis and its therapy in Japan. Optic Neuritis Treatment Trial Multicenter Cooperative Research Group (ONMRG)].

Data on the incidence of and treatment for acute idiopathic optic neuritis were obtained by questionnaire sent to departments of ophthalmology, university hospitals, and general hospitals throughout Japan. Inquiry was made as to the number of cases which developed idiopathic optic neuritis from April 1992 to March 1993 along with their clinical features. The response rate was 53.6%. There were a total of 550 cases, and the male to female ratio was 1:1.22. Patients 14 to 55 years old were 65.9%; bilateral involvement: 28.2%; recurrence: 18.6%; positive past history of the other eye; 7.5%. Assuming the answering rate to be 100% and two thirds of the patients to be included, annual incidence of this disease (the annual number of patients) was determined to be 1.62 for an adult population of 100,000 (1.03 cases/100,000 people). Tochigi, Tokyo, Kanagawa, Hyogo, Wakayama, Okayama, Yamaguchi, Tottori, Shimane, Ehime, and Fukuoka showed an annual incidence exceeding 2.0/100,000 adults. At more than 95% of all medical institutions questioned, patients with optic neuritis were usually treated with systemic corticosteroids. Oral corticosteroid therapy, which was shown in a recent study in USA to be contraindicated, was still being used at 15% of the institutions.

Acute Disease↗
PubMed1995

Immunohistochemical localization of chondroitin sulfate in the forestomach of the sheep.

The localization of chondroitin sulfate glycosaminoglycans in the forestomach mucosa was examined by use of monoclonal mouse IgMs against chondroitin sulfate (CS-56 and 2H6). Under the light microscope, immunoreactive sites were observed in subepithelial regions and around blood vessels of the rumen, reticulum and omasum. In the reticular papillae and omasal papillae, large areas of core regions also reacted with the monoclonal antibodies. The cell surfaces of fibroblasts in the core region of the epithelium were intensely stained. Under the electron microscope, heavy staining of collagen fibrils beneath the basement membrane of the mucosal epithelium was observed. In addition, products of immunoreactions were localized at the abluminal surfaces of endothelial cells, in pinocytotic vesicles and on pits of the endothelium, as well as surrounding collagen fibrils. At the core regions of reticular papillae and omasal papillae, cell surfaces, interstitial area of collagen fibrils and elastin fibers were stained. Some of the rough endoplasmic reticulum in fibroblasts was also stained. These results suggest that chondroitin sulfate in the forestomach mucosa might serve as a charge barrier in the transport of charged molecules.

Animals↗
PubMed1994

Brain development and multiple molecular species of proteoglycan.

The occurrence of multiple proteoglycan species is a characteristic of the brain. The structural features of individually characterized proteoglycans in the brain are first introduced in brief, then some examples are shown that suggest a relationship between multiple proteoglycans and the many distinct cell types and neural circuits in the brain. Typical experiments demonstrated the neuronal-activity-dependent expression of neural proteoglycans during the critical developmental period of some functional systems such as the visual and vibrissal barrel systems. In addition, the binding properties of neural proteoglycans to other cell surface molecules are discussed in conjunction with their involvement in cell-cell and cell-substratum interactions. This review also covers other potential functions of proteoglycans not only in the development and maintenance of the brain but also in the pathogenesis of Alzheimer's disease. Proteoglycans are really coming of age in neuroscience.

Alzheimer Disease↗
PubMed1994

Immunological identification of two proteoglycan fragments derived from neurocan, a brain-specific chondroitin sulfate proteoglycan.

Neurocan is a brain-unique chondroitin sulfate proteoglycan (CSPG) whose expression and proteolytic cleavage are developmentally regulated. One of the proteolytic products (C-terminal half) is known to be a CSPG with a 150 kDa core glycoprotein (CSPG-150). To identify the N-terminal half of neurocan, we raised an anti-neurocan polyclonal antibody (PAb 291) using a synthetic peptide whose amino acid sequence matched a part of the N-terminal half of neurocan. Western blots showed that PAb 291 recognized two CSPGs, one with a 220 kDa core glycoprotein (CSPG-220, namely neurocan) and one with a 130 kDa core glycoprotein (CSPG-130) isolated from young rat brains. CSPG-130 was co-purified along with CSPG-220 by PAb 291-immunoaffinity column chromatography. The amino acid sequence of the N-terminus of the immunopurified CSPG-130 was exactly the same as the N-terminal sequence of CSPG-220. These results suggest that not only the C-terminal half (CSPG-150) but also the N-terminal half (CSPG-130) of CSPG-220 exists in a CSPG form in rat brain. Using PAb 291 and monoclonal antibody 1G2 (MAb 1G2) which recognizes CSPG-150 in addition to CSPG-220, we found that the contents of CSPG-130 and CSPG-150 in the rat brain reached maximum levels around the time of birth. Both CSPG-130 and 150 were observed, while CSPG-220 was hardly detectable in extracts from the adult rat brain. Immunohistochemical investigation showed that the PAb 291 antigen had a similar distribution pattern to the MAb 1G2 antigen.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1994

Developmentally regulated expression of a brain specific species of chondroitin sulfate proteoglycan, neurocan, identified with a monoclonal antibody IG2 in the rat cerebrum.

The mammalian brain contains many species of proteoglycan. To identify each proteoglycan species, we have raised monoclonal antibodies against soluble chondroitin sulfate proteoglycans purified from 10-day-old rat brains. One monoclonal antibody, named monoclonal antibody 1G2, recognized two proteoglycan species with 220,000 and 150,000 mol. wt core glycoproteins (chondroitin sulfate proteoglycan-220 and chondroitin sulfate proteoglycan-150). Partial amino acid sequences of N-termini of their core proteins coincided with those of neurocan, a brain-unique chondroitin sulfate proteoglycan species, whose complete coding sequence was recently reported [Rauch et al. (1992) J. biol. Chem. 269, 19,536-19,547]. Western blots revealed that chondroitin sulfate proteoglycan-220 became detectable in the rat cerebrum on embryonic day 14, and that it disappeared from the brain around postnatal day 30. In contrast, a fairly large amount of chondroitin sulfate proteoglycan-150 remained in the mature brain. Immunohistochemical studies revealed that 1G2 antigen was first localized in the preplate zone, then both in the marginal zone and in the subplate of the rat cerebrum on embryonic day 16, prior to arrival of the first thalamic afferents at the cortex. On embryonic day 20, immunolabeling with monoclonal antibody 1G2 began to spread from the subplate into the developing cortical plate. On postnatal day 10, the neuropil of the cerebrum, except for the barrel field, was diffusely stained with the antibody, intensely in the hippocampus and superficial layers (I-III) of the cerebral cortex and weakly elsewhere. The barrel hollows were stained very weakly compared with the barrel walls at this stage. The immunoreactivity in the hippocampus and superficial cortical layers was weakened in the mature brain, so that no particular staining pattern, but weak and diffuse staining was observed in the adult rat cerebrum. The 1G2 antigen was immunohistochemically associated largely with glial fibrillary acidic protein-positive cells in primary cultures of the neonatal rat cerebrum. Both chondroitin sulfate proteoglycan-220 and chondroitin sulfate proteoglycan-150 were detected in the conditioned media not only of highly enriched cultures of fetal rat cortical neurons but also of pure cultures of mature astrocytes; more (12- to 20-fold) in the astrocyte conditioned media. Astrocytes, in addition to neurons, may be a cellular source of neurocan in brain at least under certain physiological conditions. The spaciotemporal expression pattern of 1G2 epitope-bearing proteoglycan, or neurocan, suggests that this proteoglycan species plays some roles at least in forming the elongation pathway for early cortical afferent fibers as well as the functional barrel structure in the somatosensory cortex.

Amino Acid Sequence↗
PubMed1994

Cell function during chondrogenesis and osteogenesis induced by bone morphogenetic protein enclosed in diffusion chamber. Biochemical studies on native products derived from outside differentiating cells.

A diffusion chamber containing rabbit bone morphogenetic protein (BMP) was implanted in the abdominal muscle of a Sprague-Dawley rat. Outside of the chamber, cartilage differentiated one to two weeks after implantation, and bone replaced the cartilage three to four weeks after implantation. The interstitial fluid inside the chamber contained only biologic substances produced by cells proliferating and differentiating outside of the chamber. To investigate the cell function during chondrogenesis and osteogenesis, alkaline phosphatase activity and the amounts of S-100 alpha protein, S-100 beta protein, creatine kinase subunits M (CK-M), creatine kinase subunits B (CK-B), hyaluronic acid (HA), and chondroitin sulfate (CS) were measured in the supernatant of interstitial fluid inside the chamber. Alkaline phosphatase activity increased two to four weeks after implantation. The amount of S-100 beta protein acutely increased during the fourth week. The amount of CK-B also increased during the fourth week. The increased levels of HA and CS were also observed after two to four weeks. The examination of such native products may help not only to clarify the mechanisms of cartilage and bone development, but also to develop a sensitive bioassay for BMP.

Alkaline Phosphatase↗
PubMed1993

Core proteins of soluble chondroitin sulfate proteoglycans purified from the rat brain block the cell cycle of PC12D cells.

The effects of soluble chondroitin sulfate proteoglycans (CSPGs) purified from the rat brain on proliferation of and neurite outgrowth from PC12D cells (Katoh-Semba et al., J Neurosci Res 17:36, 1987) were investigated. When PC12D cells are cultured under standard conditions, they proliferate with a doubling time of about 2 days, irrespective of the presence or absence of NGF. However, the addition of a mixture of several types of purified soluble brain CSPG (50 nmol uronic acid/ml) to the culture medium prevented the increase in the number of PC12D cells as well as the nerve growth factor (NGF)-induced neurite extension. The dose for 50% inhibition (ID50) was 1.6 nmol/ml for cell proliferation and 2.7 nmol/ml for neurite elongation. The increase in cell number seemed to stop around 6 h after exposure to culture medium supplemented with brain-derived CSPGs, and even substratum-attached CSPGs were able to exert such inhibitory effects. Only brain-type CSPGs, not a cartilage-derived CSPG (PGH) or a hyaluronate-binding PGH, had such inhibitory effects. Furthermore, these inhibitory activities were associated only with the core proteins of brain-derived CSPGs, and not with polysaccharide chains from brain-derived CSPGs. Incorporation of [3H]thymidine into DNA did not decrease for at least the first 12 h. Consequently, the amount of DNA per cell after 48 h of culture was about twofold higher in cells treated with brain CSPGs than in nontreated cells after exposure to the medium with CSPGs. Microspectrophotometry revealed that the population of cells with a high DNA content was greater in the culture treated with brain-derived CSPGs than in the control culture. These findings indicate that purified soluble brain CSPGs block the cell cycle of PC12D cells at the G2 phase with resultant cessation of cell proliferation and the inhibition of neurite outgrowth.

Aggrecans↗
PubMed1993

Effects of anti-mouse EGF antiserum on prenatal lung development in fetal mice.

To clarify the precise role of epidermal growth factor (EGF) on fetal lung development, rabbit anti-mouse EGF (anti-mEGF) antiserum was administered to pregnant mice from days 10 to 17 during late gestation. Control mice were administered either normal rabbit serum (NRS) or physiological saline (PS). Serum EGF was not detected in fetuses from anti-mEGF antiserum treated mothers, but the level in NRS treated control animals was 4.73 +/- 0.66 ng/mL. One day prior to birth, the fetuses were removed and their body and lung weights were measured. There was no difference between body weights and lung weights of anti-mEGF antiserum treated animals and NRS-treated control animals. On light microscopic morphometry, there was no obvious difference between pulmonary architecture of anti-mEGF antiserum treated animals and NRS treated control animals. On transmission electron microscopy, osmiophillic lamellar inclusion bodies were less prominent in the type II epithelial cells in anti-mEGF antiserum treated animals. Electron microscopic morphometric study revealed that the osmiophillic lamellar inclusion bodies in type II epithelial cells of anti-mEGF antiserum treated animals were fewer in number and had decreased area fraction. These findings support the previous finding that EGF promotes epithelial cell differentiation of the fetal lung without affecting body weight and lung weight.

Animals↗
PubMed1993

Biochemical comparison of brain glycosaminoglycans between normal and reeler mutant mice.

Glycosaminoglycans (GAGs) were isolated from the brains of reeler and normal mice on postnatal days 13 and 20. The GAG content of the reeler mouse brain, based upon the amount of DNA, was about 150% that of the normal mouse brain on both days. The GAGs consisted of chondroitin sulfate (CS), heparan sulfate (HS), hyaluronic acid (HA) and polysialosyl glycopeptides. There was no significant difference in the composition of GAGs isolated from either reeler or normal brain. Repeating disaccharide compositions of CS and HS were also similar in reeler and normal brains. Core proteins of brain chondroitin sulfate proteoglycans (CSPGs), solubilized with phosphate buffered saline, were prepared by digesting purified CSPGs with chondroitinase ABC, and were analyzed by SDS-polyacrylamide slab gel electrophoresis. There was no difference in the composition of core proteins from either reeler or normal brain. These results indicate that, although the GAG content of the reeler mouse brain is higher than the normal, all structural parameters of GAGs/CSPGs so far examined were normal. The rate of synthesis and/or degradation of brain GAGs may be affected in the mutant mouse brain.

Animals↗
PubMed1993

Vergence eye movements facilitated by saccades.

This study was carried out to determine whether the vergence velocity is influenced or not by the richness in visual cues for the perception of depth and by the association of saccade. Vergence eye movements associated with and without saccades were recorded in 4 normal subjects with two CCD cameras in both dark and illuminated rooms. Subjects fixated between the targets, which differed in direction and in depth. The peak vergence velocity was 50 degrees to 90 degrees per second for 10 degrees vergence change and 30 degrees to 70 degrees per second for 5 degrees vergence change. Transient vergence change was found during horizontal or vertical saccade. Even after deleting this transient vergence change, the peak velocity of vergence became faster when it was associated with vertical or horizontal saccade. Trajectories of fixation locus were calculated when the vergence and saccade were required simultaneously. Whether or not the room was rich in visual cues for depth perception seemed to have no effect on vergence velocity. Blinking also speeded up divergence. Most eye movements in daily life are the combination of vergence and saccade, and this vergence facilitation by saccade helps to attain prompt binocular fixation on the new target.

Adult↗
PubMed1993

A case of paraneoplastic retinopathy.

A 62-year-old male had undergone lung lobectomy for adenocarcinoma which was discovered after visual loss from paraneoplastic retinopathy. He had photopsia, decreased visual acuity, ring scotoma, extremely reduced electroretinogram and narrowing of retinal artery. Fluorescein angiography revealed progressive diminution of peripheral retinal blood flow, slow perfusion and staining of venules. The surgical removal of the tumor resulted in slight recovery of visual acuity and decrease of photopsia and photophobia, which recurred after 8 months. He has been under steroid therapy to prevent the progression of the disease for 10 months.

Adenocarcinoma↗
PubMed1993

Microvascular and cellular defects of the periosteum of osteogenesis imperfecta.

Periosteum stripped from fragments of diaphyseal long bones from osteogenesis imperfecta (OI) patients was examined both in vivo and in vitro. The OI periosteum was thickened and characteristic finding was a defective microvascular system. The vascular walls of arterioles and capillaries were thick and the lumina of many of these vessels were narrowed or occluded by hypertrophic endothelial cells and multiplication of smooth muscle cell layers. Circulatory deficiency in the OI periosteum might be regarded as one of the causes of the slender, osteopenic diaphyseal bone characteristic of the disorder. A higher proliferative activity was observed in cultured OI periosteal cells, but the cytoplasmic structure showed increased myelinoid bodies and smooth endoplasmic reticulum and decreased lysosomes and rough endoplasmic reticulum. These findings may be related to the abnormal metabolic activity of OI periosteal cells.

Adolescent↗
PubMed1992

A chondroitin sulfate proteoglycan that is developmentally regulated in the cerebellar mossy fiber system.

It is known that the mammalian brain contains many kinds of proteoglycans, but almost all of them remain to be characterized. In this study, we prepared a monoclonal antibody against a phosphate-buffered saline-soluble brain proteoglycan (MAb 6B4). MAb 6B4 recognized a 600- to 1000-kDa chondroitin sulfate proteoglycan with a 250-kDa core protein (6B4 proteoglycan). The core protein of 6B4 proteoglycan carried the HNK-1 epitope. Immunohistochemical analysis of the adult rat brain indicated that this proteoglycan was expressed on the cell surfaces of a subset of neurons. In the hindbrain, 6B4 proteoglycan was highly expressed on the cerebellar Purkinje cells and Golgi cells, and at particular nuclei including the pontine nuclei and lateral reticular nucleus. Almost all of these nuclei were connected to the cerebellum through the mossy fiber system. A developmental study indicated that the expression of this proteoglycan changed dramatically during the formation of the cerebellar mossy fiber system. The mossy fibers from the pontine nuclei expressed 6B4 proteoglycan transiently from Embryonic Day 20 (E20) to Postnatal Day 30 (P30), during which time the axonal outgrowth and glomerular synapse formation occurred. The Purkinje cells, glomeruli, and Golgi cells began to be stained with MAb 6B4 from P10, P16, and P20, respectively. These expression stages correspond with the onset of their synapse formation. These results suggest that 6B4 proteoglycan is closely involved in the development of the cerebellar mossy fiber system.

Animals↗
PubMed1992

Disconjugate ocular motor adaptation in rhesus monkey.

We report a model for inducing disconjugate, orbital-position dependent, ocular motor adaptation in the rhesus monkey. Animals wore a combination of laterally-displacing prisms placed in front of one eye calling for a discrete change in ocular alignment when the eyes reached particular orbital positions. After wearing the prism combination the animals developed adaptive changes both in static alignment during fixation and in dynamic alignment during eye movements. These changes persisted with only one eye viewing and so became independent of the immediate presence of disparity cues. There were, however, imperfections in the adaptive responses; the changes in the innervation were gradual across the prism edge, not abrupt as required. This finding may reflect inherent limitations in the capability for disconjugate adaptation.

Adaptation, Ocular↗
PubMed1992

Nerve growth factor-induced changes in the structure of sulfated proteoglycans in PC12 pheochromocytoma cells.

Structural changes in proteoglycans (PGs) were examined during the neuritogenesis of PC12 cells induced by nerve growth factor (NGF). (1) A heparan sulfate (HS) PG and a chondroitin sulfate (CS) PG were synthesized by PC12 cells, irrespective of the presence of NGF or the duration of culture. PGs released from PC12 cells into the culture medium were mostly CSPGs. (2) In the absence of NGF, the apparent molecular mass of HSPG prepared from PC12 cells after 3 days of culture was in the range of 90-190 kDa for the intact form (Kav = 0.38 on Sepharose CL-6B), 12 kDa for HS, and 61 kDa for the core protein. In the presence of NGF, these values were 90-190 kDa, 10 kDa, and 51 kDa and 61 kDa, respectively. The intact forms of cell-associated CSPG had apparent molecular mass ranges of 120-150 kDa and 120-190 kDa (Kav = 0.38 and 0.34), with CSs of 15 kDa and 20 kDa in the presence and absence of NGF, respectively. The apparent molecular mass of the core protein of cell-associated CSPG was 92 kDa, irrespective of the presence of NGF. The molecular sizes of cell-associated PGs and their glycosaminoglycans remained unchanged during culture. (3) CSPGs released by PC12 cells into the culture medium were separated into two peaks (I and II) by column chromatography on DEAE-cellulose. The peak II fraction prepared from the medium with NGF after 3 days of culture consisted of CSPG with Kav = 0.22 on Sephacryl S-300 [40-84 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)].(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1992

[Physiological significance of epidermal growth factor in fetal maturation and placental growth in mice].

To elucidate the physiological significance of epidermal growth factor (EGF) in fetal and placental development, the effects of neutralization of circulating EGF by anti-EGF antiserum on fetal and placental development were evaluated in pregnant mice. Abdominally administrated antiserum neutralized EGF in fetal and maternal circulation. Fetal weight was not affected by anti-EGF antiserum, but placental weight was suppressed when antiserum was administrated in the latter half of pregnancy. There was no significant difference between control and antiserum injected mice in the affinity and capacity of EGF receptor in the placenta. The number and volume of lamellar bodies were significantly decreased in antiserum treated mice at Day 10-18 compared to control mice. These results suggest that EGF is involved in placental development, especially in late pregnancy. Furthermore, EGF in the circulation may contribute to enhancing fetal lung maturity rather than fetal growth.

Animals↗
PubMed1991

Core protein of chondroitin sulfate proteoglycan promotes neurite outgrowth from cultured neocortical neurons.

Chondroitin sulfate proteoglycan (CS-PG) was purified from rat brain and examined for its effect on neurite outgrowth in primary cultures of embryonic rat neocortical neurons. Neurite outgrowth was increased in culture wells coated with CS-PG. The core protein and glycosaminoglycan (GAG) prepared from the CS-PG were also examined for neurite-promoting activity. The activity was observed in culture wells coated with the core protein but not with GAG. These results suggest that CS-PG stimulates neurite outgrowth from the cultured neurons via its core protein.

Aggrecans↗