PubMed Health⌕ Search

Biomedical subjects

A Ooshima

Publications and source records attributed to A Ooshima.

At least 91 records · Page 5Linked to original sources

Analysis of lymphocyte subsets in a renal allograft recipient infected with human immunodeficiency virus.

OBJECTIVE: To study the change in lymphocyte subsets of a renal allograft recipient who acquired human immunodeficiency virus (HIV) infection. PATIENT AND METHODS: A 53-year-old Japanese man who acquired HIV infection at the time of renal transplantation and died from opportunistic infection 3 years later was studied. Lymphocyte subsets were examined serially throughout his clinical course. RESULTS: The numbers of CD4 positive cells were severely decreased but those of CD8 positive cells were stable; the CD 4/8 ratio was extremely low. The numbers of B cells were also decreased but production of immunoglobulin was increased. In spite of this immunosuppressive state, graft rejection was noted when the patient's immunosuppressive medication was reduced. CONCLUSION: The lymphocyte subsets of renal transplant patients with HIV infection should be closely observed, as should the nature and timing of opportunistic infection in relation to transplantation, and the administration of immunosuppressive medication.

AIDS-Related Opportunistic Infections↗

Nodular glomerulosclerosis of unknown origin associated with the nephrotic syndrome.

A 35-year-old male patient clinically characterized by massive proteinuria and hypertension without evidence of systemic diseases is reported. Histological investigation of renal biopsy specimens revealed extensive nodular formations in the mesangial areas in every glomerulus. Light-microscopic examination did not allow discrimination between the glomerular changes found in these specimens and the nodular glomerulosclerosis described in patients with diabetes mellitus. Electron-microscopic examination confirmed the presence of massive, nodular, mesangial expansions consisting of finely fibrillar substances without electron-dense deposits and circumferential mesangial interposition. Immunofluorescent examination showed deposition of IgG, C3, fibrinogen and kappa and lambda light chains in mesangial areas, peripheral capillary loops and a part of the nodules. Furthermore, collagen types IV, V, VI and laminin were detected in the nodules. Amyloid was not observed in these nodules. This diagnosis has not been made, and the mechanism of this nodular glomerulosclerosis remains unknown.

Adult↗

Immunohistochemical distribution of type I, II and III collagens in the rabbit supraspinatus tendon insertion.

The collagen fibres in the area of attachment of the supraspinatus tendon to bone were studied immunohistochemically in 12 mature female New Zealand white rabbits. The labelling of type I collagen was uniformly prominent in the bone as well as in the fascicles of the tendon proper but inconspicuously scattered in the unmineralised and mineralised zones of the fibrocartilage. Type II collagen, not detected in the tendon proper, was widespread in both zones of the fibrocartilage. Type III collagen, on the other hand, appeared to be confined mainly to the zone of unmineralised fibrocartilage, in addition to its presence in the endotenon of the tendon proper. The region of the tidemark failed to show immunostaining for any of the collagen fibre types. In conclusion, this study demonstrates that, although all the principal fibrous collagen types are constituents of the supraspinatus tendon at its attachment site, the distribution pattern of immunolabelling varies from zone to zone.

Animals↗

Increased deposition and serum level of type IV collagen in patients with extrahepatic biliary atresia.

Increased deposition of fibrous connective tissue has been demonstrated in extrahepatic biliary atresia (EHBA). We have focused on type IV collagen, a major component of the perisinusoidal wall of the liver. We attempted to localize tyep IV collagen in liver specimens with monoclonal antibodies. Ultrastructural changes of the liver were observed by electronmicroscopy. Serum amount of type IV collagen was estimated by a recently developed sandwich enzyme immunoassay (EIA) method. Serum laminin and prolyl 4-hydroxylase were also determined by EIA for comparison with type IV collagen. Increased deposition of type IV collagen in the perisinusoidal wall was evident in the area with so-called sinusoidal capillarization. Electronmicroscopy showed a basement membrane structure underlying the endothelial cells in Disse's space. Serum type IV collagen increased in EHBA patients before living-related liver transplantation (LRLT), and returned to normal within 5 weeks after LRLT, except for some patients with postoperative complications. Serum laminin and prolyl 4-hydroxylase showed the same propensity, although less prominently so. It is suggested that the immunoassay of serum type IV collagen adopted in this study has potential application in estimating collagen synthetic activity of the liver and in monitoring the postoperative states of patients after LRLT.

Biliary Atresia↗

Cis-hydroxyproline inhibits adhesion, migration and proliferation of cultured rabbit keratocytes.

Recruitment of keratocytes into injured corneal stroma, and secretion of proteins including collagen in the cells are essential for wound healing of the corneal stroma. We examined the effect of a proline analog, cis-hydroxyproline, on the adhesion, migration and growth of rabbit keratocytes in vitro. This agent decreased the plating efficiency, migration and growth of the keratocytes in a dose-dependent manner. Reduction in these cellular activities may reflect altered functions of pericellular proteins such as collagen. Further studies are needed to determine which specific protein is involved.

Animals↗

Nephrotic syndrome with massive accumulation of type I and type III collagen in the glomeruli.

A 54-year-old woman with nephrotic syndrome underwent renal biopsy. By light microscopy, the glomerular capillary lumen was remarkably narrowed because of diffuse accumulation of Periodic acid Shiff (PAS) positive material along the glomerular capillary wall. By electron microscopy, collagenous fibers were observed in the mesangium and subendothelial area. The fibrous material reacted with antibodies against type I and III collagen but not with those against laminin or type IV collagen by an indirect immunofluorescence technique. This case seemed to be a case of collagenofibrotic glomerulonephropathy.

Collagen↗

Concentration of serum laminin and type IV collagen in liver diseases assayed by a sandwich enzyme-immunoassay using monoclonal antibodies.

Serum laminin (P1 fragment) and type IV collagen levels were determined in patients with hepatic disorders. The method was based on a sandwich enzyme-immunoassay using two monoclonal antibodies that recognize different epitopes of either laminin or type IV collagen molecule. Laminin and type IV collagen levels in the serum of patients with chronic hepatic disorders were higher as compared with those in healthy control subjects, with the increment of serum type IV collagen being far greater than that of laminin. Since type IV collagen and laminin are major basement membrane components, it is suggested that the higher levels of these peptides may reflect a so-called capillarization of the perisinusoidal wall encountered in hepatic fibrogenesis. The assay system used in this experiment is simple and sensitive and can be applied to clinical evaluation of hepatic fibrosis.

Adolescent↗

alpha 1(VIII)-collagen gene transcripts encode a short-chain collagen polypeptide and are expressed by various epithelial, endothelial and mesenchymal cells in newborn mouse tissues.

Type-VIII collagen is a major constituent of Descemet's membrane and contains two genetically distinct alpha chains, alpha 1(VIII) and alpha 2(VIII). We have previously cloned the human alpha 1(VIII) and alpha 2(VIII) genes and determined that they are located on chromosomes 3 and 1, respectively. Comparison of the alpha 1(VIII) and alpha 2(VIII) genes with the alpha 1(X)-collagen gene showed that the structure of the three genes and the sequence of their collagen polypeptides were strikingly similar. Therefore, we have grouped the three genes in a common subclass of collagens which we have named the short-chain collagens because of the relatively small size of their triple-helical domains. In the present study, we have isolated and characterized a mouse gene fragment encoding the entire mouse alpha 1(VIII)-collagen chain and determined the complete primary structure of the polypeptide chain. The size of mouse alpha 1(VIII)-collagen mRNA, as estimated by Northern-blot analysis, was 4.2 kb, compared with 2.8 kb previously reported for the corresponding rabbit mRNA. By cloning and sequencing of four overlapping cDNA, we demonstrate that this larger size of mouse alpha 1(VIII) mRNA is due to a larger 3' untranslated region in the mouse transcript. Using the gene fragment as a probe, we performed Northern-blot hybridization analysis of RNA prepared from newborn mice and demonstrated that alpha 1(VIII) collagen mRNA is expressed at high levels in the calvarium, eye and skin. In situ hybridization revealed that alpha 1(VIII) RNA is present in skin keratinocytes, corneal epithelial and endothelial cells, lens epithelial cells, as well as mesenchymal cells surrounding cartilage and calvarial bone and in the meninges surrounding the brain.

Amino Acid Sequence↗

Extracellular matrix formation in piecemeal necrosis: immunoelectron microscopic study.

Immunolocalization of Type I, Type III and Type IV collagens, laminin and prolyl hydroxylase (PH), a key enzyme in collagen synthesis, was examined to clarify the fibrotic process in chronic, active liver disease. In piecemeal necrosis of chronic, active hepatitis (CAH) and active liver cirrhosis (LC), fat-storing cells (FSCs) and transitional cells (TSCs), containing abundant rough endoplasmic reticulum (RER), were increased in number and stained intensely for PH. Immunodeposits of extracellular matrix (ECM) components were found in the RER, Golgi apparatus (GA) and vesicles of these cells, especially in cases with marked inflammation. On the other hand, in the periportal areas of chronic, persistent hepatitis (CPH) or inactive LC, immunoreaction of ECM components was seldom found in the RER of FSCs and TSCs. In the portal tract, immunodeposits of ECM components were seldom found in the organelles of fibroblasts, although ECM was increased there. These findings indicate that FSCs and TSCs in piecemeal necrosis might play a role in the production of ECM components in the progression of fibrosis during the development of chronic active liver disease. In addition, ECM component production by FSCs and TSCs is associated with marked inflammation.

Collagen↗

L-ascorbic acid 2-phosphate enhances the production of type I and type III collagen peptides in cultured rabbit keratocytes.

We studied the effect of L-ascorbic acid 2-phosphate (P-Asc), a long-acting phosphate derivative of L-ascorbic acid, on the production and secretion of type I and type III collagen peptides in cultured rabbit keratocytes using immunohistochemistry and enzyme immunoassay. P-Asc enhanced production and secretion of these collagen peptides. Our observations support a therapeutic role for P-Asc in the repair of corneal stromal damage such as caused by corneal chemical burn.

Animals↗

Identification of type I collagen-producing cells in human gastrointestinal carcinomas by non-radioactive in situ hybridization and immunoelectron microscopy.

Invasive growth of cancer cells induces desmoplastic reaction as one of the host reactions. It has been a matter of controversy whether stromal collagen is produced by cancer cells or stromal fibroblasts. In the present study, we investigated the cellular origin of Type I collagen in human gastrointestinal carcinomas by in situ hybridization and immunoelectron microscopy. In situ hybridization technique with digoxigenin-labeled RNA probes revealed that spindle-shaped fibroblasts in the stromal area were abundantly positive for transcripts of pro alpha 1(I) collagen in intestinal-type adenocarcinoma. Gland-forming carcinoma cells were negative. In diffuse-type carcinoma of the stomach, spindle-shaped or stellate fibroblasts were positive, whereas dissociated, oval carcinoma cells were negative. A precise determination of cell type was done by immunoelectron microscopy. Intracellular immunoreactivity for Type I collagen was observed in rough endoplasmic reticulum of fibroblasts (including myofibroblasts) in the stromal area. No definite reactivity was obtained in cancer cells by either in situ hybridization or immunoelectron microscopy. Our results indicated that stromal Type I collagen is produced by stromal fibroblasts, which are activated by cancer invasion.

Adenocarcinoma↗

Collagen in dilated cardiomyopathy--scanning electron microscopic and immunohistochemical observations.

The ultrastructural characteristics of collagen and the localization of collagen types were studied in formalin-fixed autopsied human hearts from patients who died in an advanced stage of dilated cardiomyopathy (DCM). The three-dimensional architecture of collagen fibers was studied by scanning electron microscopy by using the cell-maceration method. The localization of collagen type I-VI was demonstrated immunohistochemically using monoclonal antibodies specific to each collagen following the treatment of specimens with trypsin. In the hearts obtained from control subjects without heart disease, there were no significant differences in the ultrastructure and localization of collagens between the fresh and the formalin-fixed hearts. Therefore, formalin-fixation did not affect the ultrastructure of collagen or the immunoreactivity. In DCM, a dense endomysial weave network consisting of fine fibrils was associated predominantly with collagen type I and III, associated moderately with type VI collagen, but less associated with type IV collagen. Perimysial collagen bundles and collagen strands increased both in number and thickness. The outstanding finding was the presence of giant coiled perimysial fibers measuring about 20-30 microns in diameter. The prominent increase in perimysial fibrosis was closely associated with the accumulation of both type I and type III collagen, and associated moderately with type VI collagen. Interestingly, type V collagen increased in the intracellular matrix of the myocardium in DCM. Type II collagen was not present in either normal or diseased hearts. These structural and immunohistochemical characteristics of collagen may provide insights important to assessing the pathogenesis of the cardiac lesion of DCM.

Adult↗

Glucose enhances type IV collagen production in cultured rat glomerular mesangial cells.

Type IV collagen production by cultured glomerular mesangial cells and the effect of glucose on it were evaluated in order to explore the possible contribution of mesangial cells to the accumulation of type IV collagen in mesangial matrix typically seen in diabetes. Type IV collagen was measured quantitatively by enzyme-linked immuno-sorbent assay. The majority of type IV collagen was secreted into culture media and secreted-type IV collagen increased with cell growth in early log phase and decreased in late log phase and after confluency. By exposing the cells to high concentrations of glucose (27.8 mmol/l), both secreted- and cell-associated-type IV collagens increased significantly compared with the cells cultured under normal glucose concentrations (5.6 mmol/l) or under equivalent concentrations of mannitol, resulting in a significant increase in total type IV collagen accumulation from 32.1 +/- 6.4 (under 5.6 mmol/l glucose) to 51.0 +/- 4.6 micrograms/dish (mean +/- SD, n = 4) on day 4, from 113.6 +/- 6.6 to 156.8 +/- 7.1 on day 6, from 248.5 +/- 15.2 to 310.0 +/- 12.6 on day 8 and from 372.4 +/- 14.8 to 507.9 +/- 17.2 on day 12. These results indicate the importance of glucose-induced alteration of mesangial cell function in the development of diabetic mesangial expansion.

Animals↗

Immunohistochemical localization of type I, III, IV, V, and VI collagens and laminin in neurofibroma and neurofibrosarcoma.

By using antibodies to type I, III, IV, V, and VI collagens and laminin, we examined the localization of interstitial collagens and basement membrane components with indirect immunofluorescence and immunoelectron microscopy (IEM). Furthermore, the morphological changes of these collagens in malignant transformation were investigated. In neurofibroma, IEM showed type I, III, and V collagens to be present diffusely on cross-striated collagen fibrils, whereas type VI collagen was present between the fibrils. Type IV collagen and laminin were observed to surround tumor cells. In neurofibrosarcoma, tumor collagen bundles that reacted with antibodies to type I, III, V, and VI collagens were irregularly arranged. Immunofluorescent deposits that reacted with anti-type IV collagen and anti-laminin antibodies were decreased in number, showing a thin and sparse arrangement.

Collagen↗

Ultrastructural localization of type IV collagen and laminin in the Disse space of rat liver with carbon tetrachloride induced fibrosis.

Monospecific antibodies, directed against type IV collagen and laminin, were used to clarify the process of sinusoidal capillarization in rats after carbon tetrachloride (CCl4) intoxication by the direct immunoperoxidase method. After acute intoxication, both type IV collagen and laminin were increased in the area of hepatic necrosis, adjacent to the central veins; however, sinusoidal capillarization was not found. During chronic intoxication, deposition of laminin was co-distributed with that of type IV collagen, but deposition proceeded more slowly than that of the type IV collagen. Deposition of laminin was increased in the Disse space. Sinusoidal capillarization was noted as thick deposition of both antigens by light microscopy. Immunoelectron microscopy showed that both components were continuously present in the Disse space. Intracellularly, both antigens were found in the rough endoplasmic reticulum (RER) of fat-storing cells (FSC) and endothelial cells, and these cells showed morphological changes, becoming slender and flattened. In contrast, few immunoreactive products of the two components were observed in the hepatocytes. These findings suggest that type IV collagen and laminin are indispensable for the establishment of sinusoidal capillarization, and that FSC play an important role in the production of both components.

Animals↗

Release of nerve growth factor from cultured aortic smooth-muscle cells.

Conditioned medium from cultured aortic smooth-muscle cells from rat aorta yielded neurite-extending effects on sensory and sympathetic ganglia of chick embryos. These effects were blocked by adding specific antiserum against 2.5S nerve growth factor (NGF), suggesting that NGF might be released from vascular smooth-muscle cells.

Animals↗

[Effect of L-ascorbic acid 2-phosphate on cultured rabbit keratocytes (the third report). The effect on production and secretion of type I collagen].

We examined the effect of L-ascorbic acid 2-phosphate (P-Asc), a long-acting phosphate derivative of L-ascorbic acid, on intracellular distribution and production of type I collagen in cultured rabbit keratocytes by an immunohistochemistry and enzyme immunoassay. Exposure of 0.1 mM P-Asc for 10 hours decreased a type I collagen immunoreactivity of the cytoplasm as stained in fine granular materials. 0.1 mM P-Asc induced increase of type I collagen level in the medium. The results suggested that 0.1 mM P-Asc might increase the biosynthesis and secretion of type I collagen in keratocytes and have a therapeutic effect on corneal stromal damage.

Animals↗

[A case of primary intrapulmonary benign schwannoma].

A case of primary intrapulmonary schwannoma was described. A 72-year-old man was admitted to our hospital because of dry cough. A chest radiograph showed partial atelectasis of the middle lobe, but computed tomogram of the chest revealed no tumor shadow. Bronchoscopy disclosed a pale-yellow uneven endobronchial wall of the right middle lobe bronchus. Transbronchial biopsy revealed benign schwannoma. Primary intrapulmonary schwannoma has been rarely reported.

Aged↗