Biomedical subjects

A Ooshima

Publications and source records attributed to A Ooshima.

At least 73 records · Page 4Linked to original sources

PubMed1995

Extracellular matrix on intraocular lenses.

We examined the distribution of extracellular matrix components in the proteinaceous matrix on explanted IOLs using immunohistochemistry to clarify the nature of proteinaceous deposits on the surfaces of IOLs. We examined 15 polymethylmethacrylate (PMMA) IOLs and one silicone IOL explanted from patients. The IOLs were immunostained for cellular fibronectin, types I and IV collagen, and vitronectin. Various amounts of fibronectin, types I and IV collagen, and vitronectin were detected in the extracellular matrix on all IOLs with cellular deposits. Types I and IV collagen and cellular fibronectin were present in the extracellular matrix and were probably the products of cells adhering to the IOLs. Vitronectin in the fibrous extracellular matrix appeared to represent an adsorption material derived from the aqueous humor. These proteinaceous deposits associated with cellular deposits indicate unsuccessful formation of granulation tissue and could influence IOL biocompatibility.

Adult↗

PubMed1995

The slow progression of hepatic fibrosis in intrahepatic cholestasis as compared with extrahepatic biliary atresia.

It has been shown that the progression of hepatic fibrosis in intrahepatic cholestasis (IHC) is not so prominent as in extrahepatic biliary atresia (EHBA), and that the biosynthetic activity of collagen increases along with the fibrotic disease process. We conducted immunohistochemical and ultrastructural studies on the distribution of collagen types III and IV and of alpha-actinin in the smooth musculature in liver specimens obtained from 4 patients with IHC and 14 patients with EHBA in liver transplantation from living related donors (LRLT). A recently developed sandwich enzyme immunoassay (EIA) was used to determine serum concentrations of type IV collagen, laminin and prolyl 4-hydroxylase (PH) in the patients before and after LRLT. Pathological study showed that the excessive deposition of type IV collagen in the perisinusoidal walls resulted in a clearly developed basal membrane beneath the sinusoidal endothelial cells, so-called sinusoidal capillarization. In the fibrous septa of IHC, fibrogenesis was apparently lower than in EHBA, since collagen deposition and myofibroblast proliferation were not so prominent compared to EHBA. Serum type IV collagen, laminin and PH increased in IHC, although not so markedly as in EHBA, and returned to normal within 5 weeks after successful LRLT. In conclusion, it is suggested that an increased level of serum type IV collagen reflects the de novo synthesis of basal membrane components, and that the determination of their serum levels by EIA can be utilized for the differentiation of the specific fibrogenic activity in each disease, and for monitoring patients before and after liver transplantation.

Actinin↗

PubMed1995

Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney.

Alanine-glyoxylate aminotransferase (AGT) 2 is a pyridoxal 5'-phosphate dependent, mitochondrial enzyme which, in the rat, is expressed at a high level in the kidney. The amino acid sequences of nine tryptic and seven CNBr peptides of the rat kidney AGT2 were determined. Three overlapping cDNAs encoding the AGT2 were cloned on the basis of its partial amino acid sequences by means of a polymerase chain reaction-based approach involving rat kidney poly(A)+ RNA. The complete cDNA sequence comprised 1,919 bases, and contained a 1,536-base open reading frame which encodes a polypeptide of 512 amino acid residues with a putative presequence consisting of 39 amino acid residues at the amino terminus, giving a precursor protein with a molecular mass of 57,150 Da. The sequence of AGT2 exhibits significant homology with neither peroxisomal AGT1 from human liver nor mitochondrial AGT1 from rat liver. However, the sequence of AGT2 exhibited 30.8, 29.2, and 27.1% identity with those of Escherichia coli 4-aminobutyrate aminotransferase, rat ornithine aminotransferase, and Pseudomonas cepacia 2,2-dialkylglycine decarboxylase, respectively. The active site sequences were also well conserved among these aminotransferases. AGT2, thus, is more similar to the other aminotransferases than to AGT1. The results suggest that the rat kidney AGT2 may play a biological role in amino acid metabolism distinct from that of AGT1.

Alanine Transaminase↗

PubMed1995

Human type VI collagen: purification from human subcutaneous fat tissue and an immunohistochemical study of morphea and systemic sclerosis.

Collagen was isolated from human placenta by pepsin digestion and salt precipitation. This collagen was similar in its electrophoretic mobility and immunological reactivity with monoclonal antibody to form B of type VI collagen in the literature (Trueb B, Schreier T, Bruckner P and Winterhalter K. 1987. Eur. J. Biochem. 166: 699-703). We prepared polyclonal rabbit antiserum against alpha 2 chain of type VI collagen and performed an immunohistochemical study using this polyclonal antibody. It reacted in fat tissue and around vessels and peripheral nerves in normal human skin. To confirm the presence of type VI collagen in fat tissue, we isolated collagen from human subcutaneous tissue. This collagen showed a similar pattern in polyacrylamide gel electrophoresis with that from human placenta and cross-reacted with monoclonal or polyclonal antibody against type VI collagen. By immunohistochemical staining, abundant type VI collagen was observed in the septum of subcutaneous fat tissue in morphea or systemic sclerosis. In the mild hyalinizing areas or after treatment with 6M urea or hyaluronidase in highly hyalinized areas, the staining of type VI collagen increased. These data suggest that the amount of type VI collagen in subcutaneous tissue is involved in the early phases of these fibrosing disorders and that type VI collagen accumulates even more in hyalinizing tissue in late phases of these diseases.

Adipose Tissue↗

PubMed1995

Increased expression of lysyl oxidase in skin with scleroderma.

Lysyl oxidase initiates cross-linkage of collagen and elastin by catalysing the formation of a lysine-derived aldehyde. In order to study cross-linking in scleroderma, we used monoclonal antibodies to lysyl oxidase to determine the localization of this enzyme in systemic and localized scleroderma, and compared the distributions obtained with that in normal skin. Using an indirect immunofluorescent antibody method and an avidin-biotinylated enzyme complex method, 11 cases of diffuse type of systemic scleroderma and seven cases of localized scleroderma were studied. In the oedematous stage of systemic scleroderma, intracellular and extracellular lysyl oxidase were remarkably increased in the dermis, particularly in groups around blood vessels. In the sclerotic stage of systemic scleroderma, lysyl oxidase was detected intracellularly in fibroblasts and extracellularly among collagen bundles between the lower dermis and the subcutaneous fat tissue. In localized scleroderma, a marked increase in lysyl oxidase was observed in mononuclear cells and fibroblasts near blood vessels in the lower dermis and in the subcutaneous fat tissue, in addition to the extracellular deposits between collagen bundles. The increase in lysyl oxidase in localized scleroderma was much more common than in the oedematous stage of systemic scleroderma. These findings indicated that intracellular and extracellular expression of lysyl oxidase expression was greater in sclerodermatous skin than in normal skin.

Adolescent↗

PubMed1995

Increased serum levels of type IV collagen and laminin in a patient with a giant retroperitoneal schwannoma.

A 63 year old woman presented with a giant abdominal tumor. Ultrasonography, computerized tomography and drop-infused pyelography revealed a suspected retroperitoneal tumor. The tumor was removed surgically and weighted 2800 g. The pathological diagnosis of the tumor was schwannoma. Strong immunohistochemical staining specific for type IV collagen and laminin was observed in the tumor, and these components were localized in the pericellular region of Schwann cells. The serum levels of these antigens, as determined by radio-immunoassay, were very high before the operation but decreased rapidly thereafter.

Adolescent↗

PubMed1995

A sporadic case of Ehlers-Danlos syndrome type IV: diagnosed by a morphometric study of collagen content.

A sporadic case of a young woman with Ehlers-Danlos syndrome (EDS) type IV is described. Multiple aneurysms of medium-sized arteries were noted. Histological study revealed deposition of acid mucopolysaccharides in the media of major arteries and in the intima of smaller arteries with intimal thickening. Systemic changes related to stenosis were observed in arteries more than 100 microns in diameter. Histologic study revealed hyperplasia of adipocytes in the submucosal layer of the intestines and the trachea, and fibrosis of Langerhans' islets of the pancreas. Typical signs for EDS such as skin hyperelasticity and joint hypermobility, and positive family history were not present. However, type III collagen was not detected on frozen sections from either the skin or the anterior cerebral artery by immunohistochemical quantification. Thus, it was concluded that the present case is a variant of EDS.

Adolescent↗

PubMed1995

Occlusion of the right coronary artery as sequelae of Kawasaki disease: the clinical features of 9 cases.

Among the 302 children with Kawasaki disease (KD) who were evaluated by angiography from 1973 through 1992, 9 (3.0%) had either an occlusion (OC) or segmental stenosis (SS) of the right coronary artery. The interval from the onset of KD to the recognition of OC or SS ranged from 0.5 to 7.7 years (median 4.0 years). Left coronary arterial lesions were also present in 8 of 9 patients. In spite of severe sequelae, children or young adolescents with cardiovascular system-related symptoms were unexpectedly rare. Asymptomatic patients, however, are also at risk of developing myocardial infarction since they have been shown to have a high rate of abnormalities on myocardial scintigraphy. A close observation and careful follow-up are thus considered to be indispensable.

Adolescent↗

PubMed1995

Incidence of structural cardiac disorders in neonates: an evaluation by color Doppler echocardiography and the results of a 1-year follow-up.

Non-biased 502 consecutive neonates were examined by sectorial and color Doppler flow imaging at a mean age of 1.0 day (SD 0.4). Patent foramen ovale was present in 266 (53%) and transient patent ductus arteriosus in 104 (21%). Cardiac disorders were recognized in 19 (3.8%); ventricular septal defect (VSD) in 10; atrial septal defect (ASD) in 4; pulmonary stenosis in 2; aortic stenosis, endocardial cushion defect and tricuspid regurgitation in 1 each. With a spontaneous closure of 8 VSDs and 4 ASDs during the first 12 months, the incidences of cardiac malformation were, consequently, 3.2% at 1 month, 1.4% at 6 months and 1.0% at 12 months.

Birth Weight↗

PubMed1995

Type IV collagen in the basement membrane of the corneal epithelium after alkali burns in guinea pigs.

To investigate the changes in the corneal epithelial basement membrane following an alkali burn, we examined the immunolocalization of type IV collagen and laminin in the eye of the guinea pig burned with alkali. The burn damaged the corneal, limbal and conjunctival epithelium. After regeneration, basement membrane was interrupted, as indicated by laminin immunoreactivity. Type IV collagen immunoreactivity was transiently expressed in the early healing phase in the epithelial derived from both the cornea and conjunctiva, but was not seen in the normal corneal epithelial basement membrane. Later in the healing process, following transdifferentiation of the conjunctival epithelium into a cornea-like epithelium, its type IV collagen immunoreactivity was weaker than that in the basement membrane of the nontransdifferentiated epithelium. Conjunctival transdifferentiation during healing may have led to transient development of type IV collagen immunoreactivity.

Animals↗

PubMed1995

Effect of a prolyl hydroxylase inhibitor on rabbit ocular fibroblasts.

We examined the effect of a prolyl hydroxylase inhibitor, ethyl-3,4-dihydroxybenzoate (E-DHB), on collagen production, proliferation, and spreading by cultured rabbit keratocytes and subconjunctival fibroblasts. Proliferating cells were incubated with or without E-DHB, and were examined by phase-contrast microscopy and proliferation assays. In addition, wounds were made in confluent cultures and were allowed to heal with or without exposure to E-DHB. Confluent cells were also observed by transmission electron microscopy after exposure to E-DHB (0.2-0.4 mM). Finally, confluent cells were incubated in the presence or absence of E-DHB, after which the concentration of soluble collagen in the culture medium was determined. E-DHB (0.2-0.4 mM) inhibited the growth of rabbit keratocytes and subconjunctival fibroblasts and decreased collagen production without inducing cytotoxicity.. Wounds in the control culture were initially healed by individual migrating cells and later by spreading monolayer sheets and proliferating cells, while E-DHB inhibited cell migration into the wound. Electron microscopy revealed large irregular cisternae of endoplasmic reticulum in E-DHB-treated cells, possibly due to protein accumulation. These findings suggest that collagen production may be closely related to various cellular activities.

Animals↗

PubMed1995

Increased expression of matrix metalloproteinase-II in experimental liver fibrosis in rats.

Matrix metalloproteinase-II (MMP-II, 72-kd type IV collagenase, or gelatinase) is one of the gene families of zinc enzymes capable of degrading extracellular matrix molecules, and specifically of degrading type IV and V collagens, gelatin, fibronectin, and elastin. In this study, we used both the liver fibrosis model and the reversibility model of experimental cirrhosis to clarify how MMP-II participates in liver fibrosis of rats. To produce fibrosis model, rats received subcutaneous injections of CCl4 twice weekly for 7, 9, or 14 weeks. For the reversibility model, rats were treated with CCl4 three times a week for 8 weeks and killed at 3, 7, 14, 28, or 42 days after discontinuation of treatment. MMP-II gene expression was studied by Northern hybridization technique, and gelatinase activity of MMP-II was examined by zymography using gelatin substrate. At the same time, an immunohistochemical study using anti-type IV collagen antibody was carried out. In liver fibrosis model, nodule formation was established at 14 weeks. Immunodeposit of type IV collagen was increased in wide fibrous septa and was clearly observed along sinusoidal wall. Gene expression of MMP-II increased up to 7 to 12 times compared with that of controls, with the expression rate being maximum at an intermediate stage of fibrosis. Zymography showed the expressions of both 65-kd latent MMP-II, which is confirmed to be activated by adding p-aminophenylmercuric acetate, and 62-kd active MMP-II during fibrosis. The expression of both forms increased 13 to 28 times as the fibrosis progressed.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1994

Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.

We have isolated overlapping mouse cDNAs encoding a collagenous polypeptide that we have designated alpha 1(XVIII) collagen. Nucleotide sequence analysis shows that alpha 1(XVIII) collagen contains 10 triple-helical domains separated and flanked by non-triple-helical regions. Within the non-triple-helical regions, there are several Ser-Gly-containing sequences that conform to consensus sequences for glycosaminoglycan attachment sites in proteoglycan core proteins. Northern blots show that alpha 1(XVIII) transcripts are present in multiple organs, with the highest levels in liver, lung, and kidney. We have also isolated overlapping cDNAs encoding human alpha 1(XV) collagen, and their sequence extends a published partial alpha 1(XV) sequence to the 3' end. Comparison of the alpha 1(XV) and alpha 1(XVIII) sequences reveals a striking similarity in the lengths of the six most carboxyl-terminal triple-helical domains. In addition, within the carboxyl non-triple-helical domain NC1 of the two chains, a region of 177 amino acid residues shows about 60% identity at the amino acid level. We suggest, therefore, that alpha 1(XV) and alpha 1(XVIII) collagens are structurally related. Their structure is different from that of other known collagen types. We conclude that they belong to a subfamily of extracellular matrix proteins and we suggest the designation multiplexins (for protein with multiple triple-helix domains and interruptions) for members of this subfamily.

Amino Acid Sequence↗

PubMed1994

The human alpha 1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1(XVIII) collagen.

We have cloned and characterized cDNAs encoding the alpha 1 chain of type XV collagen from a human placenta library. Using primer extension cloning we extended the cDNAs to the 5' end of the mRNA and determined the complete deduced primary structure of the human alpha 1(XV) chain. The polypeptide chain contains nine triple helical domains separated by eight non-triple helical regions and flanked by large amino-terminal (555 amino acid residues) and carboxyl-terminal (256 amino acid residues) non-triple helical domains. Comparison of amino acid sequences of the human alpha 1(XV) chain with those of mouse alpha 1(XVIII) collagen showed remarkable similarity within both amino- and carboxyl-terminal non-triple helical domains. Within the carboxyl third of the amino-terminal domain a tandem repeat structure is found with an about 45-amino acid residue sequence repeated four times. This amino acid sequence has a strikingly high similarity to rat cartilage proteoglycan core protein. Northern blot analysis of human embryonic RNA revealed that alpha 1(XV) mRNA is expressed predominantly in internal organs such as the adrenal gland, kidney, and pancreas.

Amino Acid Sequence↗

PubMed1994

Remodelling of microvessels by coronary hypertension or cardiac hypertrophy in rats.

We attempted to clarify the individual effects of coronary hypertension and ventricular pressure-overload on the remodelling of coronary arterial microvessels. We examined structural vascular changes in the right ventricular free walls using two experimental rat models: 12-week ascending aortic banding, i.e. a model of coronary hypertension without ventricular pressure-overload and 12-week pulmonary artery banding, i.e. a model of ventricular pressure-overload without coronary hypertension. In vivo peak systolic left ventricular pressure and left ventricular weight to body weight ratio in the aortic banding model increased to 198 +/- 10 mmHg and by 39% above the controls, respectively. In vivo peak right ventricular pressure and right ventricular weight to body weight ratio in the pulmonary artery banding model increased to 87 +/- 7 mmHg and by 69% above the controls, respectively. The right coronary reserve measured by the Doppler method decreased in both experimental models. Aortic banding increased the medial area and perivascular collagen to lumen area ratios in the microvessels > 30 microns in lumen diameter but not in those < 30 microns. Pulmonary artery banding increased the perivascular collagen to lumen area ratio in the microvessels < 60 microns, but not in those > 60 microns. Medial thickening was not observed over the whole range of lumen diameter. These results suggest that the mechanisms responsible for the remodelling of coronary microvessels differ between non-hypertrophied hearts with coronary hypertension and hypertrophied hearts without coronary hypertension.

Animals↗

PubMed1994

Prolyl hydroxylase inhibitor and lysyl hydroxylase inhibitor inhibit spreading of corneal epithelium.

BACKGROUND: The spreading of epithelium is critical in the healing of corneal wounds. Such epithelial spreading requires the continuous production of protein and glycoprotein. To determine whether collagen production is required for the spreading of corneal epithelium, we studied the effects of inhibitors for collagen production on spreading of corneal epithelium in vitro. METHODS: We examined the effect of two proline analogs, L-azetidine 2-carboxylic acid and cis-hydroxyproline, a prolyl hydroxylase inhibitor, ethyl-3,4-dihydroxybenzoate, and a lysyl hydroxylase inhibitor, minoxidil, on the spreading of epithelium of organ-cultured rabbit cornea. RESULTS: Both analogs and inhibitors inhibited epithelial spreading in a dose-dependent manner. CONCLUSION: These observations indicate that collagen production may be involved in the spreading of corneal epithelium.

Animals↗

PubMed1994

Immunohistochemical demonstration of collagen types III and IV and myofibroblasts in the liver of patients with biliary atresia.

To clarify the pathogenesis of pericholangitis in biliary atresia, immunohistochemical and ultrastructural methods were used to quantify the amount of collagen types III and IV, and alpha-smooth muscle actin-positive myofibroblast present in the pericholangial tissue. Patients were divided into two groups: the early-stage group (n = 7; 15 to 30 days old at the time of the Kasai operation), and the advanced-stage group (n = 14; 8 months to 6 years old at the time of liver transplantation). The liver specimen was harvested at the time of the Kasai operation in the early-stage group, and during liver transplantation in the advanced-stage group. Liver tissue from the donor was used as the control. The specimen was visually inspected and classified into three grades to express the extent of proliferation. An increase of collagen types III and IV, and myofibroblast in the pericholangial area was seen even in 2- to 4-week-old patients, which became marked with the progression of the fibrotic disease process. This suggests that pericholangitis occurs in the very early stage of biliary atresia, perhaps before the development of bile duct obstruction.

Biliary Atresia↗

PubMed1994

Immunohistochemical localization of lysyl oxidase in normal human skin.

Lysyl oxidase (EC 1.4.3.13), a copper-dependent enzyme which catalyses the formation of aldehyde cross-links, and acts primarily on collagen and elastin, is known to be increased during wound healing and in fibrotic disorders including liver cirrhosis and atherosclerosis, and to be decreased in some hereditary connective tissue diseases and in malignant cell lines. A recent study showed that lysyl oxidase might possess tumour suppressor activity as an antioncogene for ras. Little is known about the localization of this enzyme in human skin. In this study, we determined immunohistochemically the localization of lysyl oxidase in normal skin of young and elderly subjects obtained from sun-exposed and unexposed regions of the body. All skin samples tested had similar distributions of lysyl oxidase. The enzyme was present both extracellularly and intracellularly. Extracellularly, a few granular aggregates of immunoreactants were observed along collagen and elastic fibres. These granules were more common in the adventitial portion of the dermis than in the reticular portion. Of all sun-exposed and unexposed regions studied, the skin of the face displayed the greatest amount of extracellular immunoreactants. Immunopositive granules were observed intracellularly in fibroblasts, vascular endothelial cells, sweat glands, sebaceous glands, arrector pili muscles and some keratinocytes. These findings provide evidence that, as suggested in recent reports, lysyl oxidase may have a variety of intracellular functions.

Adolescent↗