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Query: UMLS:C0432222 (SEM)
 47,337 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A comparative polarized light (PLM), scanning (SEM), and transmission (TEM) electron microscopy study was carried out on cross- and longitudinal sections of human lamellar bone in the tibiae of four male subjects aged 9, 23, 45, and 70 years. SEM analysis was also performed on rectangular-prismatic samples in order to observe each lamella sectioned both transversely and longitudinally. The results obtained do not confirm the model hitherto suggested to explain the lamellar appearance of bone. In particular, the classic description by Gebhardt (still accepted by the majority of bone researchers), which suggests that collagen fibers alternate between longitudinal and transversal in successive lamellae, or that they have spiral paths of different pitches, appears to be no longer acceptable in the light of our findings. In fact, SEM and TEM observations here reported agree in demonstrating that lamellar bone is made up of alternating collagen-rich (dense lamellae) and collagen-poor (loose lamellae) layers, all having an interwoven arrangement of fibers. No interlamellar cementing substance was observed between the lamellae, and collagen bundles form a continuum throughout lamellar bone. Preliminary measurements of lamellar thickness indicate that dense lamellae are significantly (P < 0.001) thinner than loose lamellae. Compared with the classic model of Gebhardt, the dense lamellae correspond to the transverse lamellae and are birifringent under PLM, whereas the loose lamellae correspond to the longitudinal lamellae and are extinguished. Collagen-fiber organization in dense and loose lamellae is discussed in terms of bone biomechanics and osteogenesis.
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PMID:A new theory of bone lamellation. 827 80

The purpose of this study is to evaluate the biocompatibility of zirconium compared with titanium by the in vitro study using human osteosarcoma cell line (HOS). Various characteristics of the HOS cells cultured on zirconium (99.9%) and titanium (99.9%) discs were investigated. On the colony formation of the HOS cells, there were no differences between the zirconium and titanium in colony size and number. Good proliferation of the HOS cells was observed on the zirconium as well as on the titanium. Morphological observation of the HOS cells by SEM revealed that the cells on the zirconium as well as on the titanium were flat and polygonal in shape with radial pseudopods. Collagen fibers and calcified substances were observed in the matrix of the HOS cells by TEM on the zirconium as well as on the titanium. The calcium of the HOS cell layer was stained well by Dahl's method. Analysis of the HOS cell layer by the Fourier transform infrared spectroscopy indicated that the HOS cells formed the same matrices including the apatite on the zirconium as on the titanium. Measurements of the zirconium and titanium elution into the human saliva indicated that the elution of zirconium was less than that of titanium. These results suggest that zirconium possesses as excellent biocompatibility as titanium.
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PMID:[In vitro study on biocompatibility of zirconium and titanium]. 848 10

Polyacrylic acid (pAA) was introduced onto Ar-plasma treatment silicone rubber (SR) membrane surfaces by plasma-induced grafted polymerization. Collagen (type III) was also linked with the carboxylic group of pAA grafted onto the SR surface via a carbodiimine agent to obtain a secondary structure of SR. The SR surface properties were characterized by ATR-FTIR, ESCA, contact angle, and SEM. The biocompatibility of the SR surface was evaluated by a culture of cornea epithelial (CE) cells. Subsequently, 75-450 micrograms cm-2 of pAA were obtained on the SR surfaces under different reactive conditions; 3-12 micrograms cm-2 of collagen were linked on modified surfaces of SR. Moreover, ATR-FTIR and ESCA were utilized to confirm the proceedings of these reactions. The hydrophility of the modified SR was measured by a contact angle meter. The values of contact angle for SR grafted with pAA were approximately 45-50 degrees; a 50-55 degrees contact angle on pAA-g-SR to be further linked with collagen was subsequently obtained. Moreover, the influence of surface properties toward migration, growth and attachment of CE cells on the modified surfaces was also examined. Here, untreated SR was used as a control. Experimental results indicated that the number of CE cells attached onto the controlled SR was negligible. The attachment of cells onto pAA-grafted surfaces was clearly observed and peusopoda occurred; however, cell growth was depressed. This depression may have been caused by the acid environment of the pAA-grafted membrane. Nevertheless, both cell attachment and growth onto collagen-linked surfaces were significant. In addition, the morphology of the cells attached onto this surface was considered normal for primary cells. Collagen introduced on the SR surface was not denatured, i.e the natural properties of collagen were maintained. The results obtained in this study will hopefully lead to the successful development of modified SR for clinical applications.
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PMID:Plasma-induced grafted polymerization of acrylic acid and subsequent grafting of collagen onto polymer film as biomaterials. 884 64

Excessive production and deposition of extracellular matrix proteins are characteristic features of diabetic nephropathy. This study tests the hypothesis that cells from diabetic patients who develop nephropathy have a disturbance in collagen metabolism compared with cells from diabetic patients without complications. Kinetics of overall collagen metabolism and total protein synthesis were examined in serially passaged, subconfluent, quiescent skin fibroblasts cultured in either normal (5 mM) or high (25 mM) glucose concentrations from 14 insulin-dependent diabetic (IDDM) patients with nephropathy; 14 IDDM patients without nephropathy matched for age, diabetes duration, and body mass index; and 14 healthy subjects. Fibroblasts were incubated in the presence of 2 microCi/ml [3H]proline, and after labeling the incorporation of [3H]proline into total protein, collagen (collagenase-sensitive material), and noncollagen proteins (collagenase-resistant material) was determined at different time points. Collagen degradation was determined in pulse-chase experiments by following the residual collagen-bound radioactivity after incubation for 8 h with 10 microCi/ml [3H]proline. In high glucose concentrations (25 mM), overall collagen synthesis (measured as [3H]proline incorporation into extracellular and intracellular collagenase-sensitive material) was significantly greater in the patients with nephropathy (mean +/- SEM after a 24-h labeling period: 7189 +/- 671 dpm/10(6) cells) than in the patients without (4341 +/- 267 dpm/10(6) cells; P < 0.01) or healthy control subjects (3836 +/- 234 dpm/10(6) cells; P < 0.01). No significant differences were observed in noncollagen protein production or in collagen degradation rates among the three groups of subjects. In the presence of normal glucose concentrations (5 mM), collagen synthesis was lower in all groups studied, but the differences between IDDM patients with nephropathy and those without remained unaltered. These results suggest that long-term cultured fibroblasts derived from diabetic patients with nephropathy exhibit an abnormality in collagen metabolism. Cells from long-standing diabetic patients without nephropathy have normal collagen metabolism. The increased collagen synthesis is likely to be intrinsic to those diabetic patients susceptible to nephropathy and may play an important role in the sclerotic processes that occur in the kidneys, arteries, and heart.
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PMID:Enhanced collagen synthesis in cultured skin fibroblasts from insulin-dependent diabetic patients with nephropathy. 921 63

Dunkin Hartley guinea pigs develop spontaneous, age-related osteoarthritis (OA) of the knee and other joints. Histologic changes are observed beginning at 3 months of age. Disease severity increases with age, and at 18 months moderate to severe OA is observed. A study was undertaken to assess the morphologic and biochemical changes of 22-month-old animals, and to compare them with values in 2-month-old guinea pigs. Biochemical indices characteristic of OA, from tibial cartilage, indicated an increase in proteoglycan content from 233 +/- 2 micrograms/mg (mean +/- SEM) at 2 months of age to 365 +/- 6 micrograms/mg at 22 months. Collagen concentration in cartilage decreased from 364 +/- 2 micrograms/mg at 2 months to 223 +/- 3 micrograms/mg at 22 months. Proteoglycan fragments found in synovial fluid measured 4.6 +/- 1 micrograms/ml at 2 months and increased to 37 +/- 2 micrograms/ml at 22 months. Radiographic changes observed at 22 months included marginal osteophytes of the tibia and femur, sclerosis of the subchondral bone of the tibial plateau, femoral condyle cysts, and calcification of the collateral ligaments. Histologic evaluation revealed severe OA, with a Mankin score of 10.7 +/- 0.5 in 22-month-old animals. In contrast, 2-month-old animals had no histologic or radiographically detectable lesions. The results of the study reported here indicate that the lesions observed in this model are similar to those of human OA. Spontaneous development of OA in guinea pigs is amenable to the study of the pathogenesis of OA and to the evaluation of potential disease-modifying agents.
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PMID:Spontaneous osteoarthritis in Dunkin Hartley guinea pigs: histologic, radiologic, and biochemical changes. 943 95

We undertook this investigation to assess alterations in shear-mediated platelet function during cardiac surgery and to determine the potential for the PFA-100 to predict post-operative bleeding. Platelet aggregation and PFA-100 closure times were determined in 18 adult patients at five intervals during cardiac surgery. Associations between post-operative bleeding and closure times were examined in an additional 58 patients. Statistical analysis consisted of Student's t, Wilcoxon signed rank, and Spearman correlation tests. All results are reported as mean +/- SEM. Collagen/epinephrine closure times were prolonged prior to and throughout surgery. Collagen/adenosine-5'-diphosphate (ADP) closure times were significantly prolonged by heparin administration, 141 +/- 15 s versus 115 +/- 10 s (P = 0.01), and subsequent initiation of cardiopulmonary bypass (CPB), 203 +/- 12 s (P= 0.0001); however, 15 min after protamine administration, closure times returned to near pre-operative values, 138 +/- 12 s (P = not significant). In contrast, platelet aggregation in response to ADP remained impaired in 17 of 19 patients after CPB. Neither ex vivo correction of sample hematocrits nor supplementation with Humate P affected closure times. Positive and negative predictive values for post-CPB collagen/ADP closure times to predict bleeding were 18 and 96%, respectively. These results suggest that factors both intrinsic and extrinsic to the platelet contribute to reversible shear-mediated platelet dysfunction during CPB, and that the PFA-100 may prove useful after CPB to identify patients unlikely to benefit from platelet transfusions.
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PMID:Reversible shear-mediated platelet dysfunction during cardiac surgery as assessed by the PFA-100 platelet function analyzer. 1199 72

The possible contributions of the angiotensin receptor subtypes 1 (AT1) and 2 (AT2) to angiotensin II-induced changes in collagen secretion and production were studied using the specific angiotensin receptor AT1 and AT2 antagonists telmisartan and P-186. The role of the renin-angiotensin system and its interaction with transforming growth factor-beta 1 (TGF-beta 1) in collagen deposition in cardiac fibroblasts in relation to the development of myocardial fibrosis is also discussed. Cardiac fibroblasts (from normal male adult rats) from passage 2 were cultured to confluency and incubated in the presence of angiotensin II (ANG II) in a concentration range of 10(-10)-10(-6) M in serum-free Dulbecco's MEM medium for 24 h. Collagen production and secretion were assayed by [3H]-proline incorporation and noncollagen production and secretion were also analyzed. ANG II dose-dependently increased collagen secretion and production in rat adult cardiac fibroblasts in culture. Noncollagen secretion and production were also concentration-dependently increased by ANG II. Addition of 100 nmol/l ANG II increased (p < 0.01) collagen secretion and production by 75 +/- 6 (SEM) and 113 +/- 23%, respectively, and noncollagen secretion and production by 65 +/- 6 and 57 +/- 16%, respectively. Pretreatment of cardiac fibroblasts with telmisartan completely blocked the ANG II-induced increase in collagen secretion (p < 0.001) and production (p < 0.05) and in noncollagen secretion (p < 0.01) and production (p < 0.01). P-186 had no effect on the ANG II-induced increase in collagen secretion and production. Addition of telmisartan and P-186 did not affect collagen secretion and production in basal cardiac fibroblasts. TGF-beta 1 also concentration- and time-dependently increased the secretion and production of collagen in cardiac fibroblasts. Our data demonstrate that the effects of ANG II on collagen secretion and production in adult rat cardiac fibroblasts in culture are AT1-receptor mediated since they were abolished by the specific AT1-receptor antagonist telmisartan but not by the specific AT2-receptor antagonist P-186. The ability of ANG II to induce collagen synthesis in cardiac fibroblasts may be mediated by increased TGF-beta 1 production.
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PMID:Induction of cardiac fibrosis by angiotensin II. 1134 91

It has been suggested that orientational changes in the collagen network of articular cartilage account for the depthwise T2 anisotropy of MRI through the magic angle effect. To investigate the relationship between laminar T2 appearance and collagen organization (anisotropy), bovine osteochondral plugs (N = 9) were T2 mapped at 9.4T with cartilage surface normal to the static magnetic field. Collagen fibril arrangement of the same samples was studied with polarized light microscopy, a quantitative technique for probing collagen organization by analyzing its ability to rotate plane polarized light, i.e., birefringence (BF). Depthwise variation of safranin O-stained proteoglycans was monitored with digital densitometry. The spatially varying cartilage T2 followed the architectural arrangement of the collagen fibril network: a linear positive correlation between T2 and the reciprocal of BF was established in each sample, with r = 0.91 +/- 0.02 (mean +/- SEM, N = 9). The current results reveal the close connection between the laminar T2 structure and the collagen architecture in histologic zones.
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PMID:T2 relaxation reveals spatial collagen architecture in articular cartilage: a comparative quantitative MRI and polarized light microscopic study. 1155 Feb 40

Platelets, a major constituent of thrombus, play a crucial role in the pathogenesis of acute ischemic coronary syndromes. The effect of ultraviolet laser emission on platelets within thrombi is unknown. The effects of increasing levels of laser energy on platelets in whole blood were investigated. Blood samples were obtained by aseptic venipuncture and anticoagulated with 3.8% sodium citrate. Samples were exposed to increased levels (0, 30, 45, 60 mJ/mm2; 25 Hz) of ultraviolet excimer laser fluence (308 nm wave-length) and then tested for ADP and collagen induced platelet aggregation, platelet concentration, and for platelet contractile force (PCF) development. Scanning electron microscopy was used to detect laser induced morphologic changes of platelets and by flow cytometric analysis to detect changes in expression of platelet surface antigens p-selectin (CD 62) and glycoprotein IIb/IIIa (CD 43). Exposure to excimer laser energy produced dose dependent suppression of platelet aggregation and force development ("stunned platelets"). ADP aggregation decreased from 8.0+/-1.1 Ohms (mean+/-SEM) to 3.7+/-0.8 Ohms (p<0.001) to 2.7+/-0.6 Ohms (p <0.001) and to 1.8+/-0.5 Ohms (p <0.001) as the laser energy increased from 0 to 30 to 45 to 60 mJ/mm2, respectively. Collagen induced aggregation decreased from 21.4+/-1.4 Ohms to 15.7+/-1.2 Ohms (p <0.001) to 11.7+/-1.1 Ohms (p <0.001) and to 9.9+/-1.0 Ohms (p <0.001), in response to the same incremental range of laser energy. Platelet contractile forces declined from 34,500+/-3700 to 27.800+/-2700 dynes as laser energy increased from 0 to 60 mJ/mm2 (p <0.03). Platelet concentration did not change with increasing laser energy. The expression of platelet surface antigen p-selectin (CD 62) remained stable through increasing levels of laser energy exposures while the percentage of CD 43 positive platelets significantly increased with exposure to laser energy, yet the level of expression did not exceed 0.5% of cells. Thus, aggregation kinetics are altered in platelets exposed to ultraviolet laser energy as manifested by decreased platelet aggregation and reduction in platelet force development capability. The response is dose dependent and most pronounced at higher energy levels such as 60 mJ/mm2.
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PMID:Alterations of platelet aggregation kinetics with ultraviolet laser emission: the "stunned platelet" phenomenon. 1168 28

Cartilage fails by fibrillation and wearing away. This study was designed to identify the microscopic failure processes in the collagen network of bovine cartilage using scanning electron microscopy. Cartilage samples from fibrillated cartilage from the bovine patella were removed from the bone, fixed, digested to remove proteoglycans, freeze-fractured, and processed for SEM. The architecture of the collagen network in the normal cartilage was first defined, and then the failure processes were identified by examining sites of fibrillation and at crack tips. The bovine patellar cartilage was organised with a superficial layer composed of 3-5 lamina, attached to a sub-superficial tissue by angled bridging fibrils. Collagen in the sub-superficial tissue was organised in lamina oriented in the radial direction up to the transition zone. Failure of the system occurred by cracks forming in superficial layer and lamina, creating flaps of lamina that rolled up into the larger 'fronds'. Larger cracks not following the laminar planes occurred in the transition, mid, and deep zones. Failure at the crack tips in the sub-superficial tissue appeared to be by peeling of collagen fibrils, as opposed to breaking of collagen fibrils, suggesting a 'glue' bonding the collagen fibrils in a parallel fashion. Cracks propagated by breaking these bonds. This bond could be a site of disease action, since weakening of the bond would accelerate crack propagation.
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PMID:Collagen architecture and failure processes in bovine patellar cartilage. 1169 9


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