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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In vitro protein synthesis of ribosomes extracted from leg muscles of 20 Sprague-Dawley rats denervated 3 and 14 days (high sciatic transections) and 10 control rats was studied. The concentration/mg protein of total ribosomes extracted from the 14-day denervated muscle showed a significant increase. Distribution of muscle polyribosomes on sucrose density gradients was normal in all cases. Noncollagen protein synthesis of the heavy polyribosomes from both early and late denervated muscles showed a significant decrease. SDS polyacrylamide gels suggested that this decrease affected the synthesis of heavy chains of myosin, while the light chains of myosin, actin and tropomyosin had normal structure and amounts. Collagen synthesis of heavy polyribosomes showed slight to moderate increase in only 50 per cent of the cases. Supplementation of ribosomes extracted from denervated muscles with normal muscle soluble enzymes increased their noncollagen synthesis by 66 per cent. This suggests that the neurogenic control of ribosomal protein synthesis is accomplished by hormonal trophic substances contained in the muscle soluble enzymes.
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PMID:Neurogenic control of muscle ribosomal protein synthesis. 121 57

Pulp cells from human permanent molars were isolated and established in culture; 40% showed positive alkaline phosphatase staining. When incubated with 50 micrograms/ml of ascorbic acid and 10 mM of beta-glycerophosphate, the cells formed a mineralized extracellular matrix; they could thus have the potential to differentiate into odontoblast-like cells in vitro. Collagen synthesis was analysed by SDS interrupted gel electrophoresis, Northern blot and slot blot: the cells produced predominantly (approximately 99%) type I collagen and only trace amount of type III collagen. The ratio of alpha 1 (I) to alpha 2(I) procollagen chains was about 68:32, indicating that no significant amount of collagen type I trimer was synthesized in this system. The ratios of alpha 1(I), alpha 2(I) and alpha 1(III) procollagen mRNAs were about 61:25:1; these were compatible with the ratios of corresponding procollagen alpha chains. In addition, a novel 5.8 kb pro alpha 1(III) mRNA was detected. These observations indicate that collagen synthesis in these cultured pulp cells was regulated at the transcriptional level.
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PMID:Collagen gene expression in human dental pulp cell cultures. 128 29

Interstitial renal fibrosis and gingival hypertrophy are frequent side-effects of cyclosporin A which have been attributed to a dysfunction of extracellular matrix synthesis. Endothelial cells might participate in the matrix accumulation observed. We studied the effects of increasing concentrations of cyclosporin A on protein synthesis by human umbilical vein endothelial cells. Collagen synthesis decreased significantly to 800 ng/ml in both medium and cell layer. The percentage of hydroxylation of its proline residues decreased significantly as from 400 ng/ml. The main proteins, analysed by SDS-PAGE, were thrombospondin, fibronectin and the alpha 1 and alpha 2 chains of type IV collagen. These fractions did not show any change after 24 hours exposure to 200 ng/ml of cyclosporin A. These results demonstrate an inhibitory effect of cyclosporin A on collagen synthesis by human umbilical vein endothelial cells. Consequently, matrix accumulation by increased collagen synthesis in cyclosporin A treated patient may not be directly related to the drug effect on endothelial cells.
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PMID:[Synthesis of collagen in culture of endothelial cells of the human umbilical vein. Effects of cyclosporine A]. 129 48

Collagen degradation is thought to be an integral part of the healing sequence of intestinal anastomoses, but almost nothing is known about the enzyme activities involved. We have studied collagenolytic activities, extracted from 1 day-old intestinal anastomoses in the rat. Using either soluble type I collagen or fibrillar type I or type III collagen as a substrate, activities measured in extracts from anastomotic segments were compared to those in extracts from uninjured intestine, removed at operation: in all cases, the collagenolytic activity in anastomotic extracts was significantly higher. This increase was significantly more pronounced in large bowel than in small bowel. The activities were strongly inhibited by serum and metallo-chelating compounds. Analysis, by means of SDS-polyacrylamide gel electrophoresis, of the reaction products of the degradation of fibrillar type I collagen by the extracts revealed the presence of a multitude of fragments, amongst them TcA fragments characteristic for the activity of mammalian collagenase. Thus, the degradative capacity towards various collagen substrates is enhanced in the anastomotic area during the first postoperative period and a true mammalian collagenase is one of the enzymes present.
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PMID:Collagenolytic activity in experimental intestinal anastomoses. Differences between small and large bowel and evidence for the presence of collagenase. 131 43

Collagen is the most important component of the extracellular matrix of the myocardium; it supports the myocytes and maintains the architecture of the heart. Collagen also participates in the myocardial response to various forms of pressure overload. Increased tissue collagen content occurs as a result of spontaneous or experimental overload-induced myocardial hypertrophy. In order to determine the mechanisms responsible for the increased collagen deposition in experimental cardiac hypertrophy, we established monolayer cultures of fibroblasts isolated from normal adult rat myocardium and studied their growth and biosynthetic characteristics. These cells have a doubling time of about 20h and synthesize and secrete several collagenous and non-collagenous proteins. We found that type I collagen was the major collagenous product of these cells representing 80% of total newly synthesized collagen. Most of the newly synthesized collagen was secreted into the culture medium as intact and partially cleaved procollagens. About 20% of the total collagen synthesized was type III collagen which was also secreted into the medium as a procollagen. A small proportion of type V collagen (less than 5%) was also synthesized by these cultures. Fibronectin which was identified by its mobility in SDS gel electrophoresis was quantified by immunoprecipitation with specific antisera and was the most abundant non-collagenous protein synthesized by these cells. Northern blot hybridization analysis demonstrated that these cells expressed transcripts for alpha 1 chains of types I and III collagen and for fibronectin.
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PMID:Growth properties and biochemical characterization of collagens synthesized by adult rat heart fibroblasts in culture. 140 9

Selection of ideal laser parameters for tissue welding is inhibited by poor understanding of the mechanism. We investigated structural changes in collagen molecules extracted from rat tail tendon (> 90% type I collagen) after tissue welding using an 808 nm diode laser and indocyanine green dye applied to the weld site. Mobility patterns on SDS-PAGE were identical in the lasered and untreated tendon extracts with urea or acetic acid. Pepsin incubation after acetic acid extraction revealed a reduction of collagen alpha and beta bands in lasered compared with untreated specimens. Circular dichroism studies of rat tail tendon showed absence of helical structure in collagen from lasered tendon. No evidence for covalent bonding was present in laser-treated tissues. Collagen molecules are denatured by the laser wavelength and parameters used in this study. No significant amount of helical structure is regenerated on cooling. We conclude that non-covalent interactions between denatured collagen molecules may be responsible for the creation of tissue welding.
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PMID:Changes in type I collagen following laser welding. 140 2

Collagen molecules are major extracellular matrix proteins involved in the development and support of delicate auditory sensory organs. Type II collagen is widely distributed within inner ear tissues, while type IX is found only within the labyrinthine membrane and dense fibers of the tectorial membrane. Antibody specific for type II collagen has been shown to be elevated in some patients with hearing loss due to several presumably autoimmune illnesses (including Meniere's disease, otosclerosis, chronic progressive sensorineural hearing loss, and relapsing polychondritis). Purified human type II and IX collagens and an extract of human cochlear tissue were subjected to isolation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to nitrocellulose. The sera of 21 patients with inner ear disease were examined for the presence of anticollagen and anticochlear antibodies; the sera were used to probe Western blots of purified human collagens II, IX, and XI, and cochlear protein extract with peroxidase-conjugated goat anti human polyvalent immunoglobulin as the second antibody. Anti-type II collagen antibodies were seen in 12 of 21 (57%) patients, while 13 of 21 (62%) had anti-type IX antibodies detectable by Western blot. A previously unreported 30 kd (probably noncollagen) protein was 21 (62%) had anti-type IX antibodies detectable by Western blot. A previously unreported 30 kd (probably noncollagen) protein was found by SDS-PAGE of human cochlear tissue extracts, with 3 patients, all with Meniere's disease, having antibody activity to this protein detected by Western blot.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Antibodies against a 30 kilodalton cochlear protein and type II and IX collagens in the serum of patients with inner ear diseases. 146 90

Cells from cutaneous neurofibromas of three patients with von Recklinghausen's disease and skin fibroblasts from four healthy adults were cultured. After two passages, DNA and collagen syntheses were determined by measuring incorporation of [3H] thymidine and [3H] proline respectively, and expressed as the values per unit DNA content. These values from neurofibroma cells were increased by 54% in DNA synthesis and 60% (p < 0.05) in nondialyzable hydroxyproline synthesis, suggesting that neurofibroma cells in culture even after several passages still possess those characteristics corresponding to their pathological features in vivo. Collagen synthesized by neurofibroma cells appears to be normal as judged by intracellular degradation rates and SDS-polyacrylamide gel electrophoresis.
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PMID:Growth and collagen synthesis of cultured neurofibroma fibroblasts. 149 Oct 87

Collagen types were studied in the lumbar intervertebral discs of non-chondrodystrophic dogs, 1 to 3 years old. Parts of intervertebral discs were frozen and sections were subjected to the 3-methyl-benzothiazol-2-on-hydrazone (MBTH) method, which permits differentiation of genetic types and maturation stages of collagen. The annulus fibrosus showed a blue (collagen I) and a violet colour (collagen II) at the external zone. The internal zone was more homogeneous and contained a mixture of both colours (collagen I and II). The nucleus pulposus showed only the violet colour, indicative of collagen II. Discs were also dissected at three different zones and submitted to an extraction technique to obtain collagen, then subjected to SDS-polyacrylamide gel electrophoresis and determination of spectrophotometric reactions of MBTH. Both studies demonstrated type I and type II collagens in the external and internal zones of the annulus fibrosus, but only type II in the nucleus pulposus. Collagen characterization, using this technique, would allow for evaluation in pathologic events of the intervertebral discs as well as for establishing the degree of alteration.
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PMID:[Characterization of collagen of canine intervertebral disks using the N-methyl-benzothiazol-2-on-hydrazone reaction]. 171 11

Clear distinctions in morphology and proteoglycan composition have been described in regions of adult tendon that pass under bone and are subjected to compressive as well as tensional forces. In this study, developing bovine deep flexor tendon from early fetal stages through 6 months of age was examined biochemically and by light and electron microscopy. Longitudinal collagen fibers were seen in the tensional region of tendon throughout development; whereas a well established network arrangement of collagen fibers with wide interfibrillar spaces was seen in the compressed region by 7 months of fetal age. Collagen fibril diameters of both regions increased with age with the mean diameter in tensional tissue always greater than in compressed tissue. Glycosaminoglycan hexosamine content of the tensional region remained low throughout development (approximately 0.2% of dry tissue weight), but increased in the compressed region from 0.4% of dry weight at the 7-month fetal stage, to 1.0% dry weight at 6 months. Keratan sulfate was not detectable in tensional tendon at any age as measured by inhibition ELISA, but was found in increasing quantities in the pressure bearing region of tendon from young calves. Small proteoglycans predominated in both tensional and compressed regions throughout fetal and early neonatal development, and were of both PG I (biglycan) and PG II (decorin) types. Large proteoglycans represented only a small proportion of total proteoglycans in both regions of fetal tendon. By SDS/PAGE analysis, immunoreactivity, and molecular sieve chromatography, large proteoglycans of fetal compressed tendon were similar to large proteoglycans of adult tensional tendon in that they contained only chondroitin-6-sulfate, with little if any KS, and appeared to be slightly smaller than cartilage large proteoglycans.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Ultrastructure and proteoglycan composition in the developing fibrocartilaginous region of bovine tendon. 208 20


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