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Query: HUMANGGP:031673 (collagen)
 124,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A total of 160 1-2 day old chickens were fed a 2% cholesterol diet for a period of 8 to 42 days and compared with an equal number of controls. Aortas were analyzed for various indexes of reactivity of connective tissue, cholesterol content and scanning electron microscopy (SEM) characteristics of the endothelial lining. Cholesterol feeding for a period up to 6 weeks resulted in doubling the level of serum cholesterol. It was, however, without effect on the activity of prolyl hydroxylase, lysyl oxidase, collagenase and collagen content in the aortic wall. As early as 3 weeks of feeding significant changes occurred in total and esterified cholesterol content. At the same time endothelial cells were characteristically contracted with several long cytoplasmic elongations and protrusions. A significant decrease of activity of the above enzymes was found in aortic tissue with increased age of the chicken. Collagen content in aortas increased with age of chickens. It is concluded that cholesterol as an atherogenic agent induces marked changes in endothelial cells and lipids of chicken aorta at earlier periods, prior to the activation of connective tissue.
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PMID:Early changes in the arterial wall of chickens fed a cholesterol diet. 0 48

1. Collagen fibrils were modified with beta-1-[3,3-dimethyl-6'-nitrospiro-(indoline-2,2'-2H-benzopyran)] propionic anhydride. 2. Urease (urea amidohydrolase, EC 3.5.1.5) was immobilized in spiropyran collagen membrane. The activity of the urease-spiropyran collagen membrane was found to increase in the dark and then decrease with visible light irradiation. 3. The optimum pH of the urease-spiropyran collagen membrane under visible light was lowered in the dark. 4. The apparent Michaelis constant (K'm) of the urease-spiropyran collagen membrane in the dark was almost the same as that under visible light. The apparent maximum velocity was increased in the dark. 5. The diffusion coefficient of urea through the spiropyran collagen membrane in the dark was 1.4 times that under visible light. However, the increase of the diffusion rate was not responsible for the activity increase of the urease-spiropyran collagen membrane.
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PMID:Photocontrol of urease activity in spiropyran collagen membrane. 0 96

Catechol analogs inhibit the formation of hydroxylysine-derived intermolecular collagen cross links in tissue cultures of chick embryo calvaria. Formation of intermolecular collagen cross links was measured following incorporation of [14C]lysine, reduction with sodium borohydride, and elution from an ion exchange column with a pyridine-formate gradient. Cultures grown in the presence of 10(-3) M catechol, 10(-3) M dopamine, 10(-3) M L-dopa, or 10(-3) M D,L-serine-(2,3,4-trihydroxybenzyl)-hydrazide demonstrated between 43 and 84% inhibition of hydroxylysine formation. Collagen biosynthesis was not diminished in these cultures as compared to controls without additions or with beta-aminopropionitrile when measured by collagenase digestion. The formation of hydroxylysine-derived intermolecular cross links was inhibited 34 to 93% for 5,5'-dihydroxylysinonorleucine and 7 to 71% for 5-hydroxylysinonorleucine. The catechol analogs also inhibit the activity of lysyl hydroxylase as measured by specific tritium release as triated water from an L-[4,5-3H]lysine-labeled unhydroxylated collagen substrate prepared from chick calvaria. Since catechol analogs inhibit the formation of hydroxylysine in a cell-free assay, these compounds must pass into the cells of calvaria in this culture system to inhibit intracellular hydroxylysine formation and subsequently to diminish the reducible intermolecular cross links of the newly synthesized collagen.
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PMID:In vitro inhibition of collagen cross links by catechol analogs. 1 15

Collagenolytic cathepsin, which can liberate soluble hydroxyproline-containing products from insoluble vitreous collagen with maximum activity at pH 3.5, was biochemically studied in uveal lysosomes of bovine eye. Collagen solubilization was proportional to both enzyme concentration and incubation time. When the enzyme was heated, no reaction was observed. Collagen solubilization by uveal lysosomal extract was almost unaffected by Ca2+ ion, cysteine, beta-mercaptoethanol, and ethylenediaminetetraacetic acid, but inhibited about one-third by pepstatin. The possible role of collagenolytic cathepsin in vitreous liquefaction was considered.
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PMID:The presence of collagenolytic cathepsin in uveal lysosomes of bovine eye. 2 92

Two groups of 60 male Sprague-Dawley rats aged 3 and 20-24 months respectively were used to establish a 3-compartmentmodel of the kinetics of the collagen metabolism in the tail tendon and skin by means of tritium labelled L-prolin. The 3 compartments were divided into pro- and tropocollagen, labile polymer collagen and stabile polymer collagen respectively. The results suggest the following conclusions concerning the metabolism and ageing of the collagens investigated: 1. Collagen of the tendon and collagen of the skin reveal different dynamics of metabolism. 2. Stabile and labile polymeric collagen originate from different tropocollagens. 3. Both intracellular and extracellular processes are responsible for the age-changes of tendon- and skin-collagen.
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PMID:[A mathematical model of the kinetics of collagen metabolism in the tendons and skin of young and old rats]. 3 56

Collagen prepared from rat, calf, or pig skin was tested on guinea pigs for active cutaneous anaphylaxis. Only one fraction of calf skin collagen gave a slight, positive reaction. No positive reactions were observed in 21 subjects submitted to patch tests and 12 subjects submitted to scratch tests with pig skin collagen. Therefore preparations of pig skin collagen may be used for wound treatment without any risk.
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PMID:Immunological investigations of antigenicity and specificity of soluble collagen fractions. IV. Anaphylaxis and allergy experiments. 5 67

The universal features of the histopathology of fibrotic lung disease are derangement of parenchymal collagen and infiltration of the parenchyma with chronic inflammatory cells. To determine if this cellular reaction might be associated with autoimmunity to a consitituent of the alveolar interstitium, peripheral blood lymphocytes were exposed to human type I collagen in vitro and evaluated for the production of migration inhibition factor and cytotoxicity. Data from 18 patients with idiopathic pulmonary fibrosis, 8 patients with pulmonary fibrosis other than idiopathic pulmonary fibrosis, 12 patients with nonfibrotic lung disease, and 9 normals demonstrated that circulating lymphocytes from more than 94% of patients with fibrotic lung disease take part in processes where the recognition of collagen results in migration inhibition factor production and lysis of collagen-coated sheep red blood cells. These collagen-induced cell-mediated phenomena are obviated with human T-lymphocyte antiserum. Collagen-induced migration inhibition factor production and cytotoxicity were found in less than 20% of patients with nonfibrotic disease and were not found in normals. Qualitatively, there was no organ (lung, skin) or species (human, rabbit) collagen specificity in these assays, but human lung alpha 2 chains were recognized more often than alpha 1(I) chains. Circulating lymphocytes from patients with fibrotic disease are present in a normal T to B ratio. These lymphocytes did not incorporate [3H]thymidine when exposed to collagen but did when exposed to T-cell mitogens. These in vitro observations suggest that circulating T-lymphocytes and lung collagen may be intimately associated in the pathogenesis of human fibrotic lung disease.
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PMID:Pathogenic mechanisms in pulmonary fibrosis: collagen-induced migration inhibition factor production and cytotoxicity mediated by lymphocytes. 6 60

A cross-linked fragment (peptide T1X) with a molecular weight of 13,000 could be isolated from a tryptic digest of insoluble type III collagen of calf skin. Peptide T1X was conjugated on to bovine serum albumin by glutaraldehyde and used for immunization of rabbits. The antisera reacted in passive haemagglutination and radioimmune assay with peptide T1X, type III collagen and its constituent alpha1(III) chain. Little or no reaction was observed with type I collagen and alpha1(I) chain. While rabbit antisera to neutral salt-soluble type III Collagen also showed a strong binding for 125I-labelled peptide T1X much less reaction was observed with antisera to type I collagen. The antigenicity of type III collagen was largely destroyed by pepsin treatment suggesting that it resided in non-helical segments. A fragment of peptide T1X produced by digestion with collagenase retained antigenic activity. The data indicated that the aminoterminal region of type III collagen contains strong antigenic determinants located in a non-helical sequence of about sixteen amino acids. Antibodies to these antigenic determinants were purified and rendered specific for type III collagen by immunoadsorption. The antibodies stained in indirect immunofluorescence tests particularly those regions in various connective tissues which are rich in reticulin fibres. Different staining patterns were observed with antibodies to type I collagen.
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PMID:Production and specificity of antibodies against the aminoterminal region in type III collagen. 6 19

Pulmonary fibrosis was induced in eight baboons with bleomycin; five untreated animals were controls. After 45-65 U/kg of bleomycin, lung volumes and diffusing capacity were reduced, and static lung pressure-volume curves were shifted to the right. Right middle lobes were resected at this time in five bleomycin-treated and two control animals. Compared to controls, right middle lobes from bleomycintreated animals had increased weight and contained increased amounts of total protein, collagen, elastin, and DNA; synthesis of collagen and noncollagen protein were also elevated. Occasional alveolar septae were edematous and infiltrated by mononuclear inflammatory cells; a slight increase in collagen was demonstrable histologically. Four of six treated animals died with extensive diffuse interstitial fibrosis after 95 U/kg of bleomycin. Biochemical analyses revealed significantly elevated lobar contents of dry weight, protein, elastin, and collagen. Two animals survived 95 U/kg of bleomycin and were terminated 6 mo after treatment. In these animals, physiologic studies were indicative of restrictive lung disease, but lung histology was nearly normal. Lung weight, total protein, and DNA had returned to control values, but collagen and elastin were increased in amount and concentration. Bleomycin induces an intense inflammatory response in the lung. During this inflammation, connective tissue proliferation occurs in concert with proliferation of other tissue components. Cessation of bleomycin treatment is followed by resolution of inflammation manifested by decreases in tissue mass, cellular content, and nonconnective tissue protein. Collagen and elastin deposited during inflammation are less successfully removed during resolution, leading to a stage characterized by increased concentrations of these proteins. A similar sequence of tissue alterations may occur in idiopathic diffuse interstitial fibrosis of man in response to various lung injuries.
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PMID:Bleomycin-induced diffuse interstitial pulmonary fibrosis in baboons. 7 49

We studied the modifications of collagen fibrils during the histogenesis of the intervertebral disc of cats. In connexion with these studies it is necessary to distinguish between the fibrillar (functional) structure, the arrangement of fibrils, and the nature of fibrils, their diameter, period and other properties. Collagen fibrils (40--50 nm) of the anulus fibrosus enter in hyaline cartilage and split off in thin fibrils (8--10 nm). In this area the cartilage fibrils have a diameter of 20--22 nm, in a greater distance the diameter is diminished to 7--8 nm. Analogous to the changing of the nature of fibrils, the number of the cells related to the sectional area is diminished. The cells of the anulus fibrosus resemble those of tendons. In the transition area their shape becomes roundish, the number of granular membranes is increased, a voluminous Golgi-Apparatus appears for a short time. Finally, the cells are once transformed in cartilage cells with a small reticulum or cells of fibrocartilage with a capsule and a decreased cytoplasm; some cells are disintegrated. In the capsule of the fibrocartilage cells, parallel orientated filaments exhibit a periodical arrangement. In the border of the capsule, filaments change into periodical fibrils. Therefore, we must regard cells and their surrounding intercellular substance as metabolic unity which in the cartilage may be characterized as the chondron.
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PMID:[Crystallization and dissolution of collagen fibrils during the histogenesis of the intervertebral disk]. 7 84


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