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Query: HUMANGGP:031456 (Sep)
 2,027,840 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extracts of highly purified lysosomes from rat liver were examined for their ability to degrade native collagen and thermally denatured collagen at pH values between 3.5 and 7.0. After a 24-h digestion at 36 degrees with the lysosomal extract at a pH of 5.5 or lower (collagen/lysosomal protein; 2/1 or 8/1), both native and denatured collagen were degraded to an extent equivalent to 60 to 70% of that observed upon total acid hydrolysis in 6 N HCl as measured by the ninhydrin reaction (570 nm). At a pH of 6.0, native collagen and denatured collagen were degraded by the mixture of lysosomal proteinases to 11% and 40% of total acid hydrolysis, respectively. At pH 6.5 AND 7.0, the corresponding values were 3% versus 33% and 0.3% versus 11%, respectively. Fragments of collagen (TCA and TCB) are produced when mammalian collagenase degrades native collagen at 25 degrees. These fragments were degraded by the lysosomal extract at 36 degrees to an extent equivalent to 28% and 8% of total acid hydrolysis at pH 6.5 and 7.0, respectively. The experiments at pH 6.5 and 7.0 were done using a collagen/lysosomal protein ratio of 2/1. At pH 5.0 (a pH which is found within secondary lysosomes), the lysosomal extracts degraded collagen to a mixture of free amino acids and small peptides. Amino acid analysis established that approximately 30% of the amino acid residues of the collagen appeared in the lysosomal hydrolysate as free amino acids. Hydroxyproline and perhaps hydroxylysine were the only amino acids found in collagen which did not appear at least to some extent as the free amino acid in this hydrolysate.
J Biol Chem 1976 Sep 10
PMID:Digestion of native collagen, denatured collagen, and collagen fragments by extracts of rat liver lysosomes. 0 59

The activities of adenylate and guanylate cyclase and cyclic nucleotide 3':5'-phosphodiesterase were determined during the aggregation of human blood platelets with thrombin, ADP, arachidonic acid and epinephrine. The activity of guanylate cyclase is altered to a much larger degree than adenylate cyclase, while cyclic nucleotide phosphodiesterease activity remains unchanged. During the early phases of thrombin-and ADP-induced platelet aggregation a marked activation of the guanylate cyclase occurs whereas aggregation induced by arachidonic acid or epinephrine results in a rapid diminution of this activity. In all four cases, the adenylate cyclase activity is only slightly decreased when examined under identical conditions. Platelet aggregation induced by a wide variety of aggregating agents including collagen and platelet isoantibodies results in the "release" of only small amounts (1-3%) of guanylate cyclase and cyclic nucleotide phosphodiesterase and no adenylate cyclase. The guanylate cyclase and cyclic nucleotide phosphodiesterase activities are associated almost entirely with the soluble cytoplasmic fraction of the platelet, while the adenylate cyclase if found exclusively in a membrane bound form. ADP and epinephrine moderately inhibit guanylate and adenylate cyclase in subcellular preparations, while arachidonic and other unsaturated fatty acids moderately stimulate (2-4-fold) the former. It is concluded that (1) the activity of platelet guanylate cyclase during aggregation depends on the nature and mode of action of the inducing agent, (2) the activity of the membrnae adenylate cyclase during aggregation is independent of the aggregating agent and is associated with a reduction of activity and (3) cyclic nucleotide phosphodiesterase remains unchanged during the process of platelet aggregation and release. Furthermore, these observations suggest a role for unsaturated fatty acids in the control of intracellular cyclic GMP levels.
Biochim Biophys Acta 1976 Sep 24
PMID:Cyclic nucleotides and platelet aggregation. Effect of aggregating agents on the activity of cyclic nucleotide-metabolizing enzymes. 0 49

Lysyl oxidase is a specific amine oxidase that catalyzes the formation of aldehyde cross-link intermediates in collagen and elastin. In this study, lysyl oxidase from embryonic chick cartilage was purified to constant specific activity and a single protein band on sodium dodecyl sulfate acrylamide gel electrophoresis. This band had an apparent molecular weight of 62,000. The eluted protein cross-reacted with inhibiting antisera developed against highly purified lysyl oxidase. The highly purified enzyme was active with both insoluble elastin and embryonic chick skin or bone collagen precipitated as reconstituted, native fibrils. There was low activity with nonhydroxylated collagen, collagen monomers, or native fibrils isolated from lathyritic calvaria. The maximum number of aldehyde intermediates formed per molecule of collagen that became insoluble was two. These results indicate that lysyl oxidase has maximum activity on ordered aggregates of collagen molecules that may be overlapping associations of only a few collagen molecules across. Formation of aldehyde intermediates and cross-links during fibril formation may facilitate the biosynthesis of stable collagen fibrils and contribute to increased fibril tensile strength in vivo.
J Biol Chem 1976 Sep 25
PMID:Collagen cross-linking. Purification and substrate specificity of lysyl oxidase. 0 1

In this paper, the synthesis of collagen cross-links in vitro was investigated in a defined system consisting of highly purified chick cartilage lysyl oxidase and chick bone collagen fibrils. Cross-link synthesis in vitro was quite similar to the biosynthesis of collagen cross-links in vivo. Enzyme-dependent synthesis of cross-link intermediates and cross-linked collagen derived from lathyritic collagen occurred. The concentration of the two principal reducible cross-links, N6:6'-dehydro-5,5'-dihydroxylysinonorleucine and N6:6'-dehydro-5-hydroxylysinonorleucine, increased to a peak value of approximately two cross-links per molecule and then decreased. Synthesis of histidinohydroxymerodesmosine and a second polyfunctional cross-link of unknown structure began after synthesis of bifunctional cross-links was largely completed and proceeded linearly afterwards. Inhibition of lysyl oxidase after the bulk of bifunctional cross-link synthesis had occurred did not alter the rate of decrease in reducible cross-link concentration but did inhibit further histidinohydroxymerodesmosine synthesis. These results indicate that lysyl oxidase and collagen fibrils are the only macromolecules required for cross-link biosynthesis in vivo. It is likely that the decrease in reducible cross-links observed during fibril maturation results from spontaneous reactions within the collagen fibril rather than additional enzymatic reactions.
J Biol Chem 1976 Sep 25
PMID:Collagen cross-linking. Synthesis of collagen cross-links in vitro with highly purified lysyl oxidase. 0 2

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.
Atherosclerosis 1976 Sep
PMID:Early changes in the arterial wall of chickens fed a cholesterol diet. 0 48

Here thermal contraction-relaxation and dissolution of collagen from rat tail tendon fibers were studied simultaneously. It is concluded that both processes change their character in the same manner with increasing age and that the relaxation phase probably is a result of the dissolution of collagen from the fibers.
Aktuelle Gerontol 1977 Sep
PMID:Thermal contraction-relaxation and dissolution of rat tail tendon collagen in different ages. 2 76

The effect of pH in the range 6.6-8.2 on the incorporation of 14C-proline into the rabbit dental pulp incubated in vitro has been studied. The amount of label in the cold TCA-soluble pool, total protein, and hydroxyproline (i.e. collagen) of the pulp tissue increased linearly with pH in all three fractions. A similar increase was found in the amount of labeled total protein and collagen recovered from the incubation medium. The results indicated that the uptake of 14C-proline into the TCA-soluble pool was the pH-sensitive step, whereas the incorporation into protein, formation of hydroxyproline, and the release of labeled macromolecules into the medium were not affected to any measurable degree by the ambient pH. In this system, zinc (60 micrometer) had less effect on the incorporation of 14C-proline into the different fractions of the pulp tissue at pH 6.6 as compared with pH 7.4, whereas with fluoride (1.3 mM) an increased inhibition of the uptake of 14C-proline into the TCA-soluble pool and the incorporation into total protein was found upon lowering the pH to 6.8. The inhibitory effect of zinc and fluoride on the release of labeled total protein and collagen into the incubation medium was not affected when the pH was lowered.
Scand J Dent Res 1977 Sep
PMID:PH and the effect of fluoride and zinc on protein and collagen biosynthesis in rabbit dental pulp in vitro. 2 25

The axial skeletal rod of Veretillium cynomorium consists of a fibrillar collagenous matrix calcified with calcite. The present paper describes ultrastructural and crystallographic details of its organization and deposition. At the inferior end of the rod is a calcification gradient between the noncalcified tip and the rest of the axis. Initial mineral deposits, which are sometimes associated with cell debris, give rise to calcitic nodules which enlarge by the radical growth of several lobes. These nodules fuse and form the core of the axis. Subsequent increase in diameter of the rod involves the radial development of irregular columns of calcite which arise from the peripheral nodules. Mineral surfaces exhibit a distinctive microarchitecture which can be related to the predominantly c-axis parallel growth of the calcite. Particular attention is paid to the relationship between mineral and matrix. The collagen fibrils, embedded in the calcite but never impregnated with it, are not responsible for the initial nucleation of mineral. The crystallographic orientation of the calcite also appears to be independent of these fibrils.
Cell Tissue Res 1978 Sep 05
PMID:Calcification of the collagenous axial skeleton of Veretillum cynomorium pall. (Cnidaria: Pennatulacea). 2 8

Soluble fibronectin is found in body fluids and media of adherent cultured cells and binds to fibrin and collagen. Insoluble fibronectin is found in tissue stroma and in extracellular matrices of cultured cells. Fibronectin is a substrate for Factor XIIIa (plasma transglutaminase) and can be cross-linked by Factor XIIIa to itself and the the alpha-chain of fibrin. We used sodium dodecyl sulfate-polyacrylamide gel electrophoresis to investigate Factor XIIIa-mediated crosslinking of fibronectin to collagen. At O degrees or 37 degrees C, fibronectin could be cross-linked to iodinated cyanogen bromide fragment 7 of the alpha 1(I) chain. At 22 degrees or 37 degrees C, fibronectin could be cross-linked to isolated alpha 1(I) chains of type I collagen. Fibronectin could also be crosslinked to types I and III collagen, but only at 37 degrees C. alpha 1(I)-CB7, alpha 1(I) collagen chains, type I collagen, type III collagen, and fibrin all blocked cross-linking between 125I-alpha 1 (I)-CB7 and fibronectin. alpha 1(I)-CB7 blocked cross-linking between fibronectin and fibrin. These results indicate that the determinants of fibronectin-fibrin and fibronectin-collagen binding and cross-linking are similar. Cross-linking of fibronectin to collagen likely occurs in vivo and may be important for normal wound healing, collagen fibrillogenesis, and embryogenesis.
J Clin Invest 1979 Sep
PMID:Cross-linking of fibronectin to collagen by blood coagulation Factor XIIIa. 3 60

The corneo-scleral changes described are highly characteristic and may be the first signs of an underlying systemic disorder so that otherwise healthy patients who present with limbal guttering and scleral disease must be continuously monitored with this association in mind. The clinical and histological features of limbal guttering in connective tissue disorders strongly suggest that a local antigen-antibody reaction triggers off a number of biochemical and cellular responses which combine to produce lysis of scleral and corneal collagen, although immune complexes have not so far been demonstrated in these eyes. Modes of therapy aimed at one particular chain of events have varying degrees of success, as indeed does more blunderbuss treatment with steroids, anti-inflammatory drugs, or cytotoxic agents. The early stages of the ocular lesion in the rabbit are now being studied, as is the immunological basis for its production. It is hoped that further work with the animal model will lead to a deeper understanding of the pathogenesis of these conditions, which will turn provide both ophthalmologists and rheumatologists with more scientific guidelines for treatment.
Trans Ophthalmol Soc U K 1978 Sep
PMID:Destructive corneal disease in the connective tissue disorders. Comparison with an experimental animal model. 3 36


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