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 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Basement membrane changes in the epidermis and hair follicle apparatus resulting from topical 9,10-dimethylbenzanthracene applications were studied in mice, rats, and hamsters by light and electron microscopy and using antibodies to human collagen type IV and laminin. The basement membrane was distinct in epidermal hyperplasia, dysplasia, and papillomas, as well as around most of the keratoacanthomas and squamous cell carcinomas, which showed basement membrane irregularities, thickening, and reduplication in some areas. The invading edges of the squamous cell carcinomas with inflammatory infiltrates were devoid of laminin and collagen. Collagen IV and laminin-positive structures were observed around preserved follicular structures in rat: hair nevi and hair-follicle nevi, but partly absent around trichoepitheliomas and trichofolliculomas. Basal cell tumors were usually surrounded by a distinct basement membrane, which was lacking around some tumor cells.
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PMID:Basement membranes in experimentally induced skin tumors. 309 Jan 55

Dermal fibrosis, characterized by collagen accumulation, is the hallmark of several cutaneous diseases. To examine the mechanisms of collagen deposition in fibrotic skin diseases, fibroblast cultures were established from the skin of patients with progressive systemic sclerosis, morphea, scleredema, familial cutaneous collagenoma, connective tissue nevi of the collagen type, or keloids; these patients served as prototypes of fibrotic skin diseases with varying clinical features and potentially different etiologic factors. Collagen production was assayed by the synthesis of [3H]hydroxyproline, and types I and III procollagen messenger RNA (mRNA) levels were determined by dot blot hybridizations using human type I and type III procollagen-specific cDNA probes. The collagen production in fibroblast cultures from the fibrotic diseases was increased up to 6-fold over the controls, and a relatively good correlation between the collagen production and type I collagen mRNA levels was noted. The type I/III procollagen mRNA ratio in control fibroblast cultures was 5.9 +/- 1.6 (mean +/- SD). The corresponding ratio in keloid cell culture was markedly increased, while slightly decreased values were noted in the case of morphea and familial cutaneous collagenoma; the values in other cultures were within the normal range. The results suggest that procollagen production in fibroblast cultures derived from fibrotic skin diseases reflects elevated levels of the corresponding procollagen mRNA. The increased mRNA abundance, suggesting pretranslational control, may result from enhanced transcriptional activity of the corresponding gene or alternatively reflects increased stability of the mRNA molecule.
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PMID:Regulation of collagen gene expression in cutaneous diseases with dermal fibrosis: evidence for pretranslational control. 358 56

During pregnancy the collagen content of the human uterus increases sevenfold and the elastin content increases fourfold to fivefold. The stable pyridinoline cross-link is found in uterine collagen at a level of 0.11 mol per mole of collagen. The same ratio, or a higher one, is found at the end of pregnancy, indicating that pyridinoline synthesis keeps pace with the rapid synthesis of collagen. This cross-link would participate in the maintenance of high mechanical strength of the uterus needed during parturition. Uterine elastin contains 2.4 residues of desmosine plus isodesmosine in 1000 residues of amino acids. This value falls to 0.95 at term, indicating that synthesis of desmosines does not keep pace with the synthesis of elastin. Therefore, desmosine measurements do not provide an accurate index of elastin changes in pregnancy. Collagen and elastin contents in nongravid uteri increase with successive pregnancies; the cross-links remain constant during this change.
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PMID:Content of the collagen and elastin cross-links pyridinoline and the desmosines in the human uterus in various reproductive states. 403 6

Collagens of the ligamentum teres of the femur and the hip joint capsule of 14 patients with congenital dislocation of the hip (CDH) were studied biochemically. Collagen was a major component of these tissues. Solubility of collagen was reversely related to age except in two cases. Collagen of both ligamentum teres of the femur and hip joint capsule was composed of type I, III and V collagens except in three cases. In these three cases with nevus or general joint laxity, two additional collagenous components were also found. The ratios of type III collagen to type I collagen were increased in CDH except in one case with short stature. These abnormalities of collagen metabolism could be the underlying cause of CDH and other clinical symptoms in these patients.
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PMID:Soft tissue collagen in congenital dislocation of the hip. Biochemical studies of the ligamentum teres of the femur and the hip joint capsule. 647 May 41

Covalent intermolecular cross-links in collagen provide the dentine matrix with stability and tensile strength. The density of collagen cross-links varies depending on the site within the same tissue. This variation is probably due to factors such as the different amounts of stress and different turnover rates at the respective sites. The aim was to quantify the collagen cross-links in different tooth groups as an adaptation to functional requirements. For this purpose, the types and content of major cross-links in dentine collagen of human teeth from three different sites were measured and compared: incisors, premolar-canines and molars. After removal of cementum and pulp, 23 extracted teeth at different ages (27-69 yr) were individually pulverized and demineralized with EDTA. Collagen was reduced with standardized NaB3H4, hydrolysed, and subjected to amino acid and cross-link analyses. Each cross-link was quantified on the basis of mole per mole of collagen. The results indicated: (1) all teeth contained labile, reducible (dehydro-dihydroxylysinonorleucine and dehydro-hydroxylysinonorleucine) and stable, non-reducible (pyridinoline and its lysyl analogue) cross-links, and (2) the content of both reducible and non-reducible cross-links was least in incisors and greatest in molars. This suggests that dentine collagen matrix maybe functionally adaptive.
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PMID:Site comparisons of dentine collagen cross-links from extracted human teeth. 836 50

The purpose of the present study was to examine the effects of acute (3 days) unilateral diaphragm denervation (DNV) on 1) levels of alpha 1(I) and alpha 1(III) procollagen mRNA; 2) collagen concentration [hydroxyproline (HYP)]; 3) amount of the nonreducible collagen cross-link hydroxylysylpyridinoline (HP); and 4) the passive force-length relationship of the muscle. The levels of alpha 1(I) and alpha 1(III) procollagen mRNA, HYP concentration, and amount of HP were measured in muscle segments from the midcostal region of DNV and intact (INT) hemidiaphragms of adult male Fischer 344 rats (250-300 g). The in vitro passive force-length relationship of DNV and INT hemidiaphragm was determined by lengthening and shortening the diaphragm muscle segments from 85 to 115% of optimal length at a constant velocity (0.6 optimal length/s). Three days after DNV, the level of alpha 1(I) procollagen mRNA was increased over 15-fold in the DNV hemidiaphragm compared with INT (P < 0.05), whereas the level of alpha 1(III) procollagen mRNA was increased by approximately sixfold in the DNV hemidiaphragm compared with INT (P < 0.05). Collagen (HYP) concentration did not differ between groups, averaging 8.7 and 8.9 micrograms/mg dry wt for the DNV and INT hemidiaphragms, respectively. In addition, there was no difference in the amount of the mature nonreducible collagen cross-link HP between the DNV and INT hemidiaphragms (0.66 vs. 0.76 mole HP/mole collagen, respectively). The amount of passive force developed during lengthening did not differ between DNV and INT hemidiaphragms. These data indicate that acute DNV of the hemidiaphragm is associated with an increase in the mRNA level of the two principal fibrillar collagen phenotypes in skeletal muscle. However, despite extensive muscle remodeling, the passive force-length relationship of the DNV hemidiaphragm is unaffected compared with the INT muscle.
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PMID:Changes in diaphragm muscle collagen gene expression after acute unilateral denervation. 856 69

Collagen biosynthesis was analyzed in C57BL/6J mice homozygous for the high-growth locus. Plasma levels of insulin-like growth factor-1 (IGF-1) were significantly elevated in high-growth mice at all ages studied (3 wk-6 mo); IGF-binding proteins were also elevated. Skin biopsies were obtained from mice aged 3, 6, and 9 wk under halothane anesthesia. Mice were killed at 6 mo of age. Collagen, expressed per weight of tissue, was significantly increased in all tissues from high-growth mice, as was collagen cross-linking, expressed as moles of cross-link per mole of collagen. Expression of types I and III collagen, lysyl oxidase, and lysyl hydroxylase was increased in all tissues analyzed. There was a preferential increase in type III expression relative to type I expression. Rate and extent of accumulation of collagen in granulation tissue were measured in polyvinyl alcohol sponges implanted subcutaneously; collagen accumulation was significantly greater in the high-growth mice. These results suggest that 1) elevated circulating IGF-1 may increase collagen deposition both in normal tissue as well as in granulation tissue by increasing collagen gene expression, 2) IGF-1 may increase collagen cross-linking by stimulating expression of lysyl oxidase, and 3) the preferential increase in dihydroxylated cross-links observed in high-growth mice may be due to the stimulation of lysyl hydroxylase expression by IGF-1. In summary, elevated levels of IGF-1 appear to affect collagen both quantitatively and qualitatively, primarily through their effects on gene expression of collagen and of those enzymes responsible for posttranslational modifications of collagen.
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PMID:Effects of elevated circulating IGF-1 on the extracellular matrix in "high-growth" C57BL/6J mice. 885 93

Adult articular cartilage is divided by the tidemark into a deep calcified layer and a more superficial uncalcified layer. Histologic examination of articular cartilage from the knee joint of golden Syrian hamsters 123 days of age or older revealed defects at the tidemark in the tibia. Defects ranged from small separations of the calcified and uncalcified layers along the tidemark to progressively larger defects apparently formed by dissolution. These larger defects appeared as cavities in the noncalcified cartilage, had smooth rather than rough edges, frequently contained coalesced debris, and often resulted in a bulge in the articular surface. Occasionally, these large defects broke through the articular surface. Defects were not observed in tibial cartilage of younger (<90 days old) hamsters or in femoral cartilage from hamsters of any age. Exercise neither protected against nor increased the severity of the defects. Collagen cross-linking by pyridinoline was examined as a function of age and increased from 1,090 to 3,062 micromoles of pyridinoline/mole of hydroxyproline over the period of 1-9 months of age but was not correlated with defect formation. With increasing age, these focal tidemark defects could lead to osteoarthrosis-like cartilage lesions.
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PMID:Histology and tissue chemistry of tidemark separation in hamsters. 1009 42

Collagen molecules in solution unfold close to the maximum body temperature of the species of animal from which the molecules are extracted. It is therefore vital that collagen is stabilized during fiber formation. In this paper, our concept that the collagen molecule is thermally stabilized by loss of configurational entropy of the molecule in the fiber lattice, is refined by examining the process theoretically. Combining an equation for the entropy of a polymer-in-a-box with our previously published rate theory analysis of collagen denaturation, we have derived a hyperbolic relationship between the denaturation temperature, Tm, and the volume fraction, epsilon, of water in the fiber. DSC data were consistent with the model for water volume fractions greater than 0.2. At a water volume fraction of about 0.2, there was an abrupt change in the slope of the linear relationship between 1/Tm and epsilon. This may have been caused by a collapse of the gap-overlap fiber structure at low hydrations. At more than 6 moles water per tripeptide, the enthalpy of denaturation on a dry tendon basis was independent of hydration at 58.55 +/- 0.59 J g-1. Between about 6 and 1 moles water per tripeptide, dehydration caused a substantial loss of enthalpy of denaturation, caused by a loss of water bridges from the hydration network surrounding the triple helix. At very low hydrations (less than 1 mole of water per tripeptide), where there was not enough water to form bridges and only sufficient to hydrogen bond to primary binding sites on the peptide chains, the enthalpy was approximately constant at 11.6 +/- 0.69 J g-1. This was assigned mainly to the breaking of the direct hydrogen bonds between the alpha chains.
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PMID:Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers. 1035 49

Crosslinking agents are used for improving the physical properties and durability of collagenous implants, glutaraldehyde (GTA) being the most widely used. Many of these reagents, including GTA, are known to be cytotoxic and to induce calcification. Hence, it is desirable to develop new crosslinking methods for collagen, so that biocompatibility and physical properties are improved. In the present study, dimethyl 3,3' -dithiobispropionimidate (DTBP) has been tried as a novel crosslinking reagent for collagen. Collagen purified from rat tail tendon has been crosslinked with DTBP and GTA. An increase of 22 degrees C in shrinkage temperature is observed for collagen treated with DTBP under optimal conditions. Crosslinking density determination shows that DTBP induces 10 crosslinks per mole, compared to 13 by GTA. While the tensile strength of GTA-treated samples is greater than those treated with DTBP, the latter shows more extensibility. In vitro degradation studies show that both GTA- and DTBP-treated samples are resistant to degradation by collagenase. The biocompatibility of crosslinked collagen samples studied by subcutaneous implantation in rats show that while both GTA- and DTBP-treated collagen do not degrade for up to 4 weeks, ultrastructural and histological studies indicate that DTBP collagen is far more biocompatible than GTA-treated matrices.
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PMID:Dimethyl 3,3'-dithiobispropionimidate: a novel crosslinking reagent for collagen. 1107 11


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