Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. In contrast to collagen from the aponeurosis of normal adult subjects, the nodules, contractures and apparently unaffected aponeurosis from patients with Dupuytren's disease contained substantial amounts of type III collagen. 2. The presence of type III collagen supports the previous proposal that the initial response to injury is the synthesis of an increased proportion of this form of collagen. The increased amounts in the apparently unaffected aponeurosis indicate the disease is not strictly focal but more systemic than is usually considered.
Clin Sci Mol Med 1977 Nov
PMID:Collagen of Dupuytren's disease. 58 33

Disulfide-groups are demonstrated in the basement membranes of glomerular capillaries, proximal convoluted tubules, and collecting ducts by means of a thiosulfathion/Alcian Blue +0.8 Mol MgCl2-staining sequence. It is suggested that the reaction shows type IV collagen of basal lamina material, which is characterized by a relatively high cystine content (8 half-cystine residues/1000).
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PMID:Histochemical demonstration of type IV collagen in the renal glomerulus. 64 Aug 66

1. Plasma and buffy-coat vitamin C, urinary proline, hydroxyproline, creatinine and total amino acid concentrations were meausred in 23 healthy elderly subjects at intervals of 3 months. 2. There was a strong positive correlation between plasma vitamin C and buffy-coat vititamin C. 3. There were not significant correlations between plasma or buffy-coat vitamin CPAMIN C. 3. There were not significant correlations between plasma or buffy-coat vitamin C and total urinary hydroxyproline, whether expressed on a creatinine basis or on a total amino acid basis. Similarly, no significant correlations could be detected involving the proline/hydroxyproline ratio in urine hydrolysates. 4. There was a significant negative correlation between plasma or buffy-coat vitamin C and total urinary proline, when expressed per unit of total urinary proline, when expressed per unit of total urinary proline, when expressed per unit of total amino acids in the hydrolysates. This correlation was not observed with unhydrolysed urine, and it appeared to reside in the diffusible fraction, part of whose proline could be liberated by prolidase digestion. In addition, in the man, there was some evidence for a positive correlation between plasma or buffy-coat vitamin C and the ratio of total urinary amino acids to creatinine. 5. These results support the view that poor vitamin C status in elderly humans may be associated with a defect in collagen proline hydroxylation, reflected by increased excretion of proline-rich, collagen-derived peptides. If this interpretation is correct, it indicates a potential defect in connective tissue repair, and could form the basis of a functional test for subclinical vitamin C deficiency.
Clin Sci Mol Med 1977 May
PMID:Proline and hydroxyproline excretion and vitamin C status in elderly human subjects. 86 47

Collagen mRNA has already been purified and characterized by us. Its purity has now been enhanced by two different methods. Gel electrophoresis shows in either method, a single peak with the same mobility already reported: 1.05 X 10(6) daltons. Base composition analyses of collagen mRNA purified by either method were almost identical. Chemical analyses of the isolated polyadenylic acid stretch show that it is, 0.48 X 10(5) daltons-long, (about 140 nucleotides-long), contains 75% AMP, and is located at the 3' end of the polymer.
Mol Biol Rep 1976 Jul
PMID:Further studies on collagen mRNA: partial chemical characterization and polyadenylic acid sequence. 95 18

The periodic protein collagen is of special interest for the study of the relationship which exists between the structure of a protein and that of its mRNA, because oligopeptides containing glycine, proline (hydroxyproline) and alanine occur with great frequency in it. Collagen is particularly rich in these amino acids, which have codons containing only G and/or C in the obligatory first and second positions. If unlimited choice of codons for all amino acids were to occur, the stretch of mRNA coding for an alpha-chain should contain about 40% G and 31% C (Bachra et al., 1974). These high values suggest that a considerable degree of secondary structure will occur, unless selective codon use would result in the avoidance of G and C in optional third codon positions. In the present paper putative secondary structure formation in collagen mRNA was studied. This was done by studying the positions and frequencies of hairpin structures which could contain stem sections composed of the coding triplets of the above mentioned amino acids and hairpin sections of 4-40 bases. Calculation of the free energy contributions of such hairpin structures, using published values for the contributions of base-pair stacking, hairpin, bulge and interior loops and also taking into account the possible minimum number of base-pairs required for helix nucleation from a single-strand RNA (3 adjacent AU-pairs or 1 or 2 adjacent GC-pairs) led to the following conclusions. A considerable number of alternative, mutually exclusive hairpins can be constructed.
J Mol Evol 1976 Aug 03
PMID:Self complementarity in messenger RNA of collagen. I. Possible hairpin structures in regions coding for oligopeptides of glycine, proline (hydroxyproline) and alanine. 96 90

1. A study has been made of peptide excretion in twenty cases of Wilson's disease, ligand-exchange column chromatography being used to separate peptides from free amino acids. Previous reports of excess of peptide output in the disease were confirmed and the excess was shown to be highly significant statistically. 2. A considerable fraction of the excess of peptide output was shown to consist of hydroxyproline-containing peptides derived from collagen degradation. 3. The method of rank correlation showed that the difference both in free amino acid and peptide-bound amino acid output in cases of Wilson's disease and in control subjects was mainly quantitative; the pattern of amino acid excretion was qualitatively similar in both groups. 4. Evidence is presented that the increase copper output in the urine in the disease is not secondary to peptiduria.
Clin Sci Mol Med 1976 Oct
PMID:Urinary excretion of peptides and of hydroxyproline in Wilson's disease. 97 77

1. Skin collagen from fifteen patients with idiopathic adolescent scoliosis, three with congenital scoliosis, and fourteen patients with various degrees of Marfan's syndrome has been examined. 2. The stability of a polymeric collagen fraction, extracted from the skin of these patients, to depolymerization, has been compared with that from thirty-one matched control subjects. 3. The mean polymeric collagen stability was significantly reduced (P less than 0-01) in the group of fifteen patients with idiopathic adolescent scoliosis. The individual reductions in stability were greater in the younger patients and no reduction was found in two patients aged 19 years who had a mature skeleton. 4. The mean stability of polymeric skin collagen from the group of patients with Marfan's syndrome was not significantly abnormal, although there were individual low values. 5. Polymeric collagen of low stability was present in individual patients from each clinical group. Instability of collagen (from whatever cause) at a time of rapid growth may contribute to the high incidence of scoliosis in adolescent girls. In boys, adolescent scoliosis is less common and the maximum growth rate occurs at a time when collagen stability is less reduced.
Clin Sci Mol Med 1976 Nov
PMID:Skin collagen in idiopathic adolescent scoliosis and Marfan's syndrome. 99 44

In recent years it has become evident that genetic polymorphism is dramatically expressed in the structural protein, collagen. Current information on the biochemical properties, biosynthesis, and tissue distribution of Type I, II, and III collagens is summarized with special reference to possible unique functional roles fulfilled by each of these collagens.
Mol Cell Biochem 1976 Dec 10
PMID:Biochemical characteristics and biological significance of the genetically-distinct collagens. 100 2

The temperature dependences of the NMR-broad line spectra of collagen from Achilles tendon have been investigated. It is found that the narrow doublet splitting collapsed at certain temperature Tx determined by age of collagen sample. The Tx varied from approx. +35 degrees C for 8 years sample to -2 degrees C for 82 years. The interpretation of results obtained is based on the theory of NMR spectra of diffusing water molecules.
Mol Biol (Mosk)
PMID:[Discovery of age effect in molecular structure of collagen]. 105 80

The insoluble collagen from methylcholanthrene induced sarcoma was isolated and characterized. It contains more glycine, hydroxyproline and acidic amino acids than normal connective tissue collagen. An anionic character of tumour collagen was stated (pI 6.1). No typical collagen subunits in this protein were found. The tumour collagen is strongly bound to acidic glycoprotein containing a significant amount of hydroxylysine. Such an insoluble complex is resistant to the dispersing action of EDTA. It dissociates during heating in concentrated urea.
Mol Cell Biochem 1975 Jul 31
PMID:Insoluble collagen of methylcholanthrene induced sarcoma. 117 75


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