hydroxylysine and Bone-Diseases

Topics: Adolescent; Bone Diseases; Bone Matrix; Collagen; Humans; Hydroxylysine; Hydroxyproline; Osteogenesis Imperfecta; Peptides

In inflammatory granuloma, synovial sclerosis or inflammation and in Dupuytren's contracture, the neocollagen contains chains and/or transverse links that are characteristic of rapidly growing immature tissues. In arthrosis, a conversion of collagen synthesis towards a cutaneous type may occur. The destruction of cartilage in rheumatoid arthritis is brought about by a specific collagenase that originates from the inflamed synovial membrane. Finally, certain forms of osteoporosis may be due to alterations of the osseous collagen which impair the mechanism of calcification.

Topics: Animals; Arthritis, Rheumatoid; Bone Diseases; Cartilage, Articular; Collagen; Collagen Diseases; Dupuytren Contracture; Fibroblasts; Granulation Tissue; Granuloma; Humans; Hydroxylysine; Microbial Collagenase; Osteitis Deformans; Osteoarthritis; Osteoporosis; Protein Conformation; Rheumatic Diseases; Sclerosis; Synovial Membrane; Synovitis

Topics: Animals; Ascorbic Acid; Bacteria; Bone Diseases; Chemical Phenomena; Chemistry; Collagen; Collagen Diseases; Endocrine System Diseases; Glycosides; Humans; Hydroxylation; Hydroxylysine; Hydroxyproline; Isomerism; Peptide Hydrolases; Plants; Polyribosomes; Procollagen-Proline Dioxygenase; Proline; Protein Precursors

Osteoarthrosis was induced in one knee joint of dogs by an established surgical procedure. Changes in the articular cartilage in the biosynthesis of collagen and other proteins were sought by radiochemical labelling in vivo, with the following findings. (1) Collagen synthesis was stimulated in all cartilage surfaces of the experimental joints at 2, 8 and 24 weeks after surgery. Systemic labelling with [3H]proline showed that over 10 times more collagen was being deposited per dry weight of experimental cartilage compared with control cartilage in the unoperated knee. (2) Type-II collagen was the radiolabelled product in all samples of experimental cartilage ranging in quality from undamaged to overtly fibrillated, and was the only collagen detected chemically in the matrix of osteoarthrotic cartilage from either dog or human joints. (3) Hydroxylysine glycosylation was examined in the newly synthesized cartilage collagen by labelling dog joints in vivo with [3H]lysine. In experimental knees the new collagen was less glycosylated than in controls. However, no difference in glycosylation of the total collagen in the tissues was observed by chemical analysis. (4) Over half the protein-bound tritium was extracted by 4 M-guanidinium chloride from control cartilage labelled with [3H]proline, compared with one-quarter or less from experimental cartilage. Two-thirds of the extracted tritium separated in the upper fraction on density-gradient centrifugation in CsCl under associative conditions. Much of this ran with a single protein band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis under reducing conditions. The identity of this protein was unknown, although it resembled serum albumin in mobility afte disulphide-bond cleavage.

Topics: Animals; Bone Diseases; Cartilage, Articular; Chromatography, DEAE-Cellulose; Collagen; Dogs; Electrophoresis, Polyacrylamide Gel; Female; Humans; Hydroxylysine; Joint Diseases; Proline; Protein Biosynthesis; Time Factors

Free hydroxylysine and hydroxylysing glycosides were separated from urine and serum extracts on cation exchange resin and assayed spectrophotometrically. The method in conjunction with gel filtration in Bio-Gel P2 allowed to separate from urine also polypeptide hydroxylysine and hydroxylysine bound in small molecules of neutral or acidic character. Glycosylgalactosylhydroxylysineand galactosylhydroxylysine were separated by partition and/or ion exchange chromatography. Patients with chronic renal insufficiency had elevated serum levels and urinary excretion of hydroxylysine glycosides with increased excretion of hydroxylysine bound in polypeptides and in small molecules of neutral or acidic character. The excretion of free hydroxylysine was often within normal limits. When compared to values found in normal growing subjects and in adult patients with increased bone turnover and normal renin function the urinary excretion of hydroxylysine glycosides in chronic uremia was more markedly increased than excretion of hydroxyproline polypeptides and total hydroxyproline.

Topics: Bone Diseases; Chemical Fractionation; Chronic Disease; Collagen; Glycosides; Humans; Hydroxylysine; Uremia

Topics: Bone Diseases; Collagen; Collagen Diseases; Female; Humans; Hydroxylysine; Hydroxyproline; Inflammation; Liver Diseases; Male; Sex Factors; Skin Diseases; Thyroid Diseases

Topics: Adult; Bone Diseases; Calcitonin; Chromatography, Ion Exchange; Creatinine; Disaccharides; Female; Galactose; Glycosides; Glycosuria; Humans; Hydroxylysine; Hyperparathyroidism; Male; Monosaccharides; Osteitis Deformans; Osteomalacia; Parathyroid Glands; Protein Binding; Skin Diseases

Topics: Bone Diseases; Bone Matrix; Glycosaminoglycans; Humans; Hydroxylysine; Hydroxyproline; Kidney; Lysine; Ossification, Heterotopic; Osteitis Deformans; Osteomalacia; Osteoporosis; Proline; Renal Aminoacidurias