CHAPTER 23 – Products of Bone Collagen Metabolism
作者： JUHA RISTELI , LEILA RISTELI
DOI: 10.1016/B978-012088562-6/50024-8
关键词:
摘要: It has been a challenge for researchers to assess the balance between bone collagen synthesis and degradation by simultaneous measurement of metabolic products related these two processes. There are possible analytes type I collagen, carboxyterminal (PICP) amino-terminal (PINP) propeptides procollagen; respective assay methods already quite well established. is great deal clinical experience on their performance in different physiological pathological situations. Although general both give relevant information synthesis, some situations intact PINP seems be superior that PICP. The picture cleared recent research, with clarification roles cathepsin K matrix metalloproteinase pathways. However, number more specific questions remain, further fates primary products, breakdown helical domain, or origins free forms cross-links. Much gained using urine samples, but present trend towards serum assays.
sci-hub.st 参考文章(87)
B Smedsrød, H Pertoft, S Gustafson, T C Laurent, Scavenger functions of the liver endothelial cell. Biochemical Journal. ,vol. 266, pp. 313- 327 ,(1990) , 10.1042/BJ2660313
M Raccurt, S Peyrol, F Gerard, J A Grimaud, C Gleyzal, P Sommer, Lysyl oxidase gene expression in the stromal reaction to in situ and invasive ductal breast carcinoma American Journal of Pathology. ,vol. 150, pp. 497- 507 ,(1997)
Shireen R. Lamand, John F. Bateman, The type I collagen pro alpha 1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis. Journal of Biological Chemistry. ,vol. 270, pp. 17858- 17865 ,(1995) , 10.1074/JBC.270.30.17858
D R Sell, V M Monnier, Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process Journal of Biological Chemistry. ,vol. 264, pp. 21597- 21602 ,(1989) , 10.1016/S0021-9258(20)88225-8
C.C. Clark, The distribution and initial characterization of oligosaccharide units on the COOH-terminal propeptide extensions of the pro-alpha 1 and pro-alpha 2 chains of type I procollagen. Journal of Biological Chemistry. ,vol. 254, pp. 10798- 10802 ,(1979) , 10.1016/S0021-9258(19)86592-4
D J Hartmann, J C Trinchet, S Ricard-Blum, M Beaugrand, P Callard, G Ville, Radioimmunoassay of type I collagen that mainly detects degradation products in serum: application to patients with liver diseases. Clinical Chemistry. ,vol. 36, pp. 421- 426 ,(1990) , 10.1093/CLINCHEM/36.3.421
J Melkko, S Niemi, L Risteli, J Risteli, Radioimmunoassay of the carboxyterminal propeptide of human type I procollagen. Clinical Chemistry. ,vol. 36, pp. 1328- 1332 ,(1990) , 10.1093/CLINCHEM/36.7.1328
Riitta Tähtelä, Juha Risteli, Leila Risteli, Klaus Vuorinen, Eric Thölix, Arja Jukkola, Guillermo Blanco, Aggressive breast cancer leads to discrepant serum levels of the type I procollagen propeptides PINP and PICP. Cancer Research. ,vol. 57, pp. 5517- 5520 ,(1997)
B J Pedersen, M Bonde, Purification of human procollagen type I carboxyl-terminal propeptide cleaved as in vivo from procollagen and used to calibrate a radioimmunoassay of the propeptide. Clinical Chemistry. ,vol. 40, pp. 811- 816 ,(1994) , 10.1093/CLINCHEM/40.5.811
A Sorva, R Tähtelä, J Risteli, L Risteli, K Laitinen, K Juntunen-Backman, R Sorva, Familial high serum concentrations of the carboxyl-terminal propeptide of type I procollagen. Clinical Chemistry. ,vol. 40, pp. 1591- 1593 ,(1994) , 10.1093/CLINCHEM/40.8.1591