PMID- 15050904
OWN - NLM
STAT- MEDLINE
DCOM- 20041222
LR  - 20061115
IS  - 8756-3282 (Print)
IS  - 1873-2763 (Linking)
VI  - 34
IP  - 4
DP  - 2004 Apr
TI  - Differently cross-linked and uncross-linked carboxy-terminal telopeptides of type 
      I collagen in human mineralised bone.
PG  - 720-7
AB  - In bone matrix, type I collagen is stabilised by covalent cross-links formed 
      between adjacent collagen molecules; the majority of which is believed to be 
      immature, divalent bonds. For studying these immature forms in detail, we have 
      developed an immunoassay for a synthetic peptide SP 4 that is analogous with and 
      detects a linear epitope within the C-telopeptide of alpha1-chain of type I 
      collagen. The SP 4 assay, together with the ICTP assay, which is specific for the 
      trivalently cross-linked C-telopeptide, was used for the isolation of the 
      differently cross-linked C-telopeptide structures of the alpha1-chain of type I 
      collagen present in mineralised human bone. Amino acid analysis, peptide 
      sequencing and MALDI-TOF mass spectrometry were used to identify and characterise 
      each of the isolated structures. The cross-link content of each isolated peptide 
      was identified. In the trivalent ICTP peptide, only 40% was cross-linked with 
      pyridinoline, the remainder of the cross-links being currently uncharacterized. 
      The divalent peptides contained only previously characterised cross-linking 
      structures. Most of the divalent cross-links were dihydroxylysinonorleucine 
      (DHLNL), with minor amounts of hydroxylysinonorleucine (HLNL). The relative 
      proportion of the HLNL cross-link was slightly higher in the divalent 
      alpha1Calpha2H peptide. A substantial amount of uncross-linked telopeptide 
      structures was also found. Previous studies, where direct chemical cross-link 
      analyses have been used to assess the maturity of cross-linking, have inferred 
      that bone contains more divalently than trivalently cross-linked C-telopeptides. 
      The immunochemical peptide approach used in this study may help to detect 
      presently uncharacterized, trivalent cross-links, the presence of which is 
      strongly suggested in this study. It also provides additional information 
      regarding the extent and maturity of tissue type I collagen cross-linking in 
      health and disease.
FAU - Eriksen, Heidi A
AU  - Eriksen HA
AD  - Department of Clinical Chemistry, University of Oulu, Finland. 
      heidi.eriksen@oulu.fi
FAU - Sharp, Christopher A
AU  - Sharp CA
FAU - Robins, Simon P
AU  - Robins SP
FAU - Sassi, Mirja-Liisa
AU  - Sassi ML
FAU - Risteli, Leila
AU  - Risteli L
FAU - Risteli, Juha
AU  - Risteli J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Bone
JT  - Bone
JID - 8504048
RN  - 0 (Collagen Type I)
RN  - 0 (Peptides)
RN  - 0 (collagen type I trimeric cross-linked peptide)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Amino Acid Sequence
MH  - Calcification, Physiologic/*physiology
MH  - Chromatography, High Pressure Liquid
MH  - Collagen/chemistry/isolation & purification/*metabolism
MH  - Collagen Type I/chemistry/*metabolism
MH  - Female
MH  - Glycosylation
MH  - Humans
MH  - Immunoassay
MH  - Male
MH  - Middle Aged
MH  - Molecular Sequence Data
MH  - Peptides/chemistry/isolation & purification/*metabolism
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
EDAT- 2004/03/31 05:00
MHDA- 2004/12/23 09:00
CRDT- 2004/03/31 05:00
PHST- 2003/07/18 00:00 [received]
PHST- 2003/11/07 00:00 [revised]
PHST- 2003/12/09 00:00 [accepted]
PHST- 2004/03/31 05:00 [pubmed]
PHST- 2004/12/23 09:00 [medline]
PHST- 2004/03/31 05:00 [entrez]
AID - S875632820300468X [pii]
AID - 10.1016/j.bone.2003.12.009 [doi]
PST - ppublish
SO  - Bone. 2004 Apr;34(4):720-7. doi: 10.1016/j.bone.2003.12.009.