PMID- 12091056
OWN - NLM
STAT- MEDLINE
DCOM- 20030304
LR  - 20190727
IS  - 0049-3848 (Print)
IS  - 0049-3848 (Linking)
VI  - 105
IP  - 6
DP  - 2002 Mar 15
TI  - Antithrombin and first complement protein recognize the same active heparin 
      fraction.
PG  - 537-41
AB  - Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a 
      specific pentasaccharide sequence. Heparin also regulates complement activity on 
      the classical and the alternative pathways. Most experimental pieces of evidence 
      accumulated show that these important activities reside in different segments of 
      the heparin molecule. We demonstrated in previous papers that a low ionic 
      strength and the presence of calcium ions are essential to detect specific 
      interactions between glycosaminoglycans and proteins. Then these very strict 
      conditions were used, and we demonstrated that the first protein complex of the 
      human complement cascade recognizes in the UFH a fraction with very high 
      anticoagulant activity. After isolation from the precipitate of the interaction, 
      this fraction of heparin also contained the pentasaccharide sequence responsible 
      for the great affinity with AT: in fact, it was strongly bound to a resin of AT 
      agarose, and to detach it, an ionic strength of 0.6 M sodium chloride was 
      required. In this way, the heparin regions responsible for the anticoagulant 
      activity and also for the effects over the complement system were identified on 
      the same short segment of the heparin molecule, which includes the active 
      fraction of the glycosaminoglycan. The differences with early results could be 
      explained by our experimental conditions of low ionic strength and the presence 
      of calcium ions used for the interaction of the protein and the 
      glycosaminoglycan.
FAU - Calabrese, Graciela C
AU  - Calabrese GC
AD  - Departamento de Ciencias Biologicas, Facultad de Farmacia y Bioquimica, 
      Universidad de Buenos Aires, Junin 954/956 Buenos Aires 1110, Argentina. 
      gcalebe@ffyb.uba.ar
FAU - Recondo, Eduardo F
AU  - Recondo EF
FAU - Fernandez de Recondo, Marta E
AU  - Fernandez de Recondo ME
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Thromb Res
JT  - Thrombosis research
JID - 0326377
RN  - 0 (Anticoagulants)
RN  - 0 (Complement C1)
RN  - 9000-94-6 (Antithrombin III)
RN  - 9005-49-6 (Heparin)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Anticoagulants/isolation & purification/metabolism/pharmacology
MH  - Antithrombin III/*metabolism
MH  - Binding Sites
MH  - Calcium
MH  - Chemical Precipitation
MH  - Chromatography, Affinity
MH  - Complement C1/*metabolism
MH  - Heparin/isolation & purification/*metabolism/pharmacology
MH  - Humans
MH  - Osmolar Concentration
MH  - Protein Binding
EDAT- 2002/07/02 10:00
MHDA- 2003/03/05 04:00
CRDT- 2002/07/02 10:00
PHST- 2002/07/02 10:00 [pubmed]
PHST- 2003/03/05 04:00 [medline]
PHST- 2002/07/02 10:00 [entrez]
AID - S0049384802000622 [pii]
AID - 10.1016/s0049-3848(02)00062-2 [doi]
PST - ppublish
SO  - Thromb Res. 2002 Mar 15;105(6):537-41. doi: 10.1016/s0049-3848(02)00062-2.