PMID- 9468482
OWN - NLM
STAT- MEDLINE
DCOM- 19980319
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 8
DP  - 1998 Feb 20
TI  - Platelet adhesion to native type I collagen fibrils. Role of GPVI in divalent 
      cation-dependent and -independent adhesion and thromboxane A2 generation.
PG  - 4338-44
AB  - Three glycoproteins (GPs), namely GPIa-IIa, GPVI, and GPIV, have been recently 
      implicated in platelet-collagen adhesive interactions. We have employed 
      antibodies to these GPs to investigate further their role in platelet adhesion to 
      immobilized monomeric and polymeric fibrillar collagen under static conditions in 
      the presence and the absence of Mg2+. In the presence of Mg2+, each antibody 
      inhibited platelet adhesion to fibrillar collagen from 70 to 85%, especially 
      during the early phase (<15 min), but the inhibitory effects diminished 
      dramatically to 25% or less by 60 min. Combination of anti-GPVI with 
      anti-GPIa-IIa antibodies completely inhibited platelet adhesion at 60 min. 
      Anti-GPIV and anti-GPIa-IIa or anti-GPVI antibodies in combinations were more 
      effective in inhibiting adhesion than was anti-GPIa-IIa or anti-GPVI alone. In 
      the absence of Mg2+, anti-GPVI completely inhibited adhesion at 60 min, while 
      anti-GPIV antibody inhibited adhesion by about 50% and minimal effects were seen 
      with anti-GPIa-IIa, suggesting that GPIa-IIa does not play a significant role in 
      the divalent cation-independent platelet adhesion to immobilized fibrillar 
      collagen. Under either divalent cation-dependent or -independent conditions, 
      platelets adhered to fibrillar collagen were able to secrete contents of both 
      alpha-granules and dense granules and generate thromboxane A2 (TXA2), but 
      platelets adhering to acid soluble monomeric collagen neither secreted their 
      granular contents nor generated TXA2. Although anti-GPVI antibodies were not able 
      to inhibit Mg2+-dependent adhesion, they completely inhibited TXA2 generation 
      under both divalent cation-dependent and -independent conditions. With the other 
      antibodies, TXA2 generation corresponded with the amount of adhesion observed. 
      These results suggest that GPVI is directly associated with the TXA2 generating 
      system during platelet-collagen interaction.
FAU - Nakamura, T
AU  - Nakamura T
AD  - Otsuka America Pharmaceutical Inc., Rockville, Maryland 20850, USA.
FAU - Jamieson, G A
AU  - Jamieson GA
FAU - Okuma, M
AU  - Okuma M
FAU - Kambayashi, J
AU  - Kambayashi J
FAU - Tandon, N N
AU  - Tandon NN
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies)
RN  - 0 (Cations, Divalent)
RN  - 0 (Platelet Membrane Glycoproteins)
RN  - 0 (beta-Thromboglobulin)
RN  - 333DO1RDJY (Serotonin)
RN  - 37270-94-3 (Platelet Factor 4)
RN  - 57576-52-0 (Thromboxane A2)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Animals
MH  - Antibodies/immunology
MH  - Blood Platelets/*metabolism
MH  - Cations, Divalent
MH  - *Cell Adhesion/immunology
MH  - Collagen/*metabolism
MH  - Humans
MH  - Platelet Factor 4/metabolism
MH  - Platelet Membrane Glycoproteins/immunology
MH  - Rats
MH  - Serotonin/metabolism
MH  - Thromboxane A2/*biosynthesis
MH  - beta-Thromboglobulin/metabolism
EDAT- 1998/03/21 00:00
MHDA- 1998/03/21 00:01
CRDT- 1998/03/21 00:00
PHST- 1998/03/21 00:00 [pubmed]
PHST- 1998/03/21 00:01 [medline]
PHST- 1998/03/21 00:00 [entrez]
AID - S0021-9258(18)92554-8 [pii]
AID - 10.1074/jbc.273.8.4338 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 Feb 20;273(8):4338-44. doi: 10.1074/jbc.273.8.4338.