Integrin alpha(2)-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen
Integrin alpha(2)-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen
The integrin 2-subunit was ablated in mice by targeted deletion of the ITGA2 gene. 2-Deficient animals develop normally, are fertile, and reproduce. Surprisingly, no obvious anatomical or histological differences were observed in mutant mice. Besides its significance in tissue morphogenesis, integrin 21 has been reported to play a major role in hemostasis by mediating platelet adhesion and activation on subendothelial collagen. To define its role in hemostasis, 2-deficient platelets were analyzed for their capacity to adhere to and aggregate in response to fibrillar or soluble collagen type I. We show that aggregation of 2-deficient platelets to fibrillar collagen is delayed but not reduced, whereas aggregation to enzymatically digested soluble collagen is abolished. Furthermore, 2-deficient platelets normally adhere to fibrillar collagen. However, in the presence of an antibody against GPVI (activating platelet collagen receptor), adhesion of 2-deficient but not wild type platelets is abrogated. These results demonstrate that integrin 21 significantly contributes to platelet adhesion to (fibrillar) collagen, which is further confirmed by the abolished adhesion of 2-deficient platelets to soluble collagen. Thus, 21 plays a supportive rather than an essential role in platelet-collagen interactions. These results are in agreement with the observation that 21-deficient animals suffer no bleeding anomalies.
10789-10794
Holtkotter, O.
3ad9f09d-cecb-418d-b812-c16ef2b5defd
Nieswandt, B.
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Smyth, N.
0eba2a40-3b43-4d40-bb64-621bd7e9d505
Muller, M.
359678c4-5d02-4ef8-b381-f31238f339d1
Hafner, M.
07c05f69-a9ef-4b5e-b771-2acecbb8a671
Schulte, V.
32a404bf-48a5-4634-b931-041a3bfda75d
Krieg, T.
7b2f2d7d-77df-4252-8629-53da67afe4cd
Eckes, B.
7734e7c5-bfcf-45af-bc31-d2c662f713ff
1 March 2002
Holtkotter, O.
3ad9f09d-cecb-418d-b812-c16ef2b5defd
Nieswandt, B.
7f48a7f0-057a-4c51-b405-598035e14e70
Smyth, N.
0eba2a40-3b43-4d40-bb64-621bd7e9d505
Muller, M.
359678c4-5d02-4ef8-b381-f31238f339d1
Hafner, M.
07c05f69-a9ef-4b5e-b771-2acecbb8a671
Schulte, V.
32a404bf-48a5-4634-b931-041a3bfda75d
Krieg, T.
7b2f2d7d-77df-4252-8629-53da67afe4cd
Eckes, B.
7734e7c5-bfcf-45af-bc31-d2c662f713ff
Holtkotter, O., Nieswandt, B., Smyth, N., Muller, M., Hafner, M., Schulte, V., Krieg, T. and Eckes, B.
(2002)
Integrin alpha(2)-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen.
The Journal of Biological Chemistry, 277 (13), .
(doi:10.1074/jbc.M112307200).
Abstract
The integrin 2-subunit was ablated in mice by targeted deletion of the ITGA2 gene. 2-Deficient animals develop normally, are fertile, and reproduce. Surprisingly, no obvious anatomical or histological differences were observed in mutant mice. Besides its significance in tissue morphogenesis, integrin 21 has been reported to play a major role in hemostasis by mediating platelet adhesion and activation on subendothelial collagen. To define its role in hemostasis, 2-deficient platelets were analyzed for their capacity to adhere to and aggregate in response to fibrillar or soluble collagen type I. We show that aggregation of 2-deficient platelets to fibrillar collagen is delayed but not reduced, whereas aggregation to enzymatically digested soluble collagen is abolished. Furthermore, 2-deficient platelets normally adhere to fibrillar collagen. However, in the presence of an antibody against GPVI (activating platelet collagen receptor), adhesion of 2-deficient but not wild type platelets is abrogated. These results demonstrate that integrin 21 significantly contributes to platelet adhesion to (fibrillar) collagen, which is further confirmed by the abolished adhesion of 2-deficient platelets to soluble collagen. Thus, 21 plays a supportive rather than an essential role in platelet-collagen interactions. These results are in agreement with the observation that 21-deficient animals suffer no bleeding anomalies.
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Published date: 1 March 2002
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Local EPrints ID: 56332
URI: http://eprints.soton.ac.uk/id/eprint/56332
ISSN: 0021-9258
PURE UUID: 9b972794-33fb-4daa-abd0-7854a4f5c4a3
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Date deposited: 07 Aug 2008
Last modified: 15 Mar 2024 11:01
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Author:
O. Holtkotter
Author:
B. Nieswandt
Author:
M. Muller
Author:
M. Hafner
Author:
V. Schulte
Author:
T. Krieg
Author:
B. Eckes
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