Identification of protein tyrosine phosphatases associating with the PDGF receptor
Markova, Boyka ; Herrlich, Peter ; Rönnstrand, Lars LU
and Bohmer, Frank-D
(2003)
In Biochemistry
42(9).
p.2691-2699
- Abstract
- Protein tyrosine phosphatase (PTP) in-gel assays were used to explore association of PTPs with the platelet-derived growth factor beta-receptor (PDGFbetaR). Five PTP activity bands of approximately 120, approximately 70, approximately 60, approximately 53, and approximately 45 kDa could be detected in PDGFbetaR immunoprecipitates and were identified by immunodepletion experiments as PTP-PEST, SHP-2, an active fragment of SHP-2, PTP-1B, and T-cell PTP, respectively. The PTP pattern that was obtained was similar in PDGFbetaR immunoprecipitates from HEK 293 cells overexpressing the human PDGFbetaR and from murine fibroblasts. Association of PTP-1B with the PDGFbetaR was stabilized by pretreatment of the cells with hydrogen peroxide. The... (More)
- Protein tyrosine phosphatase (PTP) in-gel assays were used to explore association of PTPs with the platelet-derived growth factor beta-receptor (PDGFbetaR). Five PTP activity bands of approximately 120, approximately 70, approximately 60, approximately 53, and approximately 45 kDa could be detected in PDGFbetaR immunoprecipitates and were identified by immunodepletion experiments as PTP-PEST, SHP-2, an active fragment of SHP-2, PTP-1B, and T-cell PTP, respectively. The PTP pattern that was obtained was similar in PDGFbetaR immunoprecipitates from HEK 293 cells overexpressing the human PDGFbetaR and from murine fibroblasts. Association of PTP-1B with the PDGFbetaR was stabilized by pretreatment of the cells with hydrogen peroxide. The epidermal growth factor receptor (EGFR) immunoprecipitated from fibroblasts, and c-Kit isolated from CHRF myeloid cells, were associated with partially overlapping but quantitatively different patterns of PTPs. PTP-PEST was the predominant PTP in EGFR immunoprecipitates, and SHP-1 appeared in c-Kit immunoprecipitates. We propose that the differential association of PTPs with different RTKs is related to their respective contributions to regulation of RTK signaling. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1126199
- author
- Markova, Boyka
; Herrlich, Peter
; Rönnstrand, Lars
LU
and Bohmer, Frank-D
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemistry
- volume
- 42
- issue
- 9
- pages
- 2691 - 2699
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:12614164
- scopus:0242585485
- pmid:12614164
- ISSN
- 0006-2960
- DOI
- 10.1021/bi0265574
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
- id
- abe8ab34-738b-46ca-8ead-72574d443396 (old id 1126199)
- date added to LUP
- 2016-04-01 11:32:43
- date last changed
- 2022-04-12 22:02:04
@article{abe8ab34-738b-46ca-8ead-72574d443396,
abstract = {{Protein tyrosine phosphatase (PTP) in-gel assays were used to explore association of PTPs with the platelet-derived growth factor beta-receptor (PDGFbetaR). Five PTP activity bands of approximately 120, approximately 70, approximately 60, approximately 53, and approximately 45 kDa could be detected in PDGFbetaR immunoprecipitates and were identified by immunodepletion experiments as PTP-PEST, SHP-2, an active fragment of SHP-2, PTP-1B, and T-cell PTP, respectively. The PTP pattern that was obtained was similar in PDGFbetaR immunoprecipitates from HEK 293 cells overexpressing the human PDGFbetaR and from murine fibroblasts. Association of PTP-1B with the PDGFbetaR was stabilized by pretreatment of the cells with hydrogen peroxide. The epidermal growth factor receptor (EGFR) immunoprecipitated from fibroblasts, and c-Kit isolated from CHRF myeloid cells, were associated with partially overlapping but quantitatively different patterns of PTPs. PTP-PEST was the predominant PTP in EGFR immunoprecipitates, and SHP-1 appeared in c-Kit immunoprecipitates. We propose that the differential association of PTPs with different RTKs is related to their respective contributions to regulation of RTK signaling.}},
author = {{Markova, Boyka and Herrlich, Peter and Rönnstrand, Lars and Bohmer, Frank-D}},
issn = {{0006-2960}},
language = {{eng}},
number = {{9}},
pages = {{2691--2699}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biochemistry}},
title = {{Identification of protein tyrosine phosphatases associating with the PDGF receptor}},
url = {{http://dx.doi.org/10.1021/bi0265574}},
doi = {{10.1021/bi0265574}},
volume = {{42}},
year = {{2003}},
}