The 29-kDa proteins phosphorylated ion thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein
Journal Article
·
· Proceedings of the National Academy of Sciences of the United States of America; (United States)
- Harvard Medical School, Boston, MA (United States)
Thrombin plays a critical role in platelet activation, hemostasis, and thrombosis. Cellular activation by thrombin leads to the phosphorylation of multiple proteins, most of which are unidentified. The authors have characterized several 29-kDa proteins that are rapidly phosphorylated following exposure of intact human platelets to thrombin. A murine monoclonal antibody raised to an unidentified estrogen receptor-related 29-kDa protein selectively recognized these proteins as well as a more basic, unphosphorylated 27-kDa protein. Cellular activation by thrombin led to a marked shift in the proportion of protein from the 27-kDa unphosphorylated form to the 29-kDa phosphoprotein species. Using this antibody, they isolated and sequenced a human cDNA clone encoding a protein that was identical to the mammalian 27-kDa heat shock protein (HSP27), a protein of uncertain function that is known to be phosphorylated to several forms and to be transcriptionally induced by estrogen. The 29-kDa proteins were confirmed to be phosphorylated forms of HSP27 by immunoprecipitation studies. Thus, the estrogen receptor-related protein is HSP27, and the three major 20-kDa proteins phosphorylated in thrombin-activated platelets are forms of HSP27. These data suggest a role for HSP27 in the signal transduction events of platelet activation.
- OSTI ID:
- 5823148
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 88:24; ISSN 0027-8424; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL EFFECTS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD COAGULATION FACTORS
BLOOD PLATELETS
BODY FLUIDS
CARDIOVASCULAR DISEASES
CHEMICAL REACTIONS
COAGULANTS
DAYS LIVING RADIOISOTOPES
DISEASES
DNA
DNA SEQUENCING
DRUGS
ELECTROPHORESIS
ENZYMES
ESTROGENS
HEMATOLOGIC AGENTS
HEMOSTATICS
HORMONES
HYDROLASES
ISOTOPES
LIGHT NUCLEI
MAMMALS
MAN
MATERIALS
MEMBRANE PROTEINS
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PHOSPHORYLATION
PRIMATES
PROTEINS
RADIOISOTOPES
RECEPTORS
RECOMBINANT DNA
SERINE PROTEINASES
STEROID HORMONES
STRUCTURAL CHEMICAL ANALYSIS
THROMBIN
THROMBOSIS
TWO-DIMENSIONAL ELECTROPHORESIS
VASCULAR DISEASES
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL EFFECTS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD COAGULATION FACTORS
BLOOD PLATELETS
BODY FLUIDS
CARDIOVASCULAR DISEASES
CHEMICAL REACTIONS
COAGULANTS
DAYS LIVING RADIOISOTOPES
DISEASES
DNA
DNA SEQUENCING
DRUGS
ELECTROPHORESIS
ENZYMES
ESTROGENS
HEMATOLOGIC AGENTS
HEMOSTATICS
HORMONES
HYDROLASES
ISOTOPES
LIGHT NUCLEI
MAMMALS
MAN
MATERIALS
MEMBRANE PROTEINS
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PHOSPHORYLATION
PRIMATES
PROTEINS
RADIOISOTOPES
RECEPTORS
RECOMBINANT DNA
SERINE PROTEINASES
STEROID HORMONES
STRUCTURAL CHEMICAL ANALYSIS
THROMBIN
THROMBOSIS
TWO-DIMENSIONAL ELECTROPHORESIS
VASCULAR DISEASES
VERTEBRATES