Platelet type III collagen binding protein (TIIICBP) presents high biochemical and functional similarities with kindlin-3
| Autor: | Françoise Fauvel-Lafève, Valérie Labas, Samia Mourah, Joëlle Vinh, Monique Lemesle, Chantal Legrand, Ibtissem Djaafri, Pascal Maurice, Brigitte Arbeille |
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| Přispěvatelé: | Hemostase, Endothelium, Angiogenese (UMR_S_553), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Diderot - Paris 7 (UPD7), Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Centre National de la Recherche Scientifique (CNRS)-Université de Tours-Institut Français du Cheval et de l'Equitation [Saumur]-Institut National de la Recherche Agronomique (INRA), Unité de Spectrométrie de Masse Biologique et Protéomique, ESPCI ParisTech-Centre National de la Recherche Scientifique (CNRS), Plateforme des Microscopies, Université de Tours, Institut Universitaire d'Hématologie (IUH), Université Paris Diderot - Paris 7 (UPD7), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS), Spectrométrie de Masse Biologique et Protéomique (USR3149 / FRE2032) (SMBP), Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS), Neurobiologie et diversité cellulaire (NDC), Université de Tours (UT), Hématologie -Immunologie -Cibles thérapeutiques, Centre National de la Recherche Scientifique (CNRS)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2012 |
| Předmět: |
MESH: Neoplasm Proteins
MESH: Platelet Adhesiveness Platelet Aggregation MESH: Sequence Homology Amino Acid [SDV]Life Sciences [q-bio] MESH: Amino Acid Sequence Biochemistry Collagen receptor MESH: Thrombin 0302 clinical medicine Peptide sequence MESH: Blood Platelets MESH: Platelet Aggregation MESH: Collagen Type III 0303 health sciences biology Chemistry Thrombin Convulxin General Medicine Neoplasm Proteins 3. Good health Adenosine Diphosphate 030220 oncology & carcinogenesis MESH: Crotalid Venoms MESH: Membrane Proteins GPVI Blood Platelets Receptors Collagen Molecular Sequence Data Integrin Platelet Membrane Glycoproteins Antibodies 03 medical and health sciences Platelet Adhesiveness [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] Crotalid Venoms MESH: Platelet Activation Humans Immunoprecipitation Lectins C-Type Amino Acid Sequence Platelet activation 030304 developmental biology MESH: Molecular Sequence Data MESH: Humans MESH: Adenosine Diphosphate Sequence Homology Amino Acid MESH: Immunoprecipitation MESH: Antibodies Binding protein MESH: Platelet Membrane Glycoproteins Membrane Proteins Platelet Activation MESH: Receptors Collagen Molecular biology Collagen Type III Membrane protein biology.protein MESH: Lectins C-Type |
| Zdroj: | Biochimie Biochimie, Elsevier, 2012, 94 (2), pp.416-426. ⟨10.1016/j.biochi.2011.08.009⟩ Biochimie, Elsevier, 2012, 94 (2), pp.416-26. ⟨10.1016/j.biochi.2011.08.009⟩ |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/j.biochi.2011.08.009 |
| Popis: | International audience; Type III collagen binding protein (TIIICBP) was previously described as a platelet membrane protein that recognizes the KOGEOGPK peptide sequence within type III collagen. In order to better characterize this protein, we performed different approaches including mass spectrometry sequencing and functional experiments. This study leads to identify high biochemical and functional similarities between TIIICBP and kindlin-3, a member of a family of focal adhesion proteins. Indeed, mass spectrometry surveys indicated that TIIICBP contains several peptides identical to kindlin-3, covering 41% of the amino acid sequence. Polyclonal antibodies raised against a kindlin-3 specific N-terminal sequence, recognized and immunoprecipitated TIIICBP from platelet lysates. Electron microscopy and flow cytometry experiments showed that kindlin-3, as well as TIIICBP, were present associated to platelet membrane and a trans-location of cytosolic kindlin-3 to the platelet membrane was observed after platelet activation. Similarly to anti-TIIICBP antibodies and the KOGEOGPK peptide, anti-kindlin-3 antibodies inhibited platelet interactions with type III collagen under flow conditions and slowed down platelet aggregation induced by glycoprotein VI agonists; e.g. collagen-related peptides and convulxin. In addition, the anti-kindlin-3 antibody inhibited platelet aggregation induced by low e but not high e doses of ADP or thrombin which depends on a IIb b 3 integrin function. In conclusion, our results show that the peptides identified by mass spectrometry from purified TIIICBP correspond to the kindlin-3 protein and demonstrate biochemical and functional similarities between TIIICBP and kindlin-3, strengthening a key role for TIIICBP/kindlin-3 in platelet interactions with collagen by cooperating with glycoprotein VI activation and integrin clustering in focal adhesion complexes. |
| Databáze: | OpenAIRE |
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