Osteopontin (OPN), a multifunctional acidic glycoprotein, expressed by osteoblasts within the endosteal region of the bone marrow (BM) suppresses the proliferation of hemopoietic stem and progenitor cells and also regulates their lodgment within the BM after transplantation. Herein we demonstrate that OPN cleavage fragments are the most abundant forms of this protein within the BM. Studies aimed to determine how hemopoietic stem cells (HSCs) interact with OPN revealed for the first time that murine and human HSCs express α9β1 integrin. The N-terminal thrombin cleavage fragment of OPN through its binding to the α9β 1 and α4β1 integrins plays a key role in the attraction, retention, regulation, and release of hemopoietic stem and progenitor cells to, in, and from their BM niche. Thrombin-cleaved OPN (trOPN) acts as a chemoattractant for stem and progenitor cells, mediating their migration in a manner that involves interaction with α9β 1 and α4β1 integrins. In addition, in the absence of OPN, there is an increased number of white blood cells and, specifically, stem and progenitor cells in the peripheral circulation.
Febrile Neutropenia Risk Assesment and Granulocyte-Colony Stimulating Factor Support in Patients with Diffuse Large B Cell Lymphoma Receiving R-CHOP Regimens / A. Salar, C. Haioun, F. Rossi, U. Duehrsen, R. Pettengel, H.E. Johnsen, U. Jaeger, G. Verhoef, M. Schwenkglenks, F. Principe, P. Bacon, K. Bendall, P.J. Lugtemburg. - In: BLOOD. - ISSN 0006-4971. - 114:22(2009), pp. 49-50. ((Intervento presentato al 51. convegno Annual meeting of the American society of hematology tenutosi a New Orleans nel 2009.
Febrile Neutropenia Risk Assesment and Granulocyte-Colony Stimulating Factor Support in Patients with Diffuse Large B Cell Lymphoma Receiving R-CHOP Regimens
F. Rossi;
2009
Abstract
Osteopontin (OPN), a multifunctional acidic glycoprotein, expressed by osteoblasts within the endosteal region of the bone marrow (BM) suppresses the proliferation of hemopoietic stem and progenitor cells and also regulates their lodgment within the BM after transplantation. Herein we demonstrate that OPN cleavage fragments are the most abundant forms of this protein within the BM. Studies aimed to determine how hemopoietic stem cells (HSCs) interact with OPN revealed for the first time that murine and human HSCs express α9β1 integrin. The N-terminal thrombin cleavage fragment of OPN through its binding to the α9β 1 and α4β1 integrins plays a key role in the attraction, retention, regulation, and release of hemopoietic stem and progenitor cells to, in, and from their BM niche. Thrombin-cleaved OPN (trOPN) acts as a chemoattractant for stem and progenitor cells, mediating their migration in a manner that involves interaction with α9β 1 and α4β1 integrins. In addition, in the absence of OPN, there is an increased number of white blood cells and, specifically, stem and progenitor cells in the peripheral circulation.
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