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来自正常骨髓的髓系和红系祖细胞会黏附于I型胶原。

Myeloid and erythroid progenitor cells from normal bone marrow adhere to collagen type I.

作者信息

Koenigsmann M, Griffin J D, DiCarlo J, Cannistra S A

机构信息

Division of Tumor Immunology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA.

出版信息

Blood. 1992 Feb 1;79(3):657-65.

PMID:1370640
Abstract

One of the mechanisms by which normal hematopoietic progenitor cells remain localized within the bone marrow microenvironment is likely to involve adhesion of these cells to extracellular matrix (ECM) proteins. For example, there is evidence that uncommitted, HLA-DR-negative progenitor cells and committed erythroid precursors (BFU-E) bind to fibronectin. However, fibronectin is not known to mediate binding of committed myeloid (granulocyte-macrophage) progenitors, raising the possibility that other ECM proteins may be involved in this process. We investigated the binding of the MO7 myeloid cell line to a variety of ECM proteins and observed significant specific binding to collagen type I (56% +/- 5%), minimal binding to fibronectin (18% +/- 4%) or to laminin (19% +/- 5%), and no binding to collagen type III, IV, or V. Similarly, normal bone marrow myeloid progenitor cells (CFU-GM) demonstrated significant specific binding to collagen type I (46% +/- 8% and 47% +/- 12% for day 7 CFU-GM and day 14 CFU-GM, respectively). The ability of collagen to mediate binding of progenitor cells was not restricted to the myeloid lineage, as BFU-E also showed significant binding to this ECM protein (40% +/- 10%). The binding of MO7 cells and CFU-GM was collagen-mediated, as demonstrated by complete inhibition of adherence after treatment with collagenase type VII, which was shown to specifically degrade collagen. Binding was not affected by anti-CD29 neutralizing antibody (anti-beta-1 integrin), the RGD-containing peptide sequence GRGDTP, or divalent cation chelation, suggesting that collagen binding is not mediated by the beta-1 integrin class of adhesion proteins. Finally, mature peripheral blood neutrophils and monocytes were also found to bind to collagen type I (25% +/- 8% and 29% +/- 6%, respectively). These data suggest that collagen type I may play a role in the localization of committed myeloid and erythroid progenitors within the bone marrow microenvironment.

摘要

正常造血祖细胞定位于骨髓微环境的机制之一可能涉及这些细胞与细胞外基质(ECM)蛋白的黏附。例如,有证据表明未定向的、HLA-DR阴性祖细胞和定向的红系前体细胞(BFU-E)可与纤连蛋白结合。然而,纤连蛋白并不介导定向髓系(粒细胞-巨噬细胞)祖细胞的结合,这就增加了其他ECM蛋白可能参与此过程的可能性。我们研究了MO7髓系细胞系与多种ECM蛋白的结合情况,发现其与I型胶原存在显著的特异性结合(56%±5%),与纤连蛋白(18%±4%)或层粘连蛋白(19%±5%)的结合极少,与III型、IV型或V型胶原无结合。同样,正常骨髓髓系祖细胞(CFU-GM)也显示出与I型胶原的显著特异性结合(第7天的CFU-GM和第14天的CFU-GM分别为46%±8%和47%±12%)。胶原介导祖细胞结合的能力并不局限于髓系谱系,因为BFU-E也显示出与这种ECM蛋白的显著结合(40%±10%)。用VII型胶原酶处理后黏附完全被抑制,证明MO7细胞和CFU-GM的结合是由胶原介导的,VII型胶原酶可特异性降解胶原。结合不受抗CD29中和抗体(抗β-1整合素)、含RGD肽序列GRGDTP或二价阳离子螯合的影响,这表明胶原结合不是由β-1整合素类黏附蛋白介导的。最后,还发现成熟外周血中性粒细胞和单核细胞也可与I型胶原结合(分别为25%±8%和29%±6%)。这些数据表明I型胶原可能在定向髓系和红系祖细胞于骨髓微环境中的定位中发挥作用。

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