Identical or Overlapping Sequences in the Primary Structure of Human α2-Macroglobulin Are Responsible for the Binding of Nerve Growth Factor-β, Platelet-derived Growth Factor-BB, and Transforming Growth Factor-β

Gonias, Steven L.; Carmichael, Aliya; Mettenburg, Joseph; Roadcap, David W.; Irvin, William P.; Webb, Donna J.

doi:10.1074/jbc.275.8.5826

Cited by 49 publications

(55 citation statements)

References 54 publications

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“…In certain cases, such as TGF-β1 and PDGF, both the biochemical interaction of these molecules with α 2 M and the ability of α 2 M to regulate their function have been extensively studied (12,14,16,17,43,44). With regards to VEGF, an earlier study demonstrated that radiolabeled VEGF added to human plasma coprecipitates with α 2 M (22).…”

Section: Discussionmentioning

confidence: 99%

“…Numerous cytokines and growth factors are known to bind to α 2 M and α 2 M-MA, including transforming growth factor beta (TGF-β), types 1 (11,12) and 2 (13,14), platelet derived growth factor (PDGF) (15)(16)(17), nerve growth factor (NGF) (17,18), tumor necrosis factor alpha (TNF-α) (19), basic fibroblast growth factor (bFGF) (20), interleukin six (IL-6) (21), and vascular endothelial growth factor (VEGF) (22). In some cases, such as TGF-β1, the nature of the interaction is well investigated whereas in others, such as VEGF, the nature of the interaction is not well understood.…”

Section: Introductionmentioning

confidence: 99%

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The Conformation-Dependent Interaction of alpha sub2 -Macroglobulin with Vascular Endothelial Growth Factor: A Novel Mechanism of alpha sub2 -Macroglobulin/Growth Factor Binding

Bhattacharjee

Asplin

et al. 2000

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Conformation-Dependent Interaction of alpha sub2 -Macroglobulin with Vascular Endothelial Growth Factor: A Novel Mechanism of alpha sub2 -Macroglobulin/Growth Factor Binding

Bhattacharjee

Asplin

et al. 2000

Journal of Biological Chemistry

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“…Activated ␣ 2 M is rapidly internalized by endocytosis via binding to low density lipoprotein receptor-related protein-1 (Lrp1) (18). Notably, the ligand binding activity of ␣ 2 M is mediated by several binding sites, not only the bait region (13,(21)(22)(23).…”

mentioning

confidence: 99%

“…defensin (HNP1) (17), transforming growth factor-␤1/2, etc. (7)(8)(9)(10)(11)(12)(13)24). The consequence of these interactions with ␣ 2 M/␣ 2 M-MA can be passive (24) or stimulatory (10).…”

mentioning

confidence: 99%

“…The transport of hepcidin within the blood is of interest as: 1) many peptide hormones are bound by carriers that influence their function and distribution (7)(8)(9)(10)(11)(12)(13); 2) a greater understanding of the mechanism of hepcidin delivery to the cell could provide further information on its regulatory role; and 3) understanding the binding of hepcidin to a carrier protein would facilitate development of quantitative hepcidin assays.…”

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confidence: 99%

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Hepcidin Bound to α2-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Huang

Austin

Sari

et al. 2013

Journal of Biological Chemistry

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Background:Hepcidin is the hormone of iron metabolism that is bound by ␣ 2 -macroglobulin (␣ 2 M) and its activated counterpart (␣ 2 M-MA). Results: Serum iron is reduced to a greater extent in mice treated with ␣ 2 M⅐hepcidin or ␣ 2 M-MA⅐hepcidin relative to unbound hepcidin. Conclusion: ␣ 2 M retards hepcidin excretion by the kidney, increasing its efficacy. Significance: These results are important for understanding hepcidin transport and detection in blood.

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Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

2002

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Although many studies have focused on blood vessel development and new blood vessel formation associated with disease processes, the question of how endothelial cells (ECs) assemble into tubes in three dimensions (i.e., EC morphogenesis) remains unanswered. EC morphogenesis is particularly dependent on a signaling axis involving the extracellular matrix (ECM), integrins, and the cytoskeleton, which regulates EC shape changes and signals the pathways necessary for tube formation. Recent studies reveal that genes regulating this matrix-integrin-cytoskeletal (MIC) signaling axis are differentially expressed during EC morphogenesis. The Rho GTPases represent an important class of molecules involved in these events. Cdc42 and Rac1 are required for the process of EC intracellular vacuole formation and coalescence that regulates EC lumen formation in three-dimensional (3D) extracellular matrices, while RhoA appears to stabilize capillary tube networks. Once EC tube networks are established, supporting cells, such as pericytes, are recruited to further stabilize these networks, perhaps by regulating EC basement membrane matrix assembly. Furthermore, we consider recent work showing that EC morphogenesis is balanced by a tendency for newly formed tubes to regress. This morphogenesis-regression balance is controlled by differential gene expression of such molecules as VEGF, angiopoietin-2, and PAI-1, as well as a plasmin-and matrix metalloproteinase-dependent mechanism that induces tube regression through degradation of ECM scaffolds that support EC-lined tubes. It is our hope that this review will stimulate increased interest and effort focused on the basic mechanisms regulating capillary tube formation and regression in 3D extracellular matrices. Anat Rec 268: 252-275, 2002.

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Identical or Overlapping Sequences in the Primary Structure of Human α2-Macroglobulin Are Responsible for the Binding of Nerve Growth Factor-β, Platelet-derived Growth Factor-BB, and Transforming Growth Factor-β

Cited by 49 publications

References 54 publications

The Conformation-Dependent Interaction of alpha sub2 -Macroglobulin with Vascular Endothelial Growth Factor: A Novel Mechanism of alpha sub2 -Macroglobulin/Growth Factor Binding

The Conformation-Dependent Interaction of alpha sub2 -Macroglobulin with Vascular Endothelial Growth Factor: A Novel Mechanism of alpha sub2 -Macroglobulin/Growth Factor Binding

Hepcidin Bound to α2-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

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