Fibronectin is a binding partner for the myelin‐associated glycoprotein (siglec‐4a)

Strenge, Karen; Brossmer, Reinhard; Ihrig, Petra; Schauer, Roland; Kelm, Sørge

doi:10.1016/s0014-5793(01)02566-2

Cited by 23 publications

(13 citation statements)

References 40 publications

(53 reference statements)

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“…Furthermore, MAG is physically associated with MUC1 in pancreatic tumor cells. These findings extend previous work defining sialoglycoproteins that interact with MAG, including fibronectin (43) and Nogo-66 receptor homologue NgR2 (44).…”

Section: Discussionsupporting

confidence: 89%

MUC1 Is a Counter-Receptor for Myelin-Associated Glycoprotein (Siglec-4a) and Their Interaction Contributes to Adhesion in Pancreatic Cancer Perineural Invasion

et al. 2007

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Perineural invasion in pancreatic adenocarcinoma, a common pathologic phenomenon whereby cancer cells invade and intimately contact the endoneurium of pancreatic nerves, is thought to contribute to both pain and local disease recurrence. MUC1, a type I transmembrane mucin that can affect the adhesive properties of cells, contains a large extracellular tandem repeat domain, which is heavily glycosylated in normal epithelia, but is overexpressed and differentially glycosylated in pancreatic cancer. This altered glycosylation includes the shortened core I O-glycans for monosialyl and disialyl T antigens. Myelin-associated glycoprotein (MAG), a membrane-bound protein expressed on oligodendrocytes and Schwann cells, binds myelin to neurons. MAG's preferred ligands are derivatives of the monosialyl and disialyl T antigen. We investigated whether MUC1 is a counterreceptor for MAG and if their interaction contributed to pancreatic perineural invasion. Results showed that MAG binds pancreatic cells expressing MUC1, that this binding is sialidase-sensitive, and that MAG physically associates with MUC1. Heterotypic adhesion assays between pancreatic cancer cells and Schwann cells revealed that increased expression of MUC1 or MAG enhanced adhesion. Conversely, specific inhibition of MAG or sialyl-T MUC1 partially blocked adhesion. Immunohistochemical analysis of pancreatic perineural invasion showed the expression of both MUC1 and MAG. These results support the hypothesis that the adhesive interactions between MUC1 and MAG are of biological significance in pancreatic cancer perineural invasion. [Cancer Res 2007;67(21):10222-9]

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Section: Discussionsupporting

confidence: 89%

MUC1 Is a Counter-Receptor for Myelin-Associated Glycoprotein (Siglec-4a) and Their Interaction Contributes to Adhesion in Pancreatic Cancer Perineural Invasion

et al. 2007

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“…Whether this is a reflection of MAG binding to a neuronal sialoglycoprotein or sialoglycoproteins or protein-ganglioside complexes, however, remains unknown. Although several MAG binding proteins have been characterized (Franzen et al, 2001;Strenge et al, 2001), NgR1 is the first binding protein directly shown to be part of a functional MAG receptor complex, yet the observation that MAG binding to NgR1 is VCN-insensitive and not modulated by the presence of GT1b adds an unexpected twist to the characterization of the neuronal MAG receptor (Domeniconi et al, 2002;Liu et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

The Nogo-66 Receptor Homolog NgR2 Is a Sialic Acid-Dependent Receptor Selective for Myelin-Associated Glycoprotein

et al. 2005

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The Nogo-66 receptor (NgR1) is a promiscuous receptor for the myelin inhibitory proteins Nogo/Nogo-66, myelin-associated glycoprotein (MAG), and oligodendrocyte myelin glycoprotein (OMgp). NgR1, an axonal glycoprotein, is the founding member of a protein family composed of the structurally related molecules NgR1, NgR2, and NgR3. Here we show that NgR2 is a novel receptor for MAG and acts selectively to mediate MAG inhibitory responses. MAG binds NgR2 directly and with greater affinity than NgR1. In neurons NgR1 and

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“…While the role of fibronectin in peripheral nerve myelination is not known, the production of fibronectin by Schwann cells correlates with differentiation to a myelinating state following nerve injury (Vogelezang et al 1999;Chernousov and Carey 2000). In the CNS, fibronectin is known to bind to myelin-associated glycoprotein (Strenge et al 2001), a key molecule in axoglial interactions. Although we have not investigated the possibility, the degradation of fibronectin in TrJ nerves may similarly impair support afforded by contacts between fibronectin and myelin-associated glycoprotein.…”

Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinase mediated degradation of basement membrane proteins in Trembler J neuropathy nerves

Misko

Ferguson

Notterpek

2002

Journal of Neurochemistry

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A single point mutation in peripheral myelin protein 22 (pmp22) of the Trembler-J (TrJ) mouse models the human peripheral neuropathy, Charcot-Marie-Tooth disease type 1 A (CMT1A). An unexplored aspect of this disease is the gradual remodeling of the extracellular matrix in affected nerves. To elucidate the mechanism responsible for these changes, the levels of the extracellular matrix molecules laminin, collagen IV, and fibronectin were determined. In TrJ nerves, laminin is modestly increased while full-length forms of collagen IV and fibronectin are decreased. Matrix metalloproteinases (MMPs) are known to degrade multiple matrix molecules; therefore, nerves were assayed for MMP-2 and MMP-9 proteins. In neuropathy nerves, elevated levels of MMP-2 and MMP-9 were detected on western blots, and gelatin zymography confirmed the up-regulation of gelatinalytic activity in affected samples. Immunostaining studies revealed an increase in the numbers of MMP-2-and MMP-9-expressing cells in TrJ nerves. Cell type-specific immunolabeling showed that infiltrating macrophages are a significant source of both MMP-2 and MMP-9. Finally, the degradation of exogenous collagen IV by TrJ nerve lysates was prevented with a specific MMP inhibitor. Together these observations suggest that infiltration by MMP-expressing macrophages contributes to the remodeling of the TrJ nerve matrix.

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Fibronectin is a binding partner for the myelin‐associated glycoprotein (siglec‐4a)

Cited by 23 publications

References 40 publications

MUC1 Is a Counter-Receptor for Myelin-Associated Glycoprotein (Siglec-4a) and Their Interaction Contributes to Adhesion in Pancreatic Cancer Perineural Invasion

MUC1 Is a Counter-Receptor for Myelin-Associated Glycoprotein (Siglec-4a) and Their Interaction Contributes to Adhesion in Pancreatic Cancer Perineural Invasion

The Nogo-66 Receptor Homolog NgR2 Is a Sialic Acid-Dependent Receptor Selective for Myelin-Associated Glycoprotein

Matrix metalloproteinase mediated degradation of basement membrane proteins in Trembler J neuropathy nerves

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