Laminin E8 alveolarization site: heparin sensitivity, cell surface receptors, and role in cell spreading

Chen, L.; Shick, V.V.; Matter, Michelle L.; Laurie, S M; Ogle, Roy C.; Laurie, Gordon W.

doi:10.1152/ajplung.1997.272.3.l494

Cited by 11 publications

(18 citation statements)

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“…It was previously demonstrated that ␣1: 2179 SINNNRWHSIYITRFGNMGS 2198 (SN peptide), located in the first loop of the G-domain, supports the adhesion of a variety of cells, and anti-SN peptide antibodies blocked the binding of cells to the E8 fragment (19). These data indicate that the SN peptide, unlike the proximal ␣1:…”

Section: Srarkqaasikvavsadrmentioning

confidence: 83%

“…2104 has no effect on cell adhesion to the E8 fragment (19). Third, the binding of cells to intact laminin-1 and the E8 fragment was blocked by recombinant G-domain, which does not contain ␣1:…”

Section: Sikvavmentioning

confidence: 98%

“…of three individual wells. which is located in the first loop of the G-domain, is responsible for the binding of a variety of cells to laminin-1 (19,32,33). Another G-domain peptide (␣1:Asn 2183 -Gly 2194 ; AG-10), which comprises the central portion of the SN peptide, stimulated the invasion of cross-linked gelatin films by melanoma cells (34).…”

Section: Elastase-generated Fragments Of Laminin-1 Stimulatementioning

confidence: 99%

“…Heparin binding fragments stimulated macrophage proteinase expression severalfold greater than fragments that did not bind, suggesting that the stimulatory domains were in or associated with the G-domain. A peptide from the first globular repeat in the G-domain (␣1: Ser 2179 -Ser 2198 ; SN peptide), which plays a role in the adhesion of cells to laminin-1 (19), triggered the phosphorylation of MAPK erk1/2 and stimulated the expression of macrophage uPA and MMP-9. Moreover, a heparin-binding fraction isolated from an aortic aneurysm contained fragments of ␣1-chain and stimulated macrophage proteinase expression.…”

mentioning

confidence: 99%

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Exposure of Cryptic Domains in the α1-chain of Laminin-1 by Elastase Stimulates Macrophages Urokinase and Matrix Metalloproteinase-9 Expression

Khan¹,

Laurie²,

McCaffrey³

et al. 2002

Journal of Biological Chemistry

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Degradation of the extracellular matrix leads to the release of fragments, which elicit biological responses distinct from intact molecules. We have reported that ␣1:Ser 2091 -Arg 2108 , a peptide derived from the ␣1-chain of laminin-1, triggers protein kinase C-dependent activation of MAPK erk1/2 , leading to the up-regulation of macrophage urokinase type plasminogen activator and matrix metalloproteinase (MMP)-9 expression. Since intact laminin-1 failed to trigger these events, we hypothesized that ␣1:Ser 2091 -Arg 2108 is cryptic or assumes a conformation not recognized by macrophages. Here we demonstrate that elastase cleavage of laminin-1 generates fragments, which stimulate proteinase expression by RAW264.7 macrophages and peritoneal macrophages. In contrast, fragments generated by MMP-2, MMP-7, or plasmin had no effect on macrophage proteinase expression. Elastase-generated laminin-1 fragments were fractionated by heparin-Sepharose chromatography. Heparinbinding fragments stimulated macrophages' proteinase expression severalfold greater than nonbinding fragments. The heparin binding fragments reacted with antibodies directed against regions of the ␣1-chain including ␣1:Ser In earlier studies, we tested the hypothesis that the ECM regulates macrophage proteinase expression by culturing macrophages on ECM purified from Engelbreth Holm Swarm (EHS) sarcoma (Matrigel TM ) (8,9). Results demonstrated that the expression of urokinase type plasminogen activator (uPA) and MMP-9 by murine RAW264.7 macrophages, human THP-1 monocytes, and human bone marrow-derived macrophages were strongly up-regulated. This was the first demonstration that the engagement of ECM by macrophages stimulates their expression of both uPA and MMP-9. Since the uPA/plasmin system is a physiologic activator of MMPs (10, 11), the ECM emerges as a potent regulator of the macrophage-degradative phenotype.The ECM component responsible for stimulating macrophage proteinase expression was identified as laminin-1 (8).Laminins are large heterotrimeric molecules (ϳ500 -1000 kDa) with multiple domains that mediate their attachment to cells and other ECM components (12). Twelve laminin heterotrimers (assembled from five ␣, three ␤, and three ␥ chains) have been identified in mammals. Laminin-1 was the first of this family to be identified (13) and remains the best understood of the laminin isoforms (12,14). It consists of ␣1 (ϳ400 kDa), ␤1 (ϳ200 kDa), and ␥1 (ϳ200 kDa) chains. The NH 2 -terminal portions of the ␣1-, ␤1-, and ␥1-chains are free, whereas much of the rest of the chains are twisted in a coiled-coil. The COOH-terminal portion of the ␣1-chain extends past the coiled-coil region and forms a large oblong globule (G-domain) consisting of five homologous repeats. The G-domain is the principle heparin-binding region of laminin-1 (15, 16).In an effort to identify the domains of laminin-1 responsible for stimulating macrophage proteinase expression, we examined synthetic peptides, which were reported to support cell adhesion and stimulate a variety ...

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Section: Srarkqaasikvavsadrmentioning

confidence: 83%

Section: Sikvavmentioning

confidence: 98%

Section: Elastase-generated Fragments Of Laminin-1 Stimulatementioning

confidence: 99%

mentioning

confidence: 99%

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Exposure of Cryptic Domains in the α1-chain of Laminin-1 by Elastase Stimulates Macrophages Urokinase and Matrix Metalloproteinase-9 Expression

Khan¹,

Laurie²,

McCaffrey³

et al. 2002

Journal of Biological Chemistry

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“…This is ϳ10-fold higher than the concentration of GoH3 needed to inhibit ␣ 6 -mediated cell adhesion to laminin (38). We consider three possibilities to explain these observations.…”

Section: Disintegrin-like Domain-containing Constructs Of Madam 2 Promentioning

confidence: 90%

Sequence-specific Interaction between the Disintegrin Domain of Mouse ADAM 2 (Fertilin β) and Murine Eggs

Bigler¹,

Takahashi²,

Chen³

et al. 2000

Journal of Biological Chemistry

105

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Little is yet known about the biological and biochemical properties of the disintegrin-like domains of ADAM (a disintegrin and metalloprotease) proteins. Mouse ADAM 2 (mADAM 2; fertilin ␤) is a sperm surface protein involved in murine fertilization. We produced recombinant proteins containing the disintegrin-like domain of mADAM 2 in both insect cells and in bacteria. The protein produced in insect cells (baculo D؉C) contained a signal sequence followed by the disintegrin-like and cysteine-rich domains; it was purified from the medium of recombinant baculovirus-infected cells. A bacterial construct containing the disintegrin-like domain was produced in Escherichia coli as a glutathione S-transferase chimera. Baculo D؉C, as well as the D domain of the bacterial construct (released with thrombin), bound to the microvillar surface of murine eggs. Using concentrations in the range of 1 to 5 M, both recombinant proteins strongly inhibited sperm-egg binding and fusion; the baculovirus-produced protein exhibited a somewhat greater extent of inhibition (ϳ75 versus ϳ55% maximal inhibition). Substitution of alanine for each of the five charged residues within the disintegrin loop of mADAM 2 revealed a critical importance for the aspartic acid at position nine. Binding of both recombinant proteins to the egg was inhibited by the function blocking anti-␣ 6 monoclonal antibody, GoH3, but not by a nonfunctionblocking anti-␣ 6 monoclonal antibody. Binding was also inhibited by a peptide analogue of, and with an antibody against, the disintegrin loop of mADAM 2. ADAMs1 are a large group of type I integral membrane glycoproteins that contain a disintegrin and a metalloprotease domain (1, 2). Following their metalloprotease and disintegrinlike domains, they contain a cysteine-rich domain, an EGF repeat, a transmembrane domain, and a cytoplasmic tail. Their closest relatives are the P-III snake venom metalloproteases (SVMPs), which are secreted proteins that contain a disintegrin-like and a metalloprotease domain as well as a cysteinerich domain. P-II SVMPs contain metalloprotease and disintegrin domains but lack the cysteine-rich (and other) domains.The disintegrin domains of the P-II SVMPs have a 13-amino acid loop containing, at their tips, sequences such as RGD (kistrin and echistatin), KGD (barbourin), and MVD (atrolysin E). Several P-II snake disintegrins have been shown to bind to the platelet integrin, ␣ IIb ␤ 3, thereby preventing binding of fibrinogen and inhibiting platelet aggregation. Inhibition of platelet aggregation accounts, in part, for the severe hemorrhagic response in snakebite victims. The disintegrin-like domains of P-III SVMPs differ from their P-II counterparts in having two additional cysteine residues and a 14-residue predicted loop that aligns with the 13-amino acid "RGD" loop found in the P-II disintegrins. One of the additional cysteine residues is near the center of the disintegrin loop. The disintegrin-like domain of the P-III SVMP atrolysin A has been characterized. Atrolysin A purified from snake ...

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Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland

et al. 1998

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Laminin E8 alveolarization site: heparin sensitivity, cell surface receptors, and role in cell spreading

Cited by 11 publications

References 0 publications

Exposure of Cryptic Domains in the α1-chain of Laminin-1 by Elastase Stimulates Macrophages Urokinase and Matrix Metalloproteinase-9 Expression

Exposure of Cryptic Domains in the α1-chain of Laminin-1 by Elastase Stimulates Macrophages Urokinase and Matrix Metalloproteinase-9 Expression

Sequence-specific Interaction between the Disintegrin Domain of Mouse ADAM 2 (Fertilin β) and Murine Eggs

Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland

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