A synthetic peptide derived from the carboxy terminus of the laminin A chain represents a binding site for the alpha 3 beta 1 integrin

Gehlsen, Kurt R.; Sriramarao, P.; Furcht, Leo T.; Skubitz, Amy P.N.

doi:10.1083/jcb.117.2.449

Cited by 127 publications

(70 citation statements)

References 49 publications

(106 reference statements)

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“…The ®bulin-1 binding site with Engelbreth-HolmSwarm tumor laminin has been mapped to a site contained within the E3 fragment (Pan et al, 1993b;Brown et al, 1994), a fragment derived from the carboxy terminus of the a chain. This domain has been shown to mediate integrin a3b1 binding (Gehlsen et al, 1989(Gehlsen et al, , 1992 and lies in the vicinity of binding sites for the integrins a6b1 (Aumailley et al, 1990;Hall et al, 1990;Sonnenberg et al, 1991) and a7b1 (Kramer et al, 1991;von der Mark et al, 1991). In addition, the laminin receptor dystroglycan binds to the E3 fragment (Gee et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines

et al. 1997

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Section: Discussionmentioning

confidence: 99%

Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines

et al. 1997

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“…Purification of ␣3␤1 Integrin-The purification of ␣3␤1 integrin was performed as described previously (33). Briefly, cells in confluent were detached with TBS(ϩ) (20 mM TrisHCl, pH 7.5, 130 mM NaCl, 1 mM CaCl 2 , and 1 mM MgCl 2 ) and washed with TBS(ϩ).…”

Section: Methodsmentioning

confidence: 99%

N-Acetylglucosaminyltransferase III Antagonizes the Effect of N-Acetylglucosaminyltransferase V on α3β1 Integrin-mediated Cell Migration

Zhao

Nakagawa

Itoh

et al. 2006

Journal of Biological Chemistry

134

111

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N-Acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of ␤1,6-GlcNAc branching of N-glycans, which contributes to metastasis. N-Acetylglucosaminyltransferase III (GnT-III) catalyzes the formation of a bisecting GlcNAc structure in N-glycans, resulting in the suppression of metastasis. It has long been hypothesized that the suppression of GnT-V product formation by the action of GnT-III would also exist in vivo, which will consequently lead to the inhibition of biological functions of GnT-V. To test this, we draw a comparison among MKN45 cells, which were transfected with GnT-III, GnT-V, or both, respectively. We found that ␣3␤1 integrin-mediated cell migration on laminin 5 was greatly enhanced in the case of GnT-V transfectant. This enhanced cell migration was significantly blocked after the introduction of GnT-III. Consistently, an increase in bisected GlcNAc but a decrease in ␤1,6-GlcNAcbranched N-glycans on integrin ␣3 subunit was observed in the double transfectants of GnT-III and GnT-V. Conversely, GnT-III knockdown resulted in increased migration on laminin 5, concomitant with an increase in ␤1,6-GlcNAc-branched N-glycans on the ␣3 subunit in CHP134 cells, a human neuroblastoma cell line. Therefore, in this study, the priority of GnT-III for the modification of the ␣3 subunit may be an explanation for why GnT-III inhibits GnT-V-induced cell migration. Taken together, our results demonstrate for the first time that GnT-III and GnT-V can competitively modify the same target glycoprotein and furthermore positively or negatively regulate its biological functions.Malignant transformation is accompanied by increased ␤1,6-GlcNAc branching of N-glycans attached to Asn-X-Ser/ Thr sequences in mature glycoproteins (1-3). N-Acetylglucosaminyltransferase V (GnT-V)3 catalyzes the addition of ␤1,6-linked GlcNAc (see Fig. 8 ) and defines this subset of N-glycans (4, 5). A relation between GnT-V and cancer metastasis has been reported by Dennis et al. (6) and Yamashita et al. (1).Studies on transplantable tumors in mice indicate that the product of GnT-V directly contributes to the growth of cancer and subsequent metastasis (7,8). On the other hand, somatic tumor cell mutants that are deficient in GnT-V activity produce fewer spontaneous metastases and grow more slowly than wildtype cells (6, 9). The suppression of tumor growth and metastasis has been reported in GnT-V-deficient mice (3). Moreover, Partridge et al. (10) reported that GnT-V-modified N-glycans with poly-N-acetyllactosamine, the preferred ligand for galectin-3, on surface receptors oppose their constitutive endocytosis and result in promoting intracellular signaling and consequently cell migration and tumor metastasis. These results indicate that inhibition of GnT-V might be useful in the treatment of malignancies by targeting their roles in metastasis.N-Acetylglucosaminyltransferase III (GnT-III) participates in the branching of N-glycans (see Fig. 8), catalyzing the formation of a unique sugar chain structure-bisecting GlcNAc (11). GnT-III is g...

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“…Among the integrins, α1β1 (Hall et al, 1990), α2β1 (Elices and Hemler, 1989;Languino et al, 1989;Lotz et al, 1990), α3β1 (Gehlsen et al, 1992), α6β1 (Sonnenberg et al, 1988;Lotz et al, 1990) and α6β4 (Lotz et al, 1990;Lee et al, 1992) integrins have been reported to mediate binding to LM in static condition. To determine which integrins function in flow condition, we examined the adhesion behaviour of Colo201 pretreated with functionally blocking mAbs to these integrins.…”

Section: Tethering and Spreading On Lm Is Partially Mediated By α6β1 mentioning

confidence: 99%

Laminin mediates tethering and spreading of colon cancer cells in physiological shear flow

et al. 1999

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Summary Under the physiological shear condition, cultured colon cancer cells bound to laminin (LM), but not to fibronectin or vitronectin. Most of the tethered cells did not roll, but arrested immediately and spread within 10-30 min on LM under the continuous presence of shear flow. The tethering of Colo201 was partially inhibited by monoclonal antibodies (mAbs) to α6 integrin and a combination of mAbs to β1 and β4 integrins, but not by mAb to 67KD laminin receptor. Some Colo201 cells still tethered at 4°C. This suggests that α6β1 and α6β4 integrins participate in Colo201 tethering on LM, although other non-integrin molecules play roles. In contrast, the spread of Colo201 was effectively inhibited by the mAbs to integrin α2, α6 and β1 chains. The effect of anti-α2 plus anti-α6 mAbs was almost equal to anti-β1, suggesting that Colo201 cells mainly use α2β1 and α6β1 integrins for spreading on LM. When the cells were perfused on subconfluent endothelial cells (HUVEC) cultured on LM, they did not tether on HUVEC but did on coated LM exposed at intercellular gap area. Immunohistochemistry revealed that LM abundantly existed in the cytosol of human portal and hepatic vein endothelial cells. These data suggest that LM can mediate from tethering to spreading of colon cancer cells under the blood flow and plays an essential role in haematogeneous metastasis.

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A synthetic peptide derived from the carboxy terminus of the laminin A chain represents a binding site for the alpha 3 beta 1 integrin

Cited by 127 publications

References 49 publications

Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines

Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines

N-Acetylglucosaminyltransferase III Antagonizes the Effect of N-Acetylglucosaminyltransferase V on α3β1 Integrin-mediated Cell Migration

Laminin mediates tethering and spreading of colon cancer cells in physiological shear flow

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