Endogenous muscle lectin inhibits myoblast adhesion to laminin.

Cooper, Douglas N.W.; Massa, Stephen M.; Barondes, Samuel H.

doi:10.1083/jcb.115.5.1437

Cited by 218 publications

(134 citation statements)

References 89 publications

Supporting

Mentioning

119

Contrasting

Unclassified

Order By: Relevance

“…In accordance with their proposed functions, lectins enhance or inhibit cell matrix interactions. Although little is known about the exact role of lectins in regulating cell adhesion, current models suggest that binding of lectins to matrix proteins elicits an inhibitory effect due to a steric hindrance of cell-matrix interactions [10,11]. The latter depend to a large extent upon the engagement of specific extra-cellular matrix proteins with cell surface integrins [12][13][14].…”

Section: Xcl Induces Actin Cytoskeleton Modificationsmentioning

confidence: 99%

Inhibitory action of a new lectin from Xerocomus chrysenteron on cell-substrate adhesion

Marty-Detraves¹,

Francis²,

Baricault³

et al. 2004

Mol Cell Biochem

View full text Add to dashboard Cite

Lectins are carbohydrate-binding proteins which potentially link to cell surface glycoconjugates and affect cell proliferation. We investigated the effect of a new lectin from the mushroom Xerocomus chrysenteron (XCL) on cell proliferation using adherent and suspension cell lines. XCL caused a dose-dependent inhibition of proliferation of the adherent cell lines NIH-3T3 and HeLa. Several experiments suggest that disruption of cell-substrate adhesion is the main factor affecting cell growth inhibition. (i) No antiproliferative effect was observed on the SF9 cell line, which does not require to be attached to grow. (ii) XCL was shown to affect the adherence of cells following their suspension by trypsin treatment. (iii) XCL was localized on the cell surface where it would act as a coating agent. (iv) XCL induced morphological changes from well spread to rounded cells and disrupted the actin cytoskeleton. By contrast, flow cytometric analysis showed that XCL does not interfere with the cell cycle, and does not induce apoptosis. (Mol Cell Biochem 258: [49][50][51][52][53][54][55] 2004)

show abstract

Section: Xcl Induces Actin Cytoskeleton Modificationsmentioning

confidence: 99%

Inhibitory action of a new lectin from Xerocomus chrysenteron on cell-substrate adhesion

Marty-Detraves¹,

Francis²,

Baricault³

et al. 2004

Mol Cell Biochem

View full text Add to dashboard Cite

show abstract

“…That LAMPs, along with the extracellular matrix components fibronectin and laminin, are a major cellular carrier of polylactosamine glycosylation suggests that their surface expression is involved in lectin-mediated cell adhesion Sato and Hughes, 1992). Polylactosamines of laminin are recognized by both 14-and 31-kDa endogenous f-galactoside binding lectins, and lectin secretion regulates cellular binding to polylactosamines of laminin (Woo et al, 1990;Zhou and Cummings, 1990;Cooper et al, 1991;Ochieng et al, 1992;Sato and Hughes, 1992).…”

Section: Introductionmentioning

confidence: 99%

Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer.

Nabi

Rodríguez-Boulan

1993

MBoC

View full text Add to dashboard Cite

An endogenous Madin-Darby canine kidney (MDCK) lysosomal membrane glycoprotein that exhibits a basolateral targeting pathway to the lysosome is shown here to exhibit significant N-terminal amino acid sequence identity to lysosomal associated membrane proteins (LAMP-2) of other species. During establishment of the MDCK monolayer after only 1 d of culture, this canine LAMP-2 has a larger molecular size (110 kDa) than following formation of a confluent monolayer after 3 d of culture (100 kDa) due to the increased presence of N-linked polylactosamine oligosaccharide chains. Neither polylactosamine glycosylation of LAMP-2 in MDCK cells nor truncation of N-linked oligosaccharide chains of LAMP-2 in a ricin-resistant MDCK-RCAR cell line influenced the basolateral polarity of its targeting. However, the rate of basolateral delivery of LAMP-2 in MDCK cells plated for 3 d was significantly faster (tl/2 = 28 min) than in 1-d cells (tl/2 = 40 min); in MDCK-RCAR cells the rate of basolateral delivery at both 1 and 3 d of plating was similar (t1/2 = 40 min). The rate differential in MDCK cells occurred after arrival of LAMP-2 to the Golgi apparatus because the rate of acquisition of endoglycosidase H resistance was the same (t1/2 = 25 min) at both days of plating. The rate of transit of LAMP-2 through the Golgi apparatus to the basolateral domain was therefore far more rapid (-4-fold) in 3 d compared with 1-d MDCK cultures. The increased polylactosamine glycosylation of MDCK LAMP-2 at early times of plating during the establishment of a confluent epithelial monolayer may thus be related to its longer residence time in the Golgi apparatus.

show abstract

“…As OECs continue to differentiate during fetal stages of development, they begin to express the L14 lectin (Mahanthappa et al, 1994) and the O4 antigenic epitope (Doucette and Devon, 1994;Franceschini and Barnett, 1996). The L14 lectin binds to molecules containing polylactosamine chains (Zhou and Cummings, 1993;Cooper et al, 1991) and was shown by Mahanthappa et al (1994) to promote the adhesion of primary olfactory neurons to laminin in vitro in an integrin-independent manner. The O4 mouse monoclonal antibody (Sommer and Schachner, 1981) recognizes a cell surface epitope that is also expressed by glial cells in the O 2 A lineage (Gard and Pfeiffer, 1989;Trotter and Schachner, 1989) and by Schwann cells (Mirsky et al, 1990;Morgan et al, 1991).…”

Section: Oecs Normally Differentiate Into Nonmyelinating Gliamentioning

confidence: 99%