Electron microscopic evidence for a mucin‐like region in chick muscle α‐dystroglycan

Brancaccio, Andrea; Schulthess, Therese; Gesemann, Matthias; Engel, Jürgen

doi:10.1016/0014-5793(95)00628-m

Cited by 140 publications

(117 citation statements)

References 22 publications

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“…To further verify that the effect of conditioned media to inhibit cell adhesion was due to α-DG, conditioned media from MCF7 vector control and DG-overexpressing derivatives were depleted of DG using WGL, which specifically binds and retains the α-DG protein. 17 Depletion of α-DG was able to abolish the conditioned media-induced inhibition of cell adhesion of both MCF7 vector and DG-overexpressing derivatives (Fig. 6).…”

Section: α-Dg Is Secreted In the Culture Medium Of Cancer But Not Normalmentioning

confidence: 88%

“…Native α-DG was been isolated from chicken skeletal muscles,as previously described. 17 Briefly, 10 g of freshly frozen muscle was homogeneized in 40 ml of lysis buffer (0.2 M NaCl, 50 mM Tris, 2.5 mM N-ethylmaleimide, 1 mM phenylmethanesulfonyl fluoride, 1 µg/ml leupeptine and benzamidine). After centrifugation (15000 rpm) the supernatant was filtered using a Whatman filter paper and loaded on a DEAE-Sepharose Fast Flow (Pharmacia) column (2x10cm) equilibrated with lysis buffer, at 4˚C.…”

Section: Methodsmentioning

confidence: 99%

“…WGL is a well-known glycoprotein binding agent which was shown to have a high affinity towards α-DG. 17 After washing (with approximately ten column volumes) elution was carried out with two volumes of the same buffer containing 0.25 M N-acetyl-glucosamine. After extensive dialysis against H 2 O, the α-DG solution was lyophilized and then quantitated using a spectrophotometrical assay kit (Protein Assay, Bio-Rad).…”

Section: Methodsmentioning

confidence: 99%

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Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Sgambato¹,

Camerini²,

Faraglia³

et al. 2004

Cancer Biology & Therapy

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Dystroglycan (DG) is an adhesion molecule formed by two subunits, α (extracellular) and β (transmembrane) DG, which are codified by a single gene and form a continuous link from the extracellular matrix to the intracellular cytoskeleton. Reduction or loss of expression of DG has been observed in human cancer cell lines and primary tumors and has been suggested to promote tumor development and invasiveness.In this study, the human breast epithelial non-tumorigenic MCF10F and the breast cancer MCF7 cell lines were engineered to stably express an exogenous DG cDNA and the effects on the phenotype of both cell lines were evaluated. The MCF10F transfected cells displayed an increased expression of both DG subunits which was associated with inhibition of the anchorage-dependent growth, accumulation of cells in the G 0 /G 1 phase of the cell cycle and increased adhesion to a substratum. The MCF7 transfected cells were unable to restore α-DG despite an increased expression of the β-DG subunit. Anchoragedependent and independent growth and the in vivo tumorigenicity were reduced in these derivatives that also displayed a reduced adhesion to a substratum and were shown to release α-DG in the culture medium.These findings confirm and extend previous evidence that transformation of mammary epithelial cells is associated with loss of their ability to retain α-DG on the cell membrane. Moreover, they indicate that DG is involved in cell functions other than cell adhesion to the extracellular matrix, and that its loss of function might predispose to tumor progression by compromising regulatory controls over cell growth and proliferation.

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Section: α-Dg Is Secreted In the Culture Medium Of Cancer But Not Normalmentioning

confidence: 88%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Sgambato¹,

Camerini²,

Faraglia³

et al. 2004

Cancer Biology & Therapy

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“…In addition to 1 H and 13 C 1D spectra, 2D HÀ ÀH correlation spectroscopy (COSY), H-H total correlation spectroscopy (TOCSY), and heteronuclear multiple quantum coherence (HMQC and HMBC) were used to make assignments. 1 J CH values were determined from coupled 13 …”

Section: Nmrmentioning

confidence: 99%

“…11 Interestingly, electron micrographs of a-dystroglycan have indicated that the central mucin-like segment is extended as with conventional mucins. 13 Mannose does not have the same arrangement of functional groups as does GalNAc, and particularly lacks the amide group important in interactions that stabilize the extended structure. 9 It would therefore seem unlikely that Man on its own would be capable of supporting such a structural arrangement.…”

Section: Introductionmentioning

confidence: 99%

Conformational consequences of protein glycosylation: Preparation of O‐mannosyl serine and threonine building blocks, and their incorporation into glycopeptide sequences derived from α‐dystroglycan

et al. 2008

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With the goal to investigate the structural impact of O‐mannosyl glycosylation on α‐dystroglycan, a glycoprotein that has an important role in the extracellular organization of muscle, glycopeptides derived from its mucin‐like sequence have been prepared by solid‐phase peptide synthesis. Two approaches have been explored to obtain needed mannosylated serine and threonine building blocks. With the α‐carboxyl group unprotected, and with tetraaceto‐1‐fluoro‐α‐D‐mannose as the sugar donor, the desired α‐O‐mannosyl‐Fmoc‐Ser/Thr formed, along with mannosyl ester isomers and the species with mannose attached to both hydroxyl and carboxyl functions. Relevant mechanistic questions and stability issues were elucidated. Alternatively, building blocks were made with the α‐carboxyl protected/activated as the pentafluorophenyl (Pfp) ester. Glycopeptides synthesized herein contained 5–9 residues, and featured one, two, and four consecutive Ser and/or Thr residues O‐glycosylated with mannose. Circular dichroism (CD) spectra for Man‐containing glycopeptides recorded in water show them to be not well ordered. For one of the α‐dystroglycan‐derived sequences, the comparative conformational consequences of glycosylation by either Man or GalNAc have been examined by CD and NMR, with both methods showing a more organized structure when GalNAc is present. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 358–368, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Distinct α7Aβ1 and α7Bβ1 integrin expression patterns during mouse development: α7A is restricted to skeletal muscle but α7B is expressed in striated muscle, vasculature, and nervous system

Velling

Collo²,

Sorokin

et al. 1996

Dev. Dyn.

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Electron microscopic evidence for a mucin‐like region in chick muscle α‐dystroglycan

Cited by 140 publications

References 22 publications

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Conformational consequences of protein glycosylation: Preparation of O‐mannosyl serine and threonine building blocks, and their incorporation into glycopeptide sequences derived from α‐dystroglycan

Distinct α7Aβ1 and α7Bβ1 integrin expression patterns during mouse development: α7A is restricted to skeletal muscle but α7B is expressed in striated muscle, vasculature, and nervous system

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