Interaction of sulfated glycosaminoglycans with lectins.

Toda, Nobushige; Doi, Akemi; Jimbo, Akiko; Matsumoto, Isamu; Seno, Nobuko

doi:10.1016/s0021-9258(19)69205-7

Cited by 40 publications

(5 citation statements)

References 44 publications

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“…Such an interac-tion between an integral membrane proteoglycan and the cytoskeleton has been suggested in mammary epithelial cells and cultured fibroblasts where a membrane intercalated heparan sulfate proteoglycan may link extracellular matrix components to intracellular actin filaments (45,57). WGA has been shown to bind glycosaminoglycans (52). The unusually large size of the WGA-binding component, as well as electron microscopic images of intact photoreceptors where strings of succinyl-WGA-ferritin are seen extending great distances from the plasmalemma, could be consistent with the presence of a WGA-binding glycosaminoglycan.…”

Section: Discussionmentioning

confidence: 93%

Cytoskeletal-membrane interactions: a stable interaction between cell surface glycoconjugates and doublet microtubules of the photoreceptor connecting cilium.

Horst

Forestner

Besharse

1987

The Journal of Cell Biology

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Abstract. The ciliary base is marked by a transition zone in which Y-shaped cross-linkers extend from doublet microtubules to the plasma membrane. Our goal was to investigate the hypothesis that the cross-linkers form a stable interaction between membrane or cell surface components and the underlying microtubule cytoskeleton. We have combined Triton X-100 extraction with lectin cytochemistry in sensory cilium to investigate the cell surface glycoconjugates and cytoskeleton, and to identify the nents involved.the photoreceptor relationship between the underlying cell surface compoWheat germ agglutinin (WGA) binds heavily to the cell surface in the region of the Y-shaped cross-linkers of the neonatal rat photoreceptor cilium. WGA binding is not removed by prior digestion with neuraminidase and succinyl-WGA also binds the proximal cilium, suggesting a predominance of N-acetylglucosamine containing glycoconjugates. Extraction of the photoreceptor plasma membrane with Triton X-100 removes the lipid bilayer, leaving the Y-shaped crosslinkers associated with the axoneme. WGA-binding sites are found at the distal ends of the crosslinkers after Triton X-100 extraction, indicating that the microtubule-membrane cross-linkers retain both a transmembrane and a cell surface component after removal of the lipid bilayer. To identify glycoconjugate components of the cross-linkers we used a subcellular fraction enriched in axonemes from adult bovine retinas. Isolated, detergent-extracted bovine axonemes show WGA binding at the distal ends of the cross-linkers similar to that seen in the neonatal rat. Proteins of the axoneme fraction were separated by SDS-PAGE and electrophoretically transferred to nitrocellulose. WGA labeling of the nitrocellulose transblots reveals three glycoconjugates, all of molecular mass greater than 400 kD. The major WGA-binding glycoconjugate has an apparent molecular mass of ~600 kD and is insensitive to prior digestion with neuraminidase. This glycoconjugate may correspond to the dominant WGAbinding component seen in cytochemical experiments. T HE ciliary plasma membrane represents a distinct plasma membrane domain differing functionally, biochemically, and electrophysiologically from that of the remainder of the cell (3,10,14,24,32,38,50). The base of the cilium delineates the junction between restricted domains and is marked by the structural specialization of both the membrane and the underlying axoneme. Freeze fracture of the plasma membrane reveals rows of intramembranous particles encircling the base of the cilium, the ciliary necklaces (19,22), strikingly distinct from the particle poor membrane over the remainder of the cilium. Underlying this membrane specialization is the axoneme transition zone, a 9 + 0 arrangement of microtubule doublets connecting the basal body to the 9 + 2 motile axoneme. Y-shaped crosslinkers project from each microtubule doublet at the junction of the A and B subfibers to the adjacent plasma membrane (22). The role of these connections and the ciliary necklaces is not k...

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Section: Discussionmentioning

confidence: 93%

Cytoskeletal-membrane interactions: a stable interaction between cell surface glycoconjugates and doublet microtubules of the photoreceptor connecting cilium.

Horst

Forestner

Besharse

1987

The Journal of Cell Biology

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“…To corroborate the specificity of the fluorescein reagent, we used the lectin Concanavalin A conjugated to Alexa594 (Con A-Alexa) (Thermo Fisher) to label glycosaminoglycans , found in the L. cholodnii nanofibril sheaths. The nanofibrils are made of structural glycoconjugates, which are a type of glycosaminoglycan. , By co-staining first with fluorescein and then with Con A-Alexa, we measured the amount of fluorescence overlap between NH 2 -rich regions and sugars (SI Figure S5).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Polyfunctional Nanofibril Appendages Mediate Attachment, Filamentation, and Filament Adaptability in Leptothrix cholodnii

Kunoh¹,

Morinaga²,

Sugimoto

et al. 2019

ACS Nano

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Leptothrix is a species of Fe/Mn-oxidizing bacteria known to form long filaments composed of chains of cells that eventually produce a rigid tube surrounding the filament. Prior to the formation of this brittle microtube, Leptothrix cells secrete hair-like structures from the cell surface, called nanofibrils, which develop into a soft sheath that surrounds the filament. To clarify the role of nanofibrils in filament formation in L. cholodnii SP-6, we analyze the behavior of individual cells and multicellular filaments in high-aspect ratio microfluidic chambers using time-lapse and intermittent in situ fluorescent staining of nanofibrils, complemented with atmospheric scanning electron microscopy. We show that in SP-6 nanofibrils are important for attachment and their distribution on young filaments post-attachment is correlated to the directionality of filament elongation. Elongating filaments demonstrate a surprising ability to adapt to their physical environment by changing direction when they encounter obstacles: they bend or reverse direction depending on the angle of the collision. We show that the forces involved in the collision can be used to predict the behavior of filament. Finally, we show that as filaments grow in length, the older region becomes confined by the sheath, while the newly secreted nanofibrils at the leading edge of the filament form a loose, divergent, structure from which cells periodically escape.

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“…These particular lectins were chosen due to the intense staining signal showed for all the control groups in contrast to ZYC‐ and ZYP‐treated samples, which showed a dramatic decrease in staining signal. As previously mentioned, WGA stains (GlcNAc)n and multivalent sialic acids (Sia) can be found in both N‐ and O‐glycosylation on cell membrane but also in ECM glycoproteins 53‐58 . Among sialic acids, WGA can also stain Neu5Gc and N‐acetylneuraminic acid (Neu5Ac); nevertheless, its affinity to Neu5Gc is much lower than that to Neu5Ac 59,60 .…”

Section: Discussionmentioning

confidence: 99%

“…As previously mentioned, WGA stains (GlcNAc)n and multivalent sialic acids (Sia) can be found in both N-and O-glycosylation on cell membrane but also in ECM glycoproteins. [53][54][55][56][57][58] Among sialic acids, WGA can also stain Neu5Gc…”

Section: Discussionmentioning

confidence: 99%

Generation of glycans depleted decellularized porcine pericardium, using digestive enzymatic supplements and enzymatic mixtures for food industry

Morticelli

Magdei

Tschalaki

et al. 2021

Xenotransplantation

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Interaction of sulfated glycosaminoglycans with lectins.

Cited by 40 publications

References 44 publications

Cytoskeletal-membrane interactions: a stable interaction between cell surface glycoconjugates and doublet microtubules of the photoreceptor connecting cilium.

Cytoskeletal-membrane interactions: a stable interaction between cell surface glycoconjugates and doublet microtubules of the photoreceptor connecting cilium.

Polyfunctional Nanofibril Appendages Mediate Attachment, Filamentation, and Filament Adaptability in Leptothrix cholodnii

Generation of glycans depleted decellularized porcine pericardium, using digestive enzymatic supplements and enzymatic mixtures for food industry

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