Nervous System Glycoproteins

Kelly, Paul

doi:10.1007/978-1-4684-7464-0_6

Cited by 13 publications

(4 citation statements)

References 186 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Tight binding may be accomplished by intercalation of complex carbohydrates into the plasmalemma or by the presence on intrinsic glycoproteins within or extrinsic glycoproteins on the outside of the plasmalemma. In addition, the type of complex carbohydrate changes as cells differentiate, mature and die [10].…”

mentioning

confidence: 99%

Role of Complex Carbohydrates and Neurulation

McLone¹,

Knepper²

1985

Pediatr Neurosurg

View full text Add to dashboard Cite

Extracellular and cell-coat complex carbohydrates play a major role in critical cellular functions, e.g., cell recognition and cell-to-cell adherence, which are involved in neurulation. To date, available evidence suggests that neurulation is a combination of intercellular and extracellular biochemical and morphological events which are under the direction of the genome. To define the carbohydrate components that are essential to neurulation, normal C-57 and abnormal splotch (Sp/Sp) mouse embryos were studied using fluorescein-labeled lectins and computer-aided microspectrophotometric analysis of hyaluronate lyase and chondroitin ABC lyase-sensitive Alcian blue staining. Preliminary results of these studies indicate that the neuroepithelium of the splotch Sp/Sp mutant, a genetic model of a primary neural tube defect, is characterized by alterations in the type and amount of glycoconjugates and in the concentration of individual glycosaminoglycans. This review of mammalian neurulation discusses the importance of complex carbohydrates on the cell surface of the neuroepithelium of the closing neural fold.

show abstract

mentioning

confidence: 99%

Role of Complex Carbohydrates and Neurulation

McLone¹,

Knepper²

1985

Pediatr Neurosurg

View full text Add to dashboard Cite

show abstract

“…One postulation is that this process is enabled by complementary cell adhesion molecules that may be expressed by different classes of primary sensory neurones and their postsynaptic counterparts ( Edelman, 1984 ; Dodd and Jessell, 1985 ) . Molecules implicated in such axon guidance, target recognition, and synapse maintenance include the membrane‐associated glycoconjugates ( Kelly, 1984 ; Dodd and Jessell, 1986 ) .…”

Section: Introductionmentioning

confidence: 99%

Histochemical localisation of a galactose‐containing glycoconjugate expressed by sensory neurones innervating different peripheral tissues in the rat

Thornton

Gerke

Plenderleith

2005

J Peripheral Nervous Sys

View full text Add to dashboard Cite

The plant lectin Bandeiraea simplicifolia I-isolectin B4 (BSI-B4) identifies a galactose-containing, membrane-associated glycoconjugate expressed by a discrete subpopulation of unmyelinated primary sensory neurones in the rat. We have previously suggested that BSI-B4 selectively binds to primary sensory neurones that innervate the skin. However, in that study, the tracer diamidino yellow was applied to the cut ends of peripheral nerves to identify neurones innervating particular target tissues. In this study, we have avoided axotomy by retrogradely labelling primary sensory neurones from peripheral tissues using the carbocyanine dye 1,1'-dioctadecyl-3,3,3',3'-tetramethylindocarbacyanine perchlorate (DiI). DiI was injected into the plantar skin, gastrocnemius muscle, and pyloric region of the stomach in rats. Corresponding ganglia were sectioned, incubated in BSI-B4 conjugated to fluorescein isothiocyanate, and examined with a fluorescence microscope. DiI-labelled cells were identified by red fluorescence within the cytoplasm, whereas cells binding BSI-B4 displayed green fluorescence associated with the plasma membrane and Golgi apparatus. Quantitative analysis revealed that 36.2% of cutaneous neurones, 7.6% of muscle neurones, and 6.8% of visceral neurones expressed the BSI-B4-binding site, indicating that a small but significant proportion of small-diameter primary sensory neurones innervating muscle and viscera also express BSI-B4-binding sites.

show abstract

“…GLYCOCONJUGATES Several glocolipids and glycoproteins on myelin and neuronal or axonal surface membranes in the CNS and PNS carry the Gal(p1-3)GalNAc epitope (Kelly, 1984;Thomas et al, 1989a,b;Wiegandt, 1985) (Table 1). They also serve as tumor and differentiation antigens on many other cells outside the nervous system (Feizi, 1985).…”

Section: Introductionmentioning

confidence: 99%

Antibodies to GM1 and Gal(β1–3)GalNAc at the nodes of Ranvier in human and experimental autoimmune neuropathy

Thomas

1996

Microsc. Res. Tech.

View full text Add to dashboard Cite

Autoantibodies to Gal(beta 1-3)GalNAc epitopes on glycolipids and glycoproteins are associated with motor neuron disease and motor or sensorimotor neuropathy. These epitopes are ubiquitously distributed on cell surfaces. In the nervous system they are present on axons and myelin, specifically also at the nodes of Ranvier. Binding of GM1 antibodies to the nodal area may contribute to disease development in some of these conditions.

show abstract

Nervous System Glycoproteins

Cited by 13 publications

References 186 publications

Role of Complex Carbohydrates and Neurulation

Role of Complex Carbohydrates and Neurulation

Histochemical localisation of a galactose‐containing glycoconjugate expressed by sensory neurones innervating different peripheral tissues in the rat

Antibodies to GM1 and Gal(β1–3)GalNAc at the nodes of Ranvier in human and experimental autoimmune neuropathy

Contact Info

Product

Resources

About