An L1-like molecule, the 8D9 antigen, is a potent substrate for neurite extension.

Lagenaur, Carl F.; Lemmon, Vance

doi:10.1073/pnas.84.21.7753

Cited by 396 publications

(288 citation statements)

References 19 publications

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“…Production and characterization ofthe N-CAM antibodies have been described previously (Lagenaur and Lemmon, 1987;Chung et al, 199 I). The monoclonal antibody 12F8 recognizes polysialic acid epitopes on N-CAM in mammalian as well as avian species, and identifies embryonic forms of N-CAM distinct from adult forms lacking polysialic acid (Lagenaur et al, 1988).…”

Section: Methodsmentioning

confidence: 99%

Embryonic neural cell adhesion molecule (N-CAM) is elevated in the denervated rat dentate gyrus

et al. 1994

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We evaluated the immunohistological changes in neural cell adhesion molecule (N-CAM) expression in the adult rat dentate gyrus during the period of synaptic degeneration, axonal sprouting, and synaptogenesis following ipsilateral entorhinal cortex (ERC) lesion. This lesion denervates the outer two-thirds of the dentate granule cells dendrites and induces compensatory sprouting from the subjacent inner one-third into the denervated zone, as well as reactive synaptogenesis in the denervated outer molecular layer. In unlesioned adult hippocampus, antibodies to total N-CAM stained the inner molecular layer intensely, and the outer molecular layer (ML) more lightly. After ERC lesion the intense staining of the inner layer widened, the expansion following the known temporal sequence of commissural and associational (C/A) axon sprouting into the denervated zone. In normal unlesioned controls there was very light, uniform staining of the ML with antibodies directed against embryonic N-CAM (eN-CAM). By 2 d post-ERC lesion, the outer two- thirds of the ML stained robustly with antibody to eN-CAM. This area of intense staining receded as the C/A axon collaterals from the inner one- third entered the denervated zone, so that by 30 d the intense eN-CAM staining only occupied the outer half of the ML. The increased expression of eN-CAM remained present at 60 d post-ERC lesion, past the point that synaptic volume density has returned to normal levels in the denervated zone. Ultrastructural studies showed that the newly expressed eN-CAM was located on the surface of dendrites in the denervated zone, but was not found at the synaptic contacts.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Methodsmentioning

confidence: 99%

Embryonic neural cell adhesion molecule (N-CAM) is elevated in the denervated rat dentate gyrus

et al. 1994

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“…Binding of Collagen XVIII to Retinal Basement Membranes-A PAPpen (EMS, Washington, PA) was used to circle an ϳ1-cm 2 area of a plastic dish coated with nitrocellulose (20). The hydrophobic ring reduces the volume of the incubation solutions to less than 100 l. Retinal basement membranes were isolated from E6 chick retinae as flat sheets within the encircled areas of the dishes as described (25).…”

Section: Molecular Cloning Of Chick Collagen XVIII Dna By Nested Pcr-tomentioning

confidence: 99%

Expression of Collagen XVIII and Localization of Its Glycosaminoglycan Attachment Sites

Dong

Cole²,

Halfter

2003

Journal of Biological Chemistry

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Collagen XVIII is the only currently known collagen that carries heparan sulfate glycosaminoglycan side chains. The number and location of the glycosaminoglycan attachment sites in the core protein were determined by eukaryotic expression of full-length chick collagen XVIII and site-directed mutagenesis. Three SerGly consensus sequences carrying glycosaminoglycan side chains were detected in the middle and N-terminal part of the core protein. One of the Ser-Gly consensus sequences carried a heparan sulfate side chain, and the remaining two had mixed chondroitin and heparan sulfate side chains; thus, recombinant collagen XVIII was a hybrid of heparan sulfate and chondroitin proteoglycan. In contrast, collagen XVIII from all chick tissues so far assayed have exclusively heparan sulfate side chains, indicating that the posttranslational modification of proteins expressed in vitro is not entirely identical to the processing that occurs in a living embryo. Incubating the various mutated collagen XVIIIs with retinal basement membranes showed that the heparan sulfate glycosaminoglycan side chains mediate the binding of collagen XVIII to basement membranes.The collagens type XVIII and XV are members of the multiplexins, a collagen subfamily that is characterized by multiple alternating collagen and non-collagenous domains in the protein sequence (1, 2). Collagen XVIII came into the public spotlight by the discovery that the C-terminal peptide of collagen XVIII, named endostatin, has anti-angiogenic and anti-tumor activities (3, 4). The anti-angiogenic activity of the peptide led to the idea that collagen XVIII might be involved in the development of the vascular system. The targeted deletion of collagen XVIII in mice (5) and a naturally occurring mutation in human (6), however, showed that its main function is restricted to the development of the vasculature in the eye but has no function in blood vessel development in other parts of the body. The fact that collagen XVIII is, next to collagen IV, the only collagen that is conserved from Drosophila (7) and Caenorhabditis elegans (8) to humans suggests an important function of the protein in evolution. The deduced amino acid sequences from collagen XVIII cDNA in mouse and human suggested that collagen XVIII is a proteoglycan (1, 9). It was later revealed by investigating the naturally occurring protein from chick embryos (10) that collagen XVIII is a heparan sulfate proteoglycan (HSPG), 1 which is, next to perlecan and agrin, the third extracellular matrix HSPG currently known (10, 11). HSPGs are members of a family of cell surface proteins with polysaccharide side chains characterized by alternating uronic acid and glucosamine units (12, 13). They occur as either integral membrane (14, 15) or as secreted extracellular matrix proteins (12). The polysaccharide chains are connected to the core proteins through serine of the Ser-Gly (SG) consensus sequence whereby the presence of nearby acidic amino acids and the repetition of SGs are factors that promote attachment of glyco...

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“…Among the many cues that guide the axons of embryonic neurons to their proper destinations, axon fasciculation is an important developmental mechanism. The cell adhesion molecules (CAMs) involved in neurite fasciculation 43,44 include neural cell adhesion molecule (N-CAM) and NGF-inducible large external glycoprotein in the rat, neuron-glial cell adhesion molecule, G4, and 8D9 in the chicken, and L1 in the mouse. The role of CAMs on a given axon is to promote the extension of other neurites along this axon that, in turn, produces fasciculated axons.…”

Section: Discussionmentioning

confidence: 99%

Differential expression of Csk homologous kinase (CHK) in normal brain and brain tumors

Kim¹,

Avraham

Jiang

et al. 2004

Cancer

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Approximately 9% of deceased kidney donors are classified by the Centers for Disease Control as high infectious risk donors (HRDs), donors thought to be at increased risk for having HIV infection. While the use of HRDs expands the organ supply, there is a small risk of infectious transmission. All donors are tested for antibodies to a variety of viral infections including HIV, hepatitis C virus (HCV), and hepatitis B virus; however, infections acquired in the weeks to months before death may not be serologically detectable, but will likely be transmitted to the recipient. Nucleic acid testing (NAT) shortens the window between acquisition of infection and serologic detectability, from approximately 22 days to 9 days for HIV and from 66 days to 7 days for HCV. Nucleic acid testing has not been universally adopted because it is expensive, time consuming, and has a higher rate of false positives compared with an enzyme‐linked immunosorbent assay (ELISA), which might lead to discarding viable organs. Further studies are needed to quantify the risk of infectious transmission from HRDs, identify patients on the waitlist who would most benefit from HRD receipt, and guide NAT policies.

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An L1-like molecule, the 8D9 antigen, is a potent substrate for neurite extension.

Cited by 396 publications

References 19 publications

Embryonic neural cell adhesion molecule (N-CAM) is elevated in the denervated rat dentate gyrus

Embryonic neural cell adhesion molecule (N-CAM) is elevated in the denervated rat dentate gyrus

Expression of Collagen XVIII and Localization of Its Glycosaminoglycan Attachment Sites

Differential expression of Csk homologous kinase (CHK) in normal brain and brain tumors

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