Structure and Chromosomal Localization of the Mouse Neurocan Gene

Rauch, Uwe; Grimpe, Barbara; Kulbe, Gerlinde; Arnold-Ammer, Irene; Beier, David R.; Fässler, Reinhard

doi:10.1006/geno.1995.1168

Cited by 28 publications

(21 citation statements)

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“…Because the core proteins of other hyaluronan-binding chondroitin sulfate proteoglycans, such as aggrecan and neurocan, which are now known to have similar structural characteristics and share considerable amino acid sequence identity with PG-M (Li et al, 1993;Rauch et al, 1995), have lower molecular weights than that of PG-M~(VU), the above analysis also suggests either no cross-reactivity of the anti-PG-M…”

Section: Western Blot Analysis Of Pg-m In Embryonic Chicken Retinamentioning

confidence: 92%

“…However, nucleotide sequence identities of chicken PG-M to other proteoglycans were fairly low [57.5% to chicken aggrecan (Li et al, 1993), 52.4% to mouse brevican (Rauch et al, 1995, GenBank Data Bank with accession no. X87096), and 55.2% to mouse neurocan (Rauch et al, 1995) under the conditions that unit sizes to compare were 4 and the pickup locations were 5; the nucleotide sequences of chicken neurocan and brevican are not available thus far]. It is likely that the analysis may be free of those false signals.…”

Section: Northern Blot Analysismentioning

confidence: 99%

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Transient Expression of PG‐M/Versican, a Large Chondroitin Sulfate Proteoglycan in Developing Chicken Retina

Zako

Shinomura

Miyaishi

et al. 1997

Journal of Neurochemistry

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Abstract:We previously showed the expression of PG-M/versican in embryonic chicken retina. In this study, we characterized the alternatively spliced forms of PG-MI versican and their developmental regulation to investigate the implication of PG-Mlversican in neurite outgrowth from retinal cells during development. On day 5, the immunolocalization of PG-M was first observed at the inner surface of neural retina. On day 7, the pronounced staining was observed in the nerve fiber layer and inner plexiform layer where neural networks of ganglion cells were being formed. As the development proceeded, more intensive staining was observed in these layers. The staining peaked on day 14 and then decreased. Northern analysis and western blotting revealed the presence of a single-sized transcript (13 kb) and the PG-Mlversican core protein (550 kDa) on day 14, but the absence of any transcripts or protein bands on day 20, indicating a transient expression of PG-M + (VO), the alternatively spliced form with the most abundant sites for the chondroitin sulfate attachment. Taken together, it is likely that PG-M/versican is involved in neurite outgrowth from ganglion cells during retinal development, and antiadhesion activity of its chondroitin sulfate chains may be important for regulation. Key Words: PG-M -Versican-Chondroitin sulfate proteoglycan-Neurite outgrowth -Ganglion cell-Retinal development.

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Section: Western Blot Analysis Of Pg-m In Embryonic Chicken Retinamentioning

confidence: 92%

Section: Northern Blot Analysismentioning

confidence: 99%

Transient Expression of PG‐M/Versican, a Large Chondroitin Sulfate Proteoglycan in Developing Chicken Retina

Zako

Shinomura

Miyaishi

et al. 1997

Journal of Neurochemistry

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“…Targeting constructs to inactivate the mouse neurocan gene were made using a cosmid clone of the mouse neurocan gene described earlier (40). For the NCIg construct, a 11.2-kb SpeI-XhoI fragment containing the promoter region and exons 1 to 3 was fused to a thymidine kinase expression cassette.…”

Section: Methodsmentioning

confidence: 99%

Neurocan Is Dispensable for Brain Development

Zhou

Brakebusch

Matthies

et al. 2001

Molecular and Cellular Biology

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183

139

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Neurocan is a component of the extracellular matrix in brain. Due to its inhibition of neuronal adhesion and outgrowth in vitro and its expression pattern in vivo it was suggested to play an important role in axon guidance and neurite growth. To study the role of neurocan in brain development we generated neurocan-deficient mice by targeted disruption of the neurocan gene. These mice are viable and fertile and have no obvious deficits in reproduction and general performance. Brain anatomy, morphology, and ultrastructure are similar to those of wild-type mice. Perineuronal nets surrounding neurons appear largely normal. Mild deficits in synaptic plasticity may exist, as maintenance of late-phase hippocampal long-term potentiation is reduced. These data indicate that neurocan has either a redundant or a more subtle function in the development of the brain.

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“…This observation is in contrast to the average size of exons (∼150 bp) for a variety of genes and suggests that these genes have evolved a way to bypass the rules of exon definition. In neurocan, the central nonhomologous domain is encoded by two distinct exons of relatively smaller dimension (∼0.6 and 1.2 kb) (159). An established notion is that intervening sequences function by limiting amplification of genomic DNA that needs to maintain a constant size.…”

Section: Genomic Organization and Transcriptional Controlmentioning

confidence: 99%

MATRIX PROTEOGLYCANS: From Molecular Design to Cellular Function

Iozzo

1998

Annu. Rev. Biochem.

1,485

1,111

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The proteoglycan superfamily now contains more than 30 full-time molecules that fulfill a variety of biological functions. Proteoglycans act as tissue organizers, influence cell growth and the maturation of specialized tissues, play a role as biological filters and modulate growth-factor activities, regulate collagen fibrillogenesis and skin tensile strength, affect tumor cell growth and invasion, and influence corneal transparency and neurite outgrowth. Additional roles, derived from studies of mutant animals, indicate that certain proteoglycans are essential to life whereas others might be redundant.The review focuses on the most recent genetic and molecular biological studies of the matrix proteoglycans, broadly defined as proteoglycans secreted into the pericellular matrix. Special emphasis is placed on the molecular organization of the protein core, the utilization of protein modules, the gene structure and transcriptional control, and the functional roles of the various proteoglycans. When possible, proteoglycans have been grouped into distinct gene families and subfamilies offering a simplified nomenclature based on their protein core design. The structure-function relationship of some paradigmatic proteoglycans is discussed in depth and novel aspects of their biology are examined. CONTENTS

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Structure and Chromosomal Localization of the Mouse Neurocan Gene

Cited by 28 publications

References 0 publications

Transient Expression of PG‐M/Versican, a Large Chondroitin Sulfate Proteoglycan in Developing Chicken Retina

Transient Expression of PG‐M/Versican, a Large Chondroitin Sulfate Proteoglycan in Developing Chicken Retina

Neurocan Is Dispensable for Brain Development

MATRIX PROTEOGLYCANS: From Molecular Design to Cellular Function

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