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Perlecan is essential for cartilage and cephalic development

Nature Genetics, 1999
Perlecan, a large, multi-domain, heparan sulfate proteoglycan originally identified in basement membrane, interacts with extracellular matrix proteins, growth factors and receptors, and influences cellular signalling. Perlecan is present in a variety of basement membranes and in other extracellular matrix structures. We have disrupted the gene encoding
Yoshihiko Yamada   +4 more
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PerleCan fix your muscle AChEs

Trends in Neurosciences, 2003
Efficient and accurate synaptic transmission requires proper localization of numerous signaling proteins in the synaptic membrane. At the neuromuscular junction, the nicotinic ACh receptor mediates postsynaptic depolarization, and acetylcholinesterase (AChE) terminates this process by hydrolyzing ACh.
Michelle S. Steen, Stanley C. Froehner
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Perlecan: A gem of a proteoglycan

Matrix Biology, 1994
Perlecan, the main proteoglycan of basement membranes and pericellular spaces, is one of the largest single-chain polypeptides of vertebrate animals. The five modules of perlecan are collated from protein building blocks evolutionarily related to molecules involved in nutrient metabolism, mitogenesis and adhesion.
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Role of perlecan in skeletal development and diseases

Glycoconjugate Journal, 2002
Perlecan, a large heparan sulfate proteoglycan (HSPG), is present in the basement membrane and other extracellular matrices. Its protein core is 400 kDa in size and consists of five distinct structural domains. A number of in vitro studies suggest multiple functions of perlecan in cell growth and differentiation and tissue organization.
Eri Arikawa-Hirasawa   +2 more
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Perlecan Group

2012
Chapter 26 covers disorders of the Perlecan group (dyssegmental dysplasia, Silverman-Handmaker type (MIM 224410), dyssegmental dysplasia, Rolland-Desbuquois type (MIM 224400), Schwartz-Jampel syndrom (MIM 255800)) , including major clinical findings, radiographic features, and differential diagnoses.
Jürgen W. Spranger   +4 more
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Colocalization in vivo and association in vitro of perlecan and elastin

Histochemistry and Cell Biology, 2011
We have colocalized elastin and fibrillin-1 with perlecan in extracellular matrix of tensional and weight-bearing connective tissues. Elastin and fibrillin-1 were identified as prominent components of paraspinal blood vessels, and posterior longitudinal ligament in the human fetal spine and outer annulus fibrosus of the fetal intervertebral disc.
Anthony James Hayes   +6 more
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