Laminin Expression in Adult and Developing Retinae: Evidence of Two Novel CNS Laminins

Libby, Richard T.; Champliaud, Marie-France; Claudepierre, Thomas; Xu, Yin; Gibbons, Erin; Koch, Manuel; Burgeson, Robert E.; Hunter, Dale D.; Brunken, William J.

doi:10.1523/jneurosci.20-17-06517.2000

Cited by 250 publications

(250 citation statements)

References 62 publications

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“…These laminin family members are not present in the ILM, and they have a function in the survival of photo receptors. 21 The origin from extra-retinal tissues infers that the ILM proteins are shed from ciliary body and lens into the vitreous to have access to the retinal neuroepithelium. Indeed, western blot analysis in chick and human confirmed that all ILM proteins are present in relative Figure 2 In situ hybridization of E6 chick eye with cRNA probes for the laminin g1 chain (a), collagen IV a1 (b) and nidogen-1 (c).…”

Section: Origin Of the Ilm Proteins In The Developing Eyementioning

confidence: 99%

Origin and turnover of ECM proteins from the inner limiting membrane and vitreous body

Halfter

Dong

et al. 2008

Eye

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The inner limiting membrane (ILM) and the vitreous body (VB) are two major extracellular matrix (ECM) structures that are essential for early eye development. The ILM is considered to be the basement membrane of the retinal neuroepithelium, yet in situ hybridization and chick/quail transplant experiments in organcultured eyes showed that all components critical for ILM assembly, such as laminin or collagen IV, are not synthesized by the retina. Rather, ILM proteins, with the exception of agrin, originate from the lens or (and) ciliary body and are shed into the vitreous. The VB serves as a reservoir providing high concentrations of ILM proteins for the instant assembly of new ILM during rapid embryonic eye growth. The function of the retina in ILM assembly is to provide the cellular receptor proteins for the binding of the ILM proteins from the vitreous. The VB is a gelatinous ECM structure that fills the vitreous cavity of the eye. Its major structural proteins, collagen II and fibrillin, originate primarily from the ciliary body. Reverse transcription-PCR and western blotting show that the rate of synthesis of structural, monomeric ILM and VB proteins, such as laminin, collagen IV and II is very high during embryogenesis and very low in the adult. The downregulation of ILM and VB protein synthesis occurs during early postnatal life, and both ILM and VB are from then on maintained throughout life with minimum turnover. Our data explain why ILM and VB do not regenerate after vitrectomy and ILM peeling.

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Section: Origin Of the Ilm Proteins In The Developing Eyementioning

confidence: 99%

Origin and turnover of ECM proteins from the inner limiting membrane and vitreous body

Halfter

Dong

et al. 2008

Eye

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“…Immunoprecipitation-NHKs and HT1080 cells were metabolically labeled with 100 Ci/ml sodium [ 35 S]sulfate (Na 2 35 SO 4 ) (PerkinElmer Life Sciences) for 16 h. After labeling, the cell layers were washed with PBS and extracted with RIPA buffer on ice for 10 min. All the following procedures were performed at 4°C.…”

Section: Purification Of the Recombinant ␣3lg4/5 Fragment In Mammalianmentioning

confidence: 99%

“…Immunoprecipitation experiments were therefore performed to identify the receptor. Capture of the proteoglycan-type receptor was carried out by incubating Na 2 35 SO 4 -labeled NHK or HT1080 cell lysates with beads that were immunologically covered with rLG4/5. Autoradiographic analysis of the bound material revealed a unique diffuse band of ϳ250 kDa for both cell types (Fig.…”

Section: Syndecan-1 Binding To Laminin ␣3lg4/5mentioning

confidence: 99%

“…At present, 15 heterotrimers termed LN-1 to LN-15 have been described with different subunit composition selected from five individual ␣ chains (␣1-␣5), three ␤ chains (␤1-␤3), and three ␥ chains (␥1-␥3) (1,2). All LN ␣ chains comprise a large globular domain in their carboxylterminal region (G domain), which consists of five homologous globular subdomains of about 200 amino acids each (LG1-LG5).…”

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confidence: 99%

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Normal Human Keratinocytes Bind to the α3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1

Okamoto

Bachy

Odenthal³

et al. 2003

Journal of Biological Chemistry

101

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Basal keratinocytes of the epidermis adhere to their underlying basement membrane through a specific interaction with laminin-5, which is composed by the association of ␣3, ␤3, and ␥2 chains. Laminin-5 has the ability to induce either stable cell adhesion or migration depending on specific processing of different parts of the molecule. One event results in the cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5) of the ␣3 chain. In this study, we recombinantly expressed the human ␣3LG4/5 fragment in mammalian cells, and we show that this fragment induces adhesion of normal human keratinocytes and fibrosarcoma-derived HT1080 cells in a heparan-and chondroitin sulfate-dependent manner. Immunoprecipitation experiments with Na 2 35 SO 4 -labeled keratinocyte and HT1080 cell lysates as well as immunoblotting experiments revealed that the major proteoglycan receptor for the ␣3LG4/5 fragment is syndecan-1. Syndecan-4 from keratinocytes also bound to ␣3LG4/5. Furthermore we could show for the first time that unprocessed laminin-5 specifically binds syndecan-1, while processed laminin-5 does not. These results demonstrate that the LG4/5 modules within unprocessed laminin-5 permit its cell binding activity through heparan and chondroitin sulfate chains of syndecan-1 and reinforce previous data suggesting specific properties for the precursor molecule.Laminins (LNs) 1 are extracellular matrix glycoproteins composed of ␣, ␤, and ␥ chains assembled into a cross-shaped heterotrimer (␣␤␥) by forming a triple-stranded coiled-coil structure through their ␣-helical domains. At present, 15 heterotrimers termed LN-1 to LN-15 have been described with different subunit composition selected from five individual ␣ chains (␣1-␣5), three ␤ chains (␤1-␤3), and three ␥ chains (␥1-␥3) (1, 2). All LN ␣ chains comprise a large globular domain in their carboxylterminal region (G domain), which consists of five homologous globular subdomains of about 200 amino acids each (LG1-LG5). LN-5, with chain composition ␣3␤3␥2, is a component of basement membranes underlying specialized epithelia with secretory or protective function (3). In skin, LN-5 is synthesized by keratinocytes initially as a high molecular mass precursor protein of 460 kDa of which the ␣3 and ␥2 chains undergo specific processing to smaller forms after being secreted and deposited into the extracellular matrix (ECM) (4, 5). Processing of the ␣3 chain consists of cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5) (6, 7). An additional cleavage within the aminoterminal domain IIIa of the ␣3 chain occurs subsequently and may also be important for LN-5 function (8, 9). Processing of the ␥2 chain occurs at the amino terminus with loss of a 50-kDa domain (9 -11). Processed LN-5 is the major component of anchoring filaments in skin (12) where it mediates cell adhesion via interaction of the ␣3 carboxyl-terminal LG1-3 triplet domain with both ␣ 3 ␤ 1 and ␣ 6 ␤ 4 integrins (13-16). Several studies have suggested that processed LN-5 functions both in the nuclea...

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“…Fifteen LN isoforms have been identified. 1 LN isoforms are tissue-specific and expressed in a developmentally regulated pattern. 2,3 Cell adhesion to LN plays an important role in maintaining normal tissue organization.…”

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confidence: 99%

Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin‐3 and supports cell migration

Paret

Bourouba

et al. 2005

Intl Journal of Cancer

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C4.4A is a member of the Ly6 family, with low homology to uPAR. It has been detected mainly on metastasizing carcinoma cells and proposed to be involved in wound healing. So far, C4.4A has been observed as an orphan receptor, and its functional activity has not been explored. Using recombinant rat C4.4A (rrC4.4A) made in a eukaryotic expression system, we demonstrate by immunohistology that C4.4A ligands are strongly expressed in tissues adjacent to squamous epithelia of, e.g., tongue and esophagus, the expression pattern partly overlapping with laminin (LN) and complementing the C4.4A expression that is found predominantly on the basal layers of squamous epithelium. ELISA screening of several components of the extracellular matrix revealed selective binding of rrC4.4A to LN1 and LN5 and that transfection of the BSp73AS tumor line with C4.4A cDNA (BSp73AS-1B1) promoted LN1 and LN5 binding. Binding of BSp73AS-1B1 to LN5 and, less markedly, LN1 induced spreading, lamellipodia formation and migration. C4.4A also associates with galectin-3 in nontransformed tissues and tumor lines. There is evidence that the association of C4.4A with galectin-3 influences LN adhesion. C4.4A was described originally as a metastasis-associated molecule. Our findings that LN1 and LN5 are C4.4A ligands, that galectin-3 associates with C4.4A and that C4.4A ligand binding confers a migratory phenotype are well in line with the supposed metastasis association. ' 2005 Wiley-Liss, Inc.Key words: C4.4A; laminin; galectin; cell migration LNs are adhesive glycoproteins found in the basement membrane. Fifteen LN isoforms have been identified. 1 LN isoforms are tissue-specific and expressed in a developmentally regulated pattern. 2,3 Cell adhesion to LN plays an important role in maintaining normal tissue organization. LNs promote cell adhesion and migration, 4 are involved in the control of cell proliferation and gene expression 5 and stimulate neurite outgrowth, 6 the multitude of functions being brought about by a large array of receptors. 7 The most prominent LN receptors are integrins, but distinct receptors have also been described, e.g., a-dystroglycan, syndecans, the 67 kDa LN receptor and galectins. 7,8 a-Dystroglycan provides a link between the basement membrane and the dystrophin-actin cytoskeleton. 9 Its binding to LN is Ca 2þ -dependent 10 and requires carbohydrate moieties. 11 Binding of syndecans 2 and 4 to LN5 induces expression of MMP-1. 12 Moreover, syndecan 1 interacts with unprocessed LN5 in migrating keratinocytes, and this interaction depends on the presence of the glycosaminoglycan chain. 13 Galectins belong to the family of galactose-specific lectins and bind the lactosamine-type sugars on LN1. 8 However, at high concentrations, galectins 3 and 1 can downregulate adhesion to LN, probably by blocking the cellular attachment sites. 14,15 The 67 kDa LN receptor can act in concert with a6b4 to promote cell adhesion to LN1. 16 It is also involved in the degradation of LN1 and the release of motility fragments. 17 The GPI-ancho...

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Laminin Expression in Adult and Developing Retinae: Evidence of Two Novel CNS Laminins

Cited by 250 publications

References 62 publications

Origin and turnover of ECM proteins from the inner limiting membrane and vitreous body

Origin and turnover of ECM proteins from the inner limiting membrane and vitreous body

Normal Human Keratinocytes Bind to the α3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1

Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin‐3 and supports cell migration

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