Neurite‐promoting activity from fetal skeletal muscle: Immunological comparison with laminin

Steele, John G.; Dalton, B. A.

doi:10.1002/jnr.490170205

Cited by 11 publications

(1 citation statement)

References 26 publications

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“…Other examples of laminin-like molecules are the neurite-promoting factors made in culture by Schwann cells and muscle cells. These factors bind to but are not inhibited by anti-laminin sera, which do inhibit the neurite-promoting activity of laminin from the embryonal rodent tumors, EHS and L2 (44)(45)(46)(47)(48)(49). These laminin-like factors have been reported to Biochemistry: Ehrig et al…”

Section: Discussionmentioning

confidence: 99%

Merosin, a tissue-specific basement membrane protein, is a laminin-like protein.

Ehrig

Leivo

Argraves

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

349

205

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Merosin is a basement membrane-associated protein found in placenta, striated muscle, and peripheral nerve. A 3.6-kilobase merosin cDNA clone was isolated from a placental cDNA expression library. The clone contained a 3.4-kilobase open reading frame, the 3' portion of which includes protein sequences of proteolytic fragments of merosin. The deduced amino acid sequence of the merosin polypeptide was similar to that of the COOH-terminal region of the 400-kDa A chain of laminin. This part of laminin forms the large globule at the end of the long arm of the laminin cross and is thought to contain the neurite-promoting site and the major cell binding site(s) in laminin. The sequence identity between merosin and the laminin A chain in this region is nearly 40%.An antiserum against a synthetic peptide from the middle ofthe merosin cDNA sequence identified a 300-kDa polypeptide in placental extracts, indicating that the merosin polypeptide is similar in size to the laminin A chain. Intact merosin was isolated from placental extracts and shown to be covalently associated with the laminin B chains and to have a cross-like structure similar to that of laminin. The similarities between merosin and laminin show that both proteins are members of the same family of basement membrane proteins.Merosin is a tissue-restricted basement-membrane protein (1). It is present in the trophoblast basement membrane of the human placenta and in basement membranes of striated muscle and Schwann cells. In the mouse, merosin is not present in the fetus and only appears in muscle and nerve after birth (1). This late developmental appearance suggests a role for merosin in the maturation or differentiation of tissues. These results parallel the limited expression of merosin in human malignant tumors (2, 56) and its absence in cultured cell lines (1), which are at a lower level of differentiation than their normal tissue counterparts. The interesting spatial and temporal expression of merosin prompted us to determine its structure as a step toward elucidating its function. As shown here, merosin is structurally related to laminin.In contrast to merosin, laminin is thought to be present in all basement membranes (3). It is a large glycoprotein composed of three polypeptide chains, a 400-kDa heavy (A) chain and two light (B) chains of about 200 kDa. The entire heavy chain of mouse laminin (4, 5) and part of the human laminin heavy chain (6) have been sequenced. The B1 and B2 light chains from mouse (7-9, 57), human (10, 11), and Drosophila (12, 13) have also been sequenced. The NH2-terminal twothirds of the A chain are homologous to the B1 and B2 chains but the COOH-terminal one-third has a distinct structure.Laminin promotes attachment, spreading, motility, and growth of a variety of cell types (14)(15)(16)(17)(18). One of the most striking activities of laminin is its capacity to promote outgrowth of neurites from cultured neuronal cells (19)(20)(21). A major site of cell adhesion and the neurite-promoting activity appears to reside in or...

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Section: Discussionmentioning

confidence: 99%

Merosin, a tissue-specific basement membrane protein, is a laminin-like protein.

Ehrig

Leivo

Argraves

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

349

205

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Modulation of corneal epithelial stratification by polymer surface topography

Dalton

Evans

McFarland

et al. 1999

J. Biomed. Mater. Res.

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The topography and porosity of a polymer may affect the epithelialization of a corneal implant. We used an in vitro model to examine the effect of polymer surface topography on corneal epithelial tissue stratification and the deposition of proteins associated with epithelial adhesion. A range of topographies was provided by polycarbonate membranes with nominal pore diameters of 0.1, 0.4, 0.8, 1.0, 2.0, or 3.0 microm and a nonporous surface. Stratification of epithelial tissue outgrowth on these surfaces was evaluated using light and electron microscopy. Deposition of proteins associated with basement membrane and adhesion complex formation at the tissue-polymer interface was assessed using immunohistochemistry. Surfaces with pores in the 0.1-0.8-microm-diameter range supported superior stratification and protein deposition compared with those containing pores of > or = 1.0 microm. Cytoplasmic processes penetrated single pores 2.0 and 3.0 microm in diameter and fused pores 1.0 microm in diameter. Tissue on the nonporous surface had a lower level of stratification compared with surfaces with pores 0.1-0.8 microm in diameter. These results point to the significance of surface topography in biomaterial applications that require persistent epithelialization.

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Cell growth on metallic glasses: The interaction of amorphous metal alloys with cultured neuronal, osteoblast, endothelial, and fibroblast cells

McAuslan

Johnson

Delamore

et al. 1988

J. Biomed. Mater. Res.

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Ferrous based, corrosion resistant amorphous alloys supported the adhesion and growth of cultured chick neuronal cells, human marrow stromal cells (presumptive osteoblasts), bovine aortal endothelial cells, and hamster kidney fibroblasts. Alloys of compositions Fe60Ni10Cr10P13C7, Fe70Cr10P13C7, and Fe70Cr10P13B7 were found to be suitable. In contrast the crystalline form of these alloys was markedly less effective. Outgrowth of neurites from neuronal cells was promoted by precoating the metal surface with either laminin or neurite promotion factor. The adhesion of osteoblasts and fibroblasts suggests that corrosion resistant metal glasses should be considered as biomaterials useful for orthopedic applications. The adhesion of neuronal cells accompanied by neurite outgrowth indicates that the system might provide a functional interface between the neuromuscular system and an electromagnetic material that could be useful in bionic engineering.

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Neurite‐promoting activity from fetal skeletal muscle: Immunological comparison with laminin

Cited by 11 publications

References 26 publications

Merosin, a tissue-specific basement membrane protein, is a laminin-like protein.

Merosin, a tissue-specific basement membrane protein, is a laminin-like protein.

Modulation of corneal epithelial stratification by polymer surface topography

Cell growth on metallic glasses: The interaction of amorphous metal alloys with cultured neuronal, osteoblast, endothelial, and fibroblast cells

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