The human α3b is a `full‐sized' laminin chain variant with a more widespread tissue expression than the truncated α3a

Doliana, Roberto; Bellina, Isabella; Bucciotti, Francesco; Mongiat, Maurizio; Perris, Roberto; Colombatti, Alfonso

doi:10.1016/s0014-5793(97)01251-9

Cited by 21 publications

(33 citation statements)

References 46 publications

(47 reference statements)

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“…␣5 and ␣3, seem to be evolutionally the most related among five different laminin ␣ chains (38). A full sized laminin ␣3 chain, ␣3B, was identified recently in mouse and human, showing the highest homology to the ␣5 chain at the amino acid level (4,38). Despite these similarities, however, it should be noted that morphologies of cells adhering onto surfaces coated with either laminin-10/11 or laminin-5 were significantly different.…”

Section: Discussionmentioning

confidence: 99%

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Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells

Kikkawa

Sanzen

Sekiguchi

1998

Journal of Biological Chemistry

194

151

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A panel of human tumor cell lines was screened for selective expression of laminin ␣5 chain, a newly identified laminin subunit comprising laminin-10 (␣5␤1␥1) and -11 (␣5␤2␥1). The lung adenocarcinoma cell line A549 was found to express the ␣5 chain at relatively high levels but no detectable amounts of other ␣ chains. The laminin variants containing ␣5 chain were purified from the conditioned medium of A549 cells by immunoaffinity chromatography using the anti-laminin monoclonal antibody 4C7 which was shown recently to recognize the laminin ␣5 chain (Tiger, C.-F., Champliaud, M.-F., Pedrosa-Domellof, F., Thornell, L.-E., Ekblom, P., and Gullberg, D. (1997) J. Biol. Chem. 272, 28590 -28595). The purified laminin variants consisted of three chains with molecular masses of 350, 220, and 210 kDa. The 350-kDa chain was specifically recognized by another anti-␣5 chain monoclonal antibody capable of recognizing denatured ␣5 chain on immunoblots, whereas the 210-kDa chain was recognized by an anti-␥1 chain antibody. The purified ␣5 chain-containing laminin variants (hereafter referred to as laminin-10/11) were highly active in mediating adhesion of A549 cells to the substratum with potency as high as that of laminin-5 and significantly higher than those of laminin-1, laminin-2/4, or fibronectin. Adhesion to substrata coated with laminin-10/11 was specifically inhibited by anti-integrin antibodies directed against the integrin ␣3 or ␤1 subunit but not by those against ␣2 or ␣6 subunit, indicating that laminin-10/11 is specifically recognized by integrin ␣3␤1. Given the wide distribution of laminin-10/11 in the basement membrane of various tissue types and dominant expression of integrin ␣3␤1 in most epithelial cells, specific interaction of laminin-10/11 with integrin ␣3␤1 may play an important role in in vivo regulation of proliferation and differentiation of epithelial cells through the basement membrane.

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Section: Discussionmentioning

confidence: 99%

“…Furthermore, the ␣ chains of laminin-10/11 and laminin-5, i.e. ␣5 and ␣3, seem to be evolutionally the most related among five different laminin ␣ chains (38). A full sized laminin ␣3 chain, ␣3B, was identified recently in mouse and human, showing the highest homology to the ␣5 chain at the amino acid level (4,38).…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells

Kikkawa

Sanzen

Sekiguchi

1998

Journal of Biological Chemistry

194

151

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“…The discovery of the ␣4 ) and ␣5 (Miner et al 1995) chains led to the identification of laminins 8 (␣4␤1␥1), -9 (␣4␤2␥1), -10 (␣5␤1␥1), and -11 (␣5␤2␥1). Laminin ␣-chains vary in size; the ␣1 ‫004ف(‬ kD), ␣2, ␣3b ‫063ف(‬ kD) (Doliana et al 1997;Miner et al 1997), and ␣5 ‫054ف(‬ kD) chains are full-length chains, ␣5 being the largest, whereas the ␣3a and ␣4 ‫081ف(‬ kD) chains are considered as truncated chains (Figure 6). Interactions of cells with laminin ␣-chains are critical for cell-matrix interactions.…”

Section: New Additions To the Laminin Familymentioning

confidence: 99%

Still More Complexity in Mammalian Basement Membranes

Erickson

Couchman

2000

J Histochem Cytochem.

268

193

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At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new α-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.

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“…The laminin ␣3B chain has the highest homology to the ␣5 chain (14). Therefore, Lm3B11 is most close to Lm511 in structure.…”

Section: Discussionmentioning

confidence: 99%

“…Although the ␣3B chain is known to be more widely expressed than the ␣3A chain in vivo, ␣3B-containing laminins have been poorly investigated (12)(13)(14). We previously expressed laminin-3B32 (Lm3B32; ␣3B/␤3/␥2) as a recombinant protein and revealed its biological activity (15).…”

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confidence: 99%

Laminin-3B11, a Novel Vascular-type Laminin Capable of Inducing Prominent Lamellipodial Protrusions in Microvascular Endothelial Cells

Mori

Ono

Kariya

et al. 2010

Journal of Biological Chemistry

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The basement membrane (BM) proteins laminins, which consist of ␣, ␤, and ␥ chains, support tissue structures and cellular functions. To date only ␣4 and ␣5 types of laminins have been identified in the BMs of blood vessels. Our recent study suggested the presence of novel ␣3B-containing laminins in vascular BMs. Here we identified and characterized the third member of vascular laminins, laminin-3B11 (Lm3B11). RT-PCR analysis showed that microvascular endothelial (MVE) cells and umbilical vein endothelial cells expressed the messages for the ␣3B, ␤1, ␤2, and ␥1 chains. In the culture of MVE cells, ␣3B was associated with ␤1 and ␥1, producing Lm3B11. Recombinant Lm3B11 was overexpressed by introducing the cDNAs of the three chains into HEK-293 cells and purified to homogeneity. Purified Lm3B11 exhibited relatively weak cell adhesion activity through both ␣3␤1 and ␣6␤1 integrins. Most characteristically, Lm3B11 strongly stimulated MVE cells to extend many lamellipodial protrusions. This pseudopodial branching was blocked by an inhibitor for Src or phosphatidylinositol 3-kinase. Consistently, Lm3B11 stimulated the phosphorylation of Src and Akt more strongly than other laminins, suggesting that the integrinderived signaling is mediated by these factors. The unique activity of Lm3B11 appears to be favorable to the branching of capillaries and venules.Laminin, a family of large heterotrimeric glycoproteins consisting of ␣, ␤, and ␥ chains, is a major cell-adhesive component present in the basement membranes (BMs) 2 of various tissues. It plays critical roles in the maintenance of tissue architectures and the regulation of cellular functions such as cell adhesion, migration, proliferation, apoptosis, and differentiation (1). Different combinations of five ␣, three ␤, and three ␥ chains give rise to more than 15 laminin isoforms (2). These laminins are distributed in a tissue-specific manner and are thought to play differential roles in the individual tissues. Such specific distribution and function of laminins are mainly determined by the ␣ chains. For example, ␣2 laminins (laminin-211 and -221) are localized in the BMs of muscle and neurons, whereas ␣4 laminins (laminin-411 and -421) are localized in vascular BMs.There are two splicing variants of laminin ␣3 chain, the truncated form ␣3 (or ␣3A) and the full-sized form ␣3B (3, 4), gene expression of which is regulated by alternative splicing and different promoters (5). Laminin-3A32 (Lm3A32), which is previously known as laminin-5 and consists of all truncated chains (␣3A, ␤3, and ␥2), is a major laminin isoform in the skin, esophagus, lung, breast, and other epithelial tissues. This laminin has extensively been studied because it has unique structure and biological activity as compared with other laminins (6). In the skin, Lm3A32 in the BM associates with integrin ␣6␤4 of basal keratinocytes to form the hemidesmosome structures and contributes to their stable anchorage to the underlying connective tissues (7,8). The laminin ␣3A chain also associates with the full-siz...

show abstract

The human α3b is a `full‐sized' laminin chain variant with a more widespread tissue expression than the truncated α3a

Cited by 21 publications

References 46 publications

Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells

Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells

Still More Complexity in Mammalian Basement Membranes

Laminin-3B11, a Novel Vascular-type Laminin Capable of Inducing Prominent Lamellipodial Protrusions in Microvascular Endothelial Cells

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