CDB15:0000997 LAMA5 — ITGB1

Experimentally validated in Human, Mixed species; Orthology-inferred in Human, Mouse, Rat, Frog, Zebrafish, Chicken, Macaque, Pig, Dog, Cow, Chimp, Horse, Marmoset, Sheep

Title

Journal:; Year Published:

Abstract

Characterization of bone marrow laminins and identification of alpha5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells.

Blood, 1999; PubMed, Homo sapiens LAMA5 — Mus Musculus Itgb1
ABSTRACT: Laminins are extracellular matrix glycoproteins that influence the phenotype and functions of many types of cells. Laminins are heterotrimers composed of alpha, beta, and gamma polypeptides. So far five alpha, three beta, and two gamma polypeptide chains, and 11 variants of laminins have been proposed. Laminins interact in vitro with mature blood cells and malignant hematopoietic cells. Most studies have been performed with laminin-1 (alpha1beta1gamma1), and its expression in bone marrow is unclear. Employing an antiserum reacting with most laminin isoforms, we found laminins widely expressed in mouse bone marrow. However, no laminin alpha1 chain but rather laminin alpha2, alpha4, and alpha5 polypeptides were found in bone marrow. Our data suggest presence of laminin-2 (alpha2beta1gamma1), laminin-8 (alpha4beta1gamma1), and laminin-10 (alpha5beta1gamma1) in bone marrow. Northern blot analysis showed expression of laminin alpha1, alpha2, alpha4, and alpha5 chains in long-term bone marrow cultures, indicating upregulation of laminin alpha1 chain expression in vitro. Laminins containing alpha5 chain, in contrast to laminin-1, were strongly adhesive for multipotent hematopoietic FDCP-mix cells. Integrin alpha6 and beta1 chains mediated this adhesion, as shown by antibody perturbation experiments. Our findings indicate that laminins other than laminin-1 are functional in adhesive interactions in bone marrow.

Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins.

Matrix biology : journal of the International Society for Matrix Biology, 2006; PubMed, Homo sapiens LAMA5 — Homo sapiens ITGB1
ABSTRACT: The interactions of cells with basement membranes are primarily mediated via the engagement of laminins by a group of integrin family proteins, including integrins alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4. To explore the ligand-binding specificities of these laminin-binding integrins, we produced these integrins, including two alpha7beta1 splice variants (alpha7X1beta1 and alpha7X2beta1), as soluble recombinant proteins and determined their binding specificities and affinities toward a panel of purified laminin isoforms containing distinct alpha chains. Among the five laminin-binding integrins investigated, alpha3beta1 and alpha6beta4 exhibited a clear specificity for laminin-332 (alpha3beta3gamma2) and laminin-511 (alpha5beta1gamma1)/521 (alpha5beta2gamma1), while integrin alpha6beta1 showed a broad specificity, binding to all laminin isoforms with a preference for laminin-111 (alpha1beta1gamma1), laminin-332 and laminin-511/521. The two alpha7beta1 variants were distinct from alpha3beta1, alpha6beta1 and alpha6beta4 in that they did not bind to laminin-332. alpha7X1beta1 bound to all laminins, except laminin-332, with a preference for laminin-211 (alpha2beta1gamma1)/221 (alpha2beta2gamma1) and laminin-511/521, while alpha7X2beta1 bound preferentially to laminin-111 and laminin-211/221. Laminin-511/521 was the most preferred ligand for all the laminin-binding integrins, except for alpha7X2beta1, whereas laminin-411 was the poorest ligand, capable of binding to alpha6beta1 and alpha7X1beta1 with only modest binding affinities. These comprehensive analyses of the interactions between laminin-binding integrins and a panel of laminins clearly demonstrate that the isoforms of both integrins and laminins differ in their binding specificities and affinities, and provide a molecular basis for better understanding of the adhesive interactions of cells with basement membranes of defined laminin compositions.

Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. laminin-10/11 mediates cell adhesion through integrin alpha3 beta1.

The Journal of biological chemistry, 1998; PubMed, Homo sapiens LAMA5 — Homo sapiens ITGB1
ABSTRACT: A panel of human tumor cell lines was screened for selective expression of laminin alpha5 chain, a newly identified laminin subunit comprising laminin-10 (alpha5 beta1 gamma1) and -11 (alpha5 beta2 gamma1). The lung adenocarcinoma cell line A549 was found to express the alpha5 chain at relatively high levels but no detectable amounts of other alpha chains. The laminin variants containing alpha5 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 alpha5 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-alpha5 chain monoclonal antibody capable of recognizing denatured alpha5 chain on immunoblots, whereas the 210-kDa chain was recognized by an anti-gamma1 chain antibody. The purified alpha5 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 alpha3 or beta1 subunit but not by those against alpha2 or alpha6 subunit, indicating that laminin-10/11 is specifically recognized by integrin alpha3 beta1. Given the wide distribution of laminin-10/11 in the basement membrane of various tissue types and dominant expression of integrin alpha3 beta1 in most epithelial cells, specific interaction of laminin-10/11 with integrin alpha3 beta1 may play an important role in in vivo regulation of proliferation and differentiation of epithelial cells through the basement membrane.
Basic Information on LAMA5
Ligand Name: laminin subunit alpha 5
Other Symbols: N/A
Ligand Location: secreted based on hpa, perplexity, uniprot
HGNC Gene Symbol Report: LAMA5
GeneCards: LAMA5
Interactions with other Receptors for LAMA5
Basic Information on ITGB1
Receptor Name: integrin subunit beta 1
Other Symbols: FNRB, MSK12, MDF2, CD29, GPIIA
Receptor Location: cell membrane based on hpa, perplexity, uniprot
HGNC Gene Symbol Report: ITGB1
GeneCards: ITGB1
HGNC Gene Group: CD molecules, Integrins
Interactions with other Ligands for ITGB1
ADAM12 — ITGB1ADAM15 — ITGB1ADAM17 — ITGB1ADAM2 — ITGB1ADAM9 — ITGB1ANGPT1 — ITGB1CD14 — ITGB1CHAD — ITGB1COL11A1 — ITGB1COL18A1 — ITGB1COL1A1 — ITGB1COL1A2 — ITGB1COL2A1 — ITGB1COL3A1 — ITGB1COL4A1 — ITGB1COL4A3 — ITGB1COL4A4 — ITGB1COL4A5 — ITGB1COL4A6 — ITGB1COL5A1 — ITGB1CXCL12 — ITGB1F13A1 — ITGB1FBLN1 — ITGB1FBN1 — ITGB1FGA — ITGB1VEGFD — ITGB1FN1 — ITGB1HSPG2 — ITGB1ICAM4 — ITGB1LAMA1 — ITGB1LAMA2 — ITGB1LAMA4 — ITGB1LAMB1 — ITGB1LAMB3 — ITGB1LAMC1 — ITGB1LAMC2 — ITGB1LGALS3BP — ITGB1MATN1 — ITGB1MDK — ITGB1NID1 — ITGB1NPNT — ITGB1PLG — ITGB1RELN — ITGB1SEMA7A — ITGB1SPP1 — ITGB1TGM2 — ITGB1THBS1 — ITGB1THBS2 — ITGB1TIMP2 — ITGB1TNC — ITGB1VCAM1 — ITGB1VCAN — ITGB1VEGFA — ITGB1VEGFC — ITGB1VTN — ITGB1ANGPTL2 — ITGB1CCN4 — ITGB1CLEC11A — ITGB1LGALS1 — ITGB1PLA2G2A — ITGB1SPON2 — ITGB1ADAM28 — ITGB1AGGF1 — ITGB1AGRN — ITGB1ANGPT2 — ITGB1ANGPTL4 — ITGB1CCN2 — ITGB1CCN3 — ITGB1CD40LG — ITGB1CDH1 — ITGB1COL10A1 — ITGB1COL11A2 — ITGB1COL13A1 — ITGB1COL4A2 — ITGB1COL8A1 — ITGB1COL8A2 — ITGB1CSPG4 — ITGB1CX3CL1 — ITGB1ICAM5 — ITGB1IL1B — ITGB1JAM2 — ITGB1L1CAM — ITGB1LAMA3 — ITGB1LAMB2 — ITGB1LGALS3 — ITGB1LGALS8 — ITGB1MFGE8 — ITGB1MIA — ITGB1NTN4 — ITGB1PLAUR — ITGB1SVEP1 — ITGB1TGFB1 — ITGB1TGFB3 — ITGB1THBS4 — ITGB1THY1 — ITGB1TIMP1 — ITGB1VWF — ITGB1