Critical Factors in Basal Cell Adhesion Molecule/Lutheran-mediated Adhesion to Laminin

Zen, Qin; Cottman, Maisha J.; Truskey, George A.; Fraser, Robin; Telen, Marilyn J.

doi:10.1074/jbc.274.2.728

Cited by 81 publications

(79 citation statements)

References 25 publications

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“…El Nemer et al and our work showed that the ability of RBC to bind soluble laminin increases with increased expression of B-CAM/LU [20][21][22]. However, data from Lee and colleagues have suggested that HD SS RBC account for the SS RBC most adherent to immobilized laminin during continuous flow exerting the physiological shear stress of 1 dyne/cm 2 [16].…”

Section: Introductionmentioning

confidence: 80%

“…The anti-Lu b monoclonal antibody (mAb) LM342/767:31 was generously provided by Dr. Robin Fraser (Glasgow and West Scotland Blood Transfusion Service, UK) [21]. Rabbit anti-human laminin was obtained from Invitrogen Life Technologies (Carlsbad, CA).…”

Section: Antibodiesmentioning

confidence: 99%

“…B-CAM/LU comprises two protein spliceoforms derived from a single gene; B-CAM lacks the last 40 cytosolic amino acids of the LU protein [18,19]. Both spliceoforms contain five identical extracellular immunoglobulin (Ig) superfamily (SF) domains, and both B-CAM and LU recombinant proteins expressed on the cell surface bind well to soluble and immobilized laminin [20,21]. Our previous studies of SS RBC showed about 50% more B-CAM/LU molecules on lowdensity (LD) SS RBC enriched in reticulocytes than on high-density (HD) SS RBC [21,22] and SS reticulocytes themselves express about four times as much B-CAM/LU than do mature SS RBC [20].…”

Section: Introductionmentioning

confidence: 99%

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B‐CAM/LU expression and the role of B‐CAM/LU activation in binding of low‐ and high‐density red cells to laminin in sickle cell disease

et al. 2004

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Red blood cells from patients with sickle cell disease (SS RBC) adhere to laminin and over-express the high-affinity laminin receptor basal cell adhesion molecule/Lutheran protein (B-CAM/LU). This receptor has recently been shown to undergo activation in vitro through a protein kinase A-dependent mechanism. Low-density SS RBC express twothirds more B-CAM/LU than high-density SS RBC. However, high-density SS RBC have been identified as most adherent to laminin under flow conditions. We investigated the ability of low-and high-density SS RBC to interact with laminin under various conditions and explored factors that might be responsible for the differences in B-CAM/LU-laminin interaction between high-and low-density SS RBC. We confirmed that high-density SS RBC adhere to laminin more strongly than low-density SS RBC under flow conditions. However, low-density SS RBC bind soluble laminin most strongly and are the most adherent to laminin under static conditions. Soluble recombinant Lutheran extracellular domain protein completely blocked SS RBC adhesion to laminin under both static and flow conditions. The protein kinase A inhibitor 14-22 amide inhibited adhesion to laminin during flow by high-density SS RBC from patients with strongly adherent cells but had no effect on adhesion observed after a static phase. Deletion of the cytoplasmic domain of B-CAM as well as mutation of the juxtamembranous tyrosine residue failed to reduce B-CAM-mediated adhesion to laminin by transfected MEL cells. These studies confirm that B-CAM/LU is the most critical receptor mediating adhesion to laminin under both static and flow conditions. Dense SS RBC are most adherent to laminin despite bearing fewer laminin receptors, apparently due to a reversible protein kinase A-dependent process that is unlikely to involve direct phosphorylation of B-CAM/LU. Our results also suggest that the nature of the interaction of B-CAM/LU with laminin may be different under static and flow conditions. Am.

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Section: Introductionmentioning

confidence: 80%

Section: Antibodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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B‐CAM/LU expression and the role of B‐CAM/LU activation in binding of low‐ and high‐density red cells to laminin in sickle cell disease

et al. 2004

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“…Another potential non-integrin receptor for laminin ␣5 is the Lutheran blood group glycoprotein (Lu), which is a member of the Ig superfamily. A splice variant of Lu is known as basal cell adhesion molecule (B-CAM) (19,20). Lu/B-CAM has been studied primarily in the contexts of blood group antigens, sickle cell disease, and cancer (20 -26).…”

mentioning

confidence: 99%

Identification of the Binding Site for the Lutheran Blood Group Glycoprotein on Laminin α5 through Expression of Chimeric Laminin Chains in Vivo

Kikkawa¹,

Moulson²,

Virtanen

et al. 2002

Journal of Biological Chemistry

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The Lutheran blood group glycoprotein (Lu), also known as basal cell adhesion molecule, is an Ig superfamily transmembrane receptor for laminin ␣5. Lu is expressed on the surface of a subset of muscle and epithelial cells in diverse tissues and is thought to be involved in both normal and disease processes, including sickle cell disease and cancer. Here we investigated the binding of Lu to laminin ␣5 in vivo and in vitro. We prepared a soluble recombinant Lu (sol-Lu) composed of the Lu extracellular domain and a His 6 tag. Sol-Lu bound specifically to laminin-10/11 (␣5␤1/␤2␥1) in enzyme-linked immunosorbent assays and bound to bona fide basement membranes containing laminin ␣5 in tissue sections. Sol-Lu did not bind to tissue sections of laminin ␣5 knockout embryos, despite the fact that the four other ␣ chains were present. To identify the Lubinding site on laminin ␣5, we prepared modified ␣5 cDNAs encoding chimeric laminins containing all or part of the laminin ␣1 G domain in place of the analogous ␣5 regions. These constructs were used to generate transgenic mice. Proteins derived from transgenes were detected in basement membranes and were assayed for their ability to bind Lu by examining the localization of endogenous Lu and the binding of sol-Lu applied to tissue sections. Our results demonstrate that the ␣5 LG3 module is essential for Lu binding to laminin ␣5.

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“…28 Lutheran protein is involved in basal cell adhesion 30 and functions as a laminin receptor. 31 It is specifically expressed at the BBB compared with liver and kidney and can be used as a BBB marker in brain. 32 CD46 is a regulator of complement activation, has been shown to actively bind the measles virus, 33 and thus could potentially function in measles virus entry into the brain.…”

Section: Membrane Proteomics and Subtractive Antibody Expression Cloningmentioning

confidence: 99%

Blood-brain barrier genomics, proteomics, and new transporter discovery

Shusta

2005

Neurotherapeutics

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Summary:The blood-brain barrier (BBB) is an impermeable cellular interface that physically separates the blood from the interstices of the brain. The endothelial cells lining the brain blood vessels form the principle barrier, and their unique phenotype is a consequence of dynamic interactions with several perivascular cell types present in the brain parenchyma. In addition, BBB dysfunction has been observed in the large majority of neurological diseases, but the causes of aberrant vascular behavior are generally unknown. Because of its barrier phenotype, drug delivery to the brain has also proven to be a very difficult task. Global genomics and proteomics analyses are currently being used to examine BBB function in healthy and diseased brain to better characterize this dynamic interface. It is becoming increasingly evident that these approaches have the potential to clarify the unique attributes of a healthy BBB, to identify therapeutic targets in diseased brain, and to identify novel conduits for noninvasive delivery of drugs against these targets. This review will discuss the application of genomics and proteomics to blood-brain barrier research and will offer views on the prospects of such approaches.

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Critical Factors in Basal Cell Adhesion Molecule/Lutheran-mediated Adhesion to Laminin

Cited by 81 publications

References 25 publications

B‐CAM/LU expression and the role of B‐CAM/LU activation in binding of low‐ and high‐density red cells to laminin in sickle cell disease

B‐CAM/LU expression and the role of B‐CAM/LU activation in binding of low‐ and high‐density red cells to laminin in sickle cell disease

Identification of the Binding Site for the Lutheran Blood Group Glycoprotein on Laminin α5 through Expression of Chimeric Laminin Chains in Vivo

Blood-brain barrier genomics, proteomics, and new transporter discovery

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