Identification of a 110-kDa nonintegrin cell surface laminin-binding protein which recognizes an a chain neurite-promoting peptide

Kleinman, Hynda K.; Weeks, Benjamin S.; Cannon, Frances B.; Sweeney, Thomas M.; Sephel, Gregory C.; Clément, Bruno; Zain, Mona; Olson, Matthew S.; Jucker, Mathias; Burrous, Beth A.

doi:10.1016/0003-9861(91)90547-v

Cited by 127 publications

(74 citation statements)

References 32 publications

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“…Nucleolin can interact with the IKVAV site of laminin, which is a major component of basement membranes (35,36). In the current study, we report evidence that NRP is located on both apical and basolateral surfaces of tubular epithelial cells, to a greater degree during proliferation and just afterward, compared with when they have become quiescent.…”

Section: Discussionsupporting

confidence: 54%

An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells

Сорокина¹,

Wesson²,

Kleinman³

2004

Journal of the American Society of Nephrology

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Abstract. Crystals that form in tubular fluid must be retained in the kidney to become stones. Nucleolin-related protein (NRP) is found on the surface of inner medullary collecting duct (IMCD) cells in culture (cIMCD) and selectively adsorbs to calcium oxalate (CaOx). We proposed that NRP mediates attachment to the renal tubular epithelium of Ca stone crystals through an electrostatic interaction with a highly acidic region (acidic fragment [AF]) similar to those of other proteins that have been reported to affect urinary crystal formation. The current studies demonstrate that nucleolin is expressed on both apical and basolateral cell surfaces of cIMCD, reaching a peak in the late stages of mitosis and gradually declining to undetectable levels with maturation of the polarized epithelium. Scraping areas of mature monolayers stimulated the cells surrounding the defects to migrate and proliferate so as to repair them, and these areas demonstrate surface NRP expression and enhanced attachment of CaOx monohydrate crystals. Surface expression of the NRP AF was produced by cloning the NRP AF into a display vector. Transfected cIMCD demonstrating copious surface expression of AF enhanced CaOx attachment 6.7-fold compared with control cIMCD, whereas cells transfected with a vector without the AF did not differ from control. AF was also cloned into a replication-deficient adenovirus and expressed in 293 cells, resulting in AF secretion into the nutrient medium. This medium inhibited CaOx attachment to cIMCD, compared with conditioned medium from cells infected with wild-type virus. These results demonstrate that surface-bound AF can mediate CaOx attachment and that secreted AF can inhibit attachment. These results support the notion that surface-associated NRP could mediate attachment of CaOx to the renal tubule epithelium, thereby causing retention of crystals that might eventually become kidney stones.Several groups of investigators have suggested that an important early event in the formation of kidney stones is the attachment of calcium oxalate (CaOx) crystals to the apical surface of renal tubular epithelium (1-3). Well-polarized, undisturbed tubular epithelial cells in culture demonstrate little capacity for crystal attachment (4 -6). This resistance to attachment may be due to the confinement of molecules with crystal-binding properties to domains other than the apical membrane. When tight junctions between cells are disrupted in the course of cellular proliferation or migration or when cells are exposed to a number of different agents, apical membranes seem to express constituents with affinity for CaOx.Nucleolin-related protein (NRP) is a surface-associated protein of cultured inner medullary collecting duct (IMCD) cells that selectively adsorbs to CaOx and binds to membrane skeletal elements in a Ca-dependent manner (7). NRP has a highly acidic region composed of 62% Asp and Glu residues (135KNGKNAKKEDSDEEDDDDSEEEDEEDEDEEDEFE PTVMKAAAAAPAS-DEEEDDEEDDDEDDDEEDEDED-EDDSEEEAMETTPAKGKKAPVKAVPVKAKSTAEE-DEEEDDEDEEDDEE...

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Section: Discussionsupporting

confidence: 54%

An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells

Сорокина¹,

Wesson²,

Kleinman³

2004

Journal of the American Society of Nephrology

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“…Nucleolin has been implicated in various aspects of ribosome biogenesis (rDNA transcription, rRNA maturation, and ribosome assembly) and nucleocytoplasmic transport (20). Surprisingly, nucleolin was also reported to be located on the cell surface (8,13,35,40). We therefore localized nucleolin in cells used in this study.…”

Section: Midkine Is Internalized and Translocated To The Nucleusmentioning

confidence: 93%

Nuclear Targeting by the Growth Factor Midkine

Shibata

Muramatsu²,

Hirai

et al. 2002

Molecular and Cellular Biology

131

129

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Ligand-receptor internalization has been traditionally regarded as part of the cellular desensitization system. Low-density lipoprotein receptor-related protein (LRP) is a large endocytosis receptor with a diverse array of ligands. We recently showed that LRP binds heparin-binding growth factor midkine. Here we demonstrate that LRP mediates nuclear targeting by midkine and that the nuclear targeting is biologically important. Exogenous midkine reached the nucleus, where intact midkine was detected, within 20 min. Midkine was not internalized in LRP-deficient cells, whereas transfection of an LRP expression vector restored midkine internalization and subsequent nuclear translocation. Internalized midkine in the cytoplasm bound to nucleolin, a nucleocytoplasmic shuttle protein. The midkine-binding sites were mapped to acidic stretches in the N-terminal domain of nucleolin. When the nuclear localization signal located next to the acidic stretches was deleted, we found that the mutant nucleolin not only accumulated in the cytoplasm but also suppressed the nuclear translocation of midkine. By using cells that overexpressed the mutant nucleolin, we further demonstrated that the nuclear targeting was necessary for the full activity of midkine in the promotion of cell survival. This study therefore reveals a novel role of LRP in intracellular signaling by its ligand and the importance of nucleolin in this process.

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“…We demonstrated that the 67-kDa monomeric laminin receptor (67LR), which is overexpressed (Martignone et al, 1993;Ménard et al, 1998) and released by various tumor cell types (Karpatová et al, 1996;Starkey et al, 1999), changes the conformation of the laminin adhesion molecule upon binding to it . Because the integrin recognition domains of laminin appear to be conformation-dependent (Mercurio, 1995), 67LR-modified laminin interacts more readily with integrins and with other molecules that normally do not participate significantly in laminin binding to the cell surface (Ramos et al, 1990;Feldman et al, 1991;Kleinman et al, 1991;Magnifico et al, 1996). This mechanism provides the cells with a greater number of binding sites and modulates the interaction between tumor cells and laminin, with consequences for metastatic potential (Pellegrini et al, 1995).…”

Section: Unmasking Of Cryptic Sitesmentioning

confidence: 99%

New insights into the role of extracellular matrix during tumor onset and progression

Pupa

Ménard

Forti

et al. 2002

Journal Cellular Physiology

303

210

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Recently, a view of the tumor as a functional tissue interconnected with the microenvironment has recently been described. For many years, the stroma has been studied in the context of the malignant lesion, and only rarely has its role been considered before carcinogenic lesions appear. Recent studies have provided evidence that stromal cells and their products can cause the transformation of adjacent cells through transient signaling that leads to the disruption of homeostatic regulation, including control of tissue architecture, adhesion, cell death, and proliferation. It is now well established that tumor progression requires a continually evolving network of interactions between neoplastic cells and extracellular matrix. A relevant step of this process is the remodeling of microenvironment which surrounds tumors leading to the release of ECM-associated growth factors which can then stimulate tumor and/or endothelial cells. Finally, tumor cells reorganizing the extracellular matrix to facilitate communications and escape the homeostatic control exerted by the microenvironment modify response to cytotoxic treatments.

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Identification of a 110-kDa nonintegrin cell surface laminin-binding protein which recognizes an a chain neurite-promoting peptide

Cited by 127 publications

References 32 publications

An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells

An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells

Nuclear Targeting by the Growth Factor Midkine

New insights into the role of extracellular matrix during tumor onset and progression

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