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Mononuclear leukocytes bind to specific hyaluronan structures on colon mucosal smooth muscle cells treated with polyinosinic acid:: Polycytidylic acid -: Inter-α-trypsin inhibitor is crucial to structure and function

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AMERICAN JOURNAL OF PATHOLOGY 2003年第1期163卷 121-133页

作者： de la Motte, CA Hascall, VC Drazba, J Bandyopadhyay, SK Strong, SA Cleveland Clin Fdn Lerner Res Inst Dept Colorectal Surg Cleveland OH 44195 USA Cleveland Clin Fdn Lerner Res Inst Dept Immunol Cleveland OH 44195 USA Cleveland Clin Fdn Dept Biomed Engn Cleveland OH 44195 USA Cleveland Clin Fdn Imaging Core Lab Cleveland OH 44195 USA

Inflammatory bowel disease (IBD) is a chronic disorder whose etiology is linked to triggering events, including viral infections, that lead to immunoregulatory dysfunction in genetically susceptible people. Characteristic pathological changes include increased mononuclear leukocyte influx into the intestinal mucosa as well as mucosal smooth muscle cell (M-SMC) hyperplasia. Virus infection or viral mimic [polyinosinic acid:polycytidylic acid (polyI:C)] treatment of human colon M-SMCs in vitro increases cell surface hyaluronan (HA), and nonactivated mononuclear leukocytes bind to virus-induced RA structures by interactions that involve the HA-binding receptor CD44. In this study, confocal microscopy reveals increased HA on poly I:C-treated M-SMC surfaces within 3 hours, arrayed in coat-like structures. By 17 hours, novel, lengthy cable structures are evident, and these are primarily responsible for mediating leukocyte adhesion. Immunohistochemical staining demonstrates components of the inter-alpha-trypsin inhibitor (IalphaI) complex in both coat-like and cable structures. M-SMCs co-treated with polyI:C and a polyclonal. antibody to IalphaI display RA in coats but with diminished cables, and they bind significantly fewer leukocytes than M-SMCs;treated with polyI:C alone. Western blot data suggest that heavy chains of IalphaI are specifically associated with cable structures. Staining of tissue sections from patients with IBD demonstrates the presence of RA in inflamed colon tissue, and shows that HA-associated IalphaI staining increases in the mucosa of inflamed IBD specimens compared to noninflamed sections from the same patient, establishing a probable link between the observations in vitro and the progression of the inflammatory process in IBD.

关键词：甲种球蛋白类/免疫学甲种球蛋白类/代谢抗病毒药/药理学细胞黏附/生理学细胞培养的硫酸软骨素蛋白聚糖类/代谢结肠/解剖学和组织学结肠/代谢结肠/病理学透明质酸/代谢炎症/代谢炎性肠疾病/免疫学炎性肠疾病/代谢炎性肠疾病/病理学肠黏膜/细胞学肠黏膜/代谢外源凝集素类 C型白细胞单核/代谢显微镜检查荧光肌细胞平滑肌/药物作用肌细胞平滑肌/代谢聚肌胞苷酸/药理学多功能蛋白聚糖类人类

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Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns - Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第42期275卷 33038-33045页

作者： Mercuri, FA Maciewicz, RA Tart, J Last, K Fosang, AJ Univ Melbourne Dept Paediat Orthopaed Mol Biol Res Unit Parkville Vic 3052 Australia Royal Childrens Hosp Murdoch Childrens Res Inst Parkville Vic 3052 Australia AstraZeneca Resp & Inflammat Res Dept Macclesfield SK10 4TG Cheshire England

We have expressed G1-G2 mutants with amino acid changes at the DIPEN(341)down arrow (342)FFGVG and ITEGE(373)down arrow (374)-ARGSV cleavage sites, in order to investigate the relationship between matrix metalloproteinase (MMP) and aggrecanase activities in the interglobular domain (IGD) of aggrecan. The mutation DIPEN341 to DIGSA(341) partially blocked cleavage by MMP-13 and MMP-8 at the MMP site, while the mutation (342)FFGVG to (342)GTRVG;completely blocked cleavage at this site by MMP-1, -2, -3, -7, -8, -9, -13, -14. Each of the MMP cleavage site mutants, including a four-amino acid deletion mutant lacking residues ENFF343, were efficiently cleaved by aggrecanase, suggesting that the primary sequence at the MMP site had no effect on aggrecanase activity in the IGD. The mutation (374)ARGSV to (NVYSV)-N-374 completely blocked cleavage at the aggrecanase site by aggrecanase, MMP-8 and atrolysin C but had no effect on the ability of MMP-8 and MMP-13 to cleave at the Asn(341)down arrow Phe bond. Susceptibility to atrolysin C cleavage at the MMP site was conferred in the DIGSA(341) mutant but absent in the wildtype, (342)GTRVG, (NVYSV)-N-374, and deletion mutants. To further explore the relationship between MMP and aggrecanase activities, sequential digest experiments were done in which MMP degradation products were subsequently digested with aggrecanase and vice versa. Aggrecanase-derived G1 domains with ITEGE(373) C termini were viable substrates for MMPs;however, MMP-derived G2 fragments were resistant to cleavage by aggrecanase. A 10-mer peptide FVDIPENFFG, which is a substrate analogue for the MMP cleavage site, inhibited aggrecanase cleavage at the Glu(373)down arrow Ala bond. This study demonstrates that MMPs and aggrecanase have unique substrate recognition in the IGD of aggrecan and suggests that sequences at the C terminus of the DIPEN341 G1 domain may be important for regulating aggrecanase cleavage.

关键词：软骨蛋白聚糖类氨基酸序列碱基序列结合部位硫酸软骨素蛋白聚糖类/化学硫酸软骨素蛋白聚糖类/代谢胶原酶类/代谢 DNA引物内肽酶类/代谢酶前体/代谢细胞外基质蛋白质类明胶酶类/代谢外源凝集素类 C型基质金属蛋白酶1 基质金属蛋白酶9/代谢基质金属蛋白酶类/代谢金属内肽酶类/代谢分子序列数据诱变定点蛋白聚糖类/化学蛋白聚糖类/遗传学蛋白聚糖类/代谢重组蛋白质类/化学重组蛋白质类/代谢斜纹夜蛾属底物特异性金属蛋白酶1组织抑制剂/代谢动物人类

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Proteoglycans in the developing brain: New conceptual insights for old proteins

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PHYSIOLOGICAL REVIEWS 2000年第4期80卷 1267-1290页

作者： Bandtlow, CE Zimmermann, DR Univ Zurich Brain Res Inst CH-8057 Zurich Switzerland Swiss Fed Inst Technol Zurich Switzerland Univ Zurich Hosp Dept Pathol Mol Biol Lab CH-8091 Zurich Switzerland

Proteoglycans are a heterogeneous class of proteins bearing sulfated glycosaminoglycans. Some of the proteoglycans have distinct core protein structures, and others display similarities and thus may be grouped into families such as the syndecans, the glypicans, or the hyalectans (or lecticans). Proteoglycans can be found in almost all tissues being present in the extracellular matrix, on cellular surfaces, or in intracellular granules. In recent years, brain proteoglycans have attracted growing interest due to their highly regulated spatiotemporal expression during nervous system development and maturation. There is increasing evidence that different proteoglycans act as regulators of cell migration, axonal pathfinding, synaptogenesis, and structural plasticity. This review summarizes the most recent data on structures and functions of brain proteoglycans and focuses on new physiological concepts for their potential roles in the developing central nervous system.

关键词：轴突/生理学脑/胚胎学脑/生长和发育脑/代谢细胞运动硫酸软骨素蛋白聚糖类/代谢葡糖氨基聚糖类/代谢类肝素硫酸蛋白聚糖类/代谢配体膜糖蛋白类/代谢神经组织蛋白质类/代谢神经突/生理学神经胶质/细胞学神经胶质/代谢神经元可塑性/生理学神经元/细胞学神经元/代谢蛋白质酪氨酸磷酸酶类/代谢蛋白聚糖类/代谢受体样蛋白质酪氨酸磷酸酶类 5类突触传递/生理学多配体蛋白聚糖类动物人类

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Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第29期274卷 20444-20449页

作者： Aspberg, A Adam, S Kostka, G Timpl, R Heinegård, D Univ Lund Dept Cell & Mol Biol Sect Connect Tissue Biol SE-22100 Lund Sweden Max Planck Inst Biochem D-82152 Martinsried Germany

The aggregating proteoglycans (aggrecan, versican, neurocan, and brevican) are important components of many extracellular matrices. Their N-terminal globular domain binds to hyaluronan, but the function of their C-terminal region containing a C-type lectin domain is less clear. We now report that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican. Amino acid sequencing of tryptic peptides from this protein identified it as fibulin-1. This extracellular matrix glycoprotein is strongly expressed in tissues where versican is expressed (blood vessels, skin, and developing heart), and also expressed in developing cartilage and bone. It is thus likely to interact with these proteoglycans in vivo. Surface plasmon resonance measurements confirmed that aggrecan and versican lectin domains bind fibulin-1, whereas brevican and neurocan do not. As expected for a C-type lectin, the interactions with fibulin-1 are Ca2+-dependent, with K-D values in the low nanomolar range. Using various deletion mutants, the binding site for aggrecan and versican lectin domains was mapped to the epidermal growth factor-like repeats in domain II of fibulin-1. No difference in affinity was found for deglycosylated fibulin-1, indicating that the proteoglycan C-type lectin domains bind to the protein part of fibulin-1.

关键词：软骨蛋白聚糖类氨基酸序列钙/代谢钙结合蛋白质类/分离和提纯钙结合蛋白质类/代谢硫酸软骨素蛋白聚糖类/化学硫酸软骨素蛋白聚糖类/代谢表皮生长因子/化学表皮生长因子/代谢细胞外基质蛋白质类/代谢糖基化免疫组织化学外源凝集素类/代谢外源凝集素类 C型配体蛋白质结合蛋白聚糖类/化学蛋白聚糖类/代谢重组蛋白质类/化学重组蛋白质类/分离和提纯重组蛋白质类/代谢序列同源性氨基酸多功能蛋白聚糖类动物人类

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Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第14期274卷 9636-9647页

作者： Svensson, L Aszódi, A Reinholt, FP Fässler, R Heinegård, D Oldberg, Å Univ Lund Dept Cell & Mol Biol S-22100 Lund Sweden Univ Lund Hosp Dept Expt Pathol S-22185 Lund Sweden Natl Hosp Norway Dept Pathol Lab Electron Microscopy N-0027 Oslo Norway

Fibromodulin is a member of a family of connective tissue glycoproteins/proteoglycans containing leucine-rich repeat motifs. Several members of this gene family bind to fibrillar collagens and are believed to function in the assembly of the collagen network in connective tissues. Here we show that mice lacking a functional fibromodulin gene exhibit an altered morphological phenotype in tail tendon with fewer and abnormal collagen fiber bundles. In fibromodulin-null animals virtually all collagen fiber bundles are disorganized and have an abnormal morphology. Also 10-20% of the bundles in heterozygous mice are similar to the abnormal bundles in fibromodulin-null tail tendon. Ultrastructural analysis of Achilles tendon from fibromodulin-null mice show collagen fibrils with irregular and rough outlines in cross-section. Morphometric analysis show that fibromodulin-null mice have on the average thinner fibrils than wild type animals as a result of a larger preponderance of very thin fibrils in an overall similar range of fibril diameters. Protein and RNA analyses show an approximately 4-fold increase in the content of lumican in fibromodulin-null as compared with wild type tail tendon, despite a decrease in lumican mRNA These results demonstrate a role for fibromodulin in collagen fibrillogenesis and suggest that the orchestrated action of several leucine-rich repeat glycoproteins/proteoglycans influence the architecture of collagen matrices.

关键词：载体蛋白质类/遗传学载体蛋白质类/生理学细胞系硫酸软骨素蛋白聚糖类/代谢胶原结缔组织/畸形细胞外基质蛋白质类免疫组织化学原位杂交硫酸角质素/代谢小鼠基因敲除显微镜检查电子蛋白聚糖类 RNA 信使/代谢腱/畸形腱/代谢动物小鼠

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The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第16期274卷 11431-11438页

作者： Miura, R Aspberg, A Ethell, IM Hagihara, K Schnaar, RL Ruoslahti, E Yamaguchi, Y Burnham Inst La Jolla CA 92037 USA Johns Hopkins Univ Sch Med Dept Pharmacol & Neurosci Baltimore MD 21205 USA

The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W, B., and Yamaguchi, Y. (1997) J. Neurosci, 17, 7784-7795), In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides, Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo.

关键词：结合部位短蛋白聚糖细胞黏附硫酸软骨素蛋白聚糖类/化学硫酸软骨素蛋白聚糖类/代谢糖脂类/代谢外源凝集素类/化学外源凝集素类/代谢外源凝集素类 C型膜脂质类/代谢神经组织蛋白质类/化学神经组织蛋白质类/代谢蛋白质结合腱糖蛋白/代谢动物牛

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Integrin and neurocan binding to L1 involves distinct Ig domains

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第35期274卷 24602-24610页

作者： Oleszewski, M Beer, S Katich, S Geiger, C Zeller, Y Rauch, U Altevogt, P German Canc Res Ctr Tumor Immunol Programme D-69120 Heidelberg Germany Univ Lund Hosp Dept Expt Pathol S-22185 Lund Sweden

The cell adhesion molecule L1, a 200-220-kDa type I membrane glycoprotein of the Ig superfamily, mediates many neuronal processes. Originally studied in the nervous system, L1 is expressed by hematopoietic and many epithelial cells, suggesting a more expanded role, L1 supports homophilic L1-L1 and integrin-mediated cell binding and can also bind with high affinity to the neural proteoglycan neurocan;however, the binding site is unknown. We have dissected the L1 molecule and investigated the cell binding ability of Ig domains 1 and 6. We report that RGD sites in domain 6 support alpha 5 beta 1- or alpha v beta 3-mediated integrin binding and that both RGD sites are essential. Cooperation of RGD sites with neighboring domains are necessary for alpha(5)beta(1). A T cell hybridoma and activated T cells could bind to L1 in the absence of RGDs. This binding was supported by Ig domain 1 and mediated by cell surface-exposed neurocan. Lymphoid and brain-derived neurocan were structurally similar. We also present evidence that a fusion protein of the Ig 1-like domain of L1 can bind to recombinant neurocan. Our results support the notion that L1 provides distinct cell binding sites that may serve in cell-cell or cell-matrix interactions.

关键词：结合部位阳离子/代谢硫酸软骨素蛋白聚糖类/代谢荧光抗体技术糖苷水解酶类/药理学肝素/药理学杂交瘤/代谢免疫球蛋白类/化学整合素类/代谢外源凝集素类 C型白细胞L1抗原复合物膜糖蛋白类/遗传学膜糖蛋白类/代谢诱变定点神经组织蛋白质类/代谢神经细胞黏附分子类/遗传学神经细胞黏附分子类/代谢寡肽类/化学寡肽类/遗传学蛋白质结合重组蛋白质类/代谢 T淋巴细胞/代谢动物小鼠

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Lipoprotein lipase enhances the binding of native and oxidized low density lipoproteins to versican and biglycan synthesized by cultured arterial smooth muscle cells

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第49期274卷 34629-34636页

作者： Olin, KL Potter-Perigo, S Barrett, PHR Wight, TN Chait, A Univ Washington Dept Med Seattle WA 98195 USA Univ Washington Dept Pathol Seattle WA 98195 USA Univ Western Australia Dept Med Perth WA 6001 Australia

Retention of low density lipoproteins (LDL) by vascular proteoglycans and their subsequent oxidation are important in atherogenesis, Lipoprotein lipase (LPL) can bind LDL and proteoglycans, although the effect of different proteoglycans to influence the ability of LPL to act as a bridge in the formation of LDL-proteoglycan complexes is unknown. Using an electrophoretic gel mobility shift assay, [S-35]SO4-labeled versican and biglycan, two extracellular proteoglycans secreted by vascular cells, bound native LDL in a saturable fashion, The addition of bovine milk LPL dose-dependently increased the binding of native LDL to both versican and biglycan, approaching saturation at 30-40 mu g/ml LPL for versican and 20 mu g/ml LPL for biglycan. LDL was oxidized by several methods, including copper, 2,2-azobis(2-amidinopropane)-2HCl and hypochlorite, Extensively copper- and hypochlorite-oxidized LDL bound poorly to versican and biglycan, Proteoglycan binding to LDL was correlated inversely with the extent of LDL;however, the addition of LPL to oxidized LDL together with biglycan or versican allowed the oxidized LDL to bind the proteoglycans in an LPL dose-dependent manner. Addition of LPL had a greater relative effect on the binding of extensively oxidized LDL to proteoglycans compared with native LDL, LPL had a slightly greater effect on increasing the binding of native and oxidized LDL to biglycan than versican, Thus, LPL in the artery wall might increase the atherogenicity of oxidized LDL, since it enables its binding to vascular biglycan and versican.

关键词：动脉/代谢双糖链蛋白多糖细胞培养的硫酸软骨素蛋白聚糖类/代谢剂量效应关系药物细胞外基质蛋白质类动力学外源凝集素类 C型脂蛋白脂酶/药理学脂蛋白类 LDL/代谢乳蛋白质类/代谢肌平滑血管/代谢氧化还原蛋白质结合/药物作用蛋白聚糖类/代谢多功能蛋白聚糖类动物牛人类

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