Dysregulation of laminins in intestinal inflammation

Spenlé, Caroline; Hussenet, Thomas; Joël, Lacroute; Lefèbvre, Olivier; Kédinger, Michèle; Orend, Gertraud; Simon‐Assmann, Patricia

doi:10.1016/j.patbio.2011.10.005

Cited by 20 publications

(14 citation statements)

References 79 publications

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“…Alterations in islet ECM integrity may precede the initiation of inflammation as it has been described in other inflammatory conditions (40,52). Intravital imaging studies in a mouse diabetes model showed that β-cell killing was preceded by cytotoxic T-cell trapping within the vicinity of the β-cells at sites of capillary leakage (53).…”

Section: Discussionmentioning

confidence: 79%

Hyaluronan and Hyaluronan-Binding Proteins Accumulate in Both Human Type 1 Diabetic Islets and Lymphoid Tissues and Associate With Inflammatory Cells in Insulitis

et al. 2014

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Hyaluronan (HA) is an extracellular matrix glycosaminoglycan that is present in pancreatic islets, but little is known about its involvement in the development of human type 1 diabetes (T1D). We have evaluated whether pancreatic islets and lymphoid tissues of T1D and nondiabetic organ donors differ in the amount and distribution of HA and HA-binding proteins (hyaladherins), such as inter-α-inhibitor (IαI), versican, and tumor necrosis factor–stimulated gene-6 (TSG-6). HA was dramatically increased both within the islet and outside the islet endocrine cells, juxtaposed to islet microvessels in T1D. In addition, HA was prominent surrounding immune cells in areas of insulitis. IαI and versican were present in HA-rich areas of islets, and both molecules accumulated in diabetic islets and regions exhibiting insulitis. TSG-6 was observed within the islet endocrine cells and in inflammatory infiltrates. These patterns were only observed in tissues from younger donors with disease duration of <10 years. Furthermore, HA and IαI amassed in follicular germinal centers and in T-cell areas in lymph nodes and spleens in T1D patients compared with control subjects. Our observations highlight potential roles for HA and hyaladherins in the pathogenesis of diabetes.

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Section: Discussionmentioning

confidence: 79%

Hyaluronan and Hyaluronan-Binding Proteins Accumulate in Both Human Type 1 Diabetic Islets and Lymphoid Tissues and Associate With Inflammatory Cells in Insulitis

et al. 2014

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“…Spenlé et al [43] proposed that the invasion of the intestine by pathogens may require an interaction of pathogens with laminin as an intestinal BM component and that processed laminin α LG4-5 module peptides together with other host-defense peptides might provide protection of intestinal crypts.…”

Section: Discussionmentioning

confidence: 99%

Processing of Laminin α Chains Generates Peptides Involved in Wound Healing and Host Defense

Senyürek¹,

Kempf²,

Klein³

et al. 2014

J Innate Immun

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Laminins play a fundamental role in basement membrane architecture and function in human skin. The C-terminal laminin G domain-like (LG) modules of laminin α chains are modified by proteolysis to generate LG1-3 and secreted LG4-5 tandem modules. In this study, we provide evidence that skin-derived cells process and secrete biologically active peptides from the LG4-5 module of the laminin α3, α4 and α5 chain in vitro and in vivo. We show enhanced expression and processing of the LG4-5 module of laminin α3 in keratinocytes after infection and in chronic wounds in which the level of expression and further processing of the LG4-5 module correlated with the speed of wound healing. Furthermore, bacterial or host-derived proteases promote processing of laminin α3 LG4-5. On a functional level, we show that LG4-5-derived peptides play a role in wound healing. Moreover, we demonstrate that LG4-derived peptides from the α3, α4 and α5 chains have broad antimicrobial activity and possess strong chemotactic activity to mononuclear cells. Thus, the data strongly suggest a novel multifunctional role for laminin LG4-5-derived peptides in human skin and its involvement in physiological processes and pathological conditions such as inflammation, chronic wounds and skin infection.

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“…[33][34][35] In addition to their role in stable adhesion, these proteins are also important in cell migration and have consequently been found upregulated during wound healing and tumorigenesis. [35][36][37] The lower LAMC2, ITGA6, and EZR gene expressions in UC-associated dysplasia as described in cohort 1 have, to our knowledge, not been described previously.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional Analysis of Left-sided Colitis, Pancolitis, and Ulcerative Colitis-associated Dysplasia

Bjerrum

Nielsen

Riis

et al. 2014

Inflammatory Bowel Diseases

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Dysregulation of laminins in intestinal inflammation

Cited by 20 publications

References 79 publications

Hyaluronan and Hyaluronan-Binding Proteins Accumulate in Both Human Type 1 Diabetic Islets and Lymphoid Tissues and Associate With Inflammatory Cells in Insulitis

Hyaluronan and Hyaluronan-Binding Proteins Accumulate in Both Human Type 1 Diabetic Islets and Lymphoid Tissues and Associate With Inflammatory Cells in Insulitis

Processing of Laminin α Chains Generates Peptides Involved in Wound Healing and Host Defense

Transcriptional Analysis of Left-sided Colitis, Pancolitis, and Ulcerative Colitis-associated Dysplasia

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