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Comparison of Two Diagnostic Assays for Anti-Laminin 332 Mucous Membrane Pemphigoid

Frontiers in Immunology, 2021
Anti-laminin 332 mucous membrane pemphigoid (MMP) is an autoimmune blistering disease characterized by predominant mucosal lesions and autoantibodies against laminin 332.
Stephanie Goletz, Federica Giurdanella, Maike M. Holtsche, Miranda Nijenhuis, Barbara Horvath, Gilles F. H. Diercks, Detlef Zillikens, Takashi Hashimoto, Enno Schmidt, Enno Schmidt, Hendri H. Pas   +10 more
doaj   +1 more source

Keratinocyte-targeted expression of human laminin γ2 rescues skin blistering and early lethality of laminin γ2 deficient mice. [PDF]

PLoS ONE, 2012
Laminin-332 is a heterotrimeric basement membrane component comprised of the α3, ß3, and γ2 laminin chains. Laminin-332 modulates epithelial cell processes, such as adhesion, migration, and differentiation and is prominent in many embryonic and adult ...
Tracy L Adair-Kirk, Gail L Griffin, Michelle J Meyer, Diane G Kelley, Jeffrey H Miner, Douglas R Keene, M Peter Marinkovich, J Michael Ruppert, Jouni Uitto, Robert M Senior   +9 more
doaj   +1 more source

Subunit-Specific Reactivity of Autoantibodies Against Laminin-332 Reveals Direct Inflammatory Mechanisms on Keratinocytes

Frontiers in Immunology, 2021
Laminin-332 pemphigoid is a rare and severe autoimmune blistering disease, caused by IgG autoantibodies targeting laminin-332 in the dermal-epidermal basement zone.
Lei Bao, Jing Li, Farzan Solimani, Farzan Solimani, Dario Didona, Payal M. Patel, Xiaoguang Li, Hua Qian, Norito Ishii, Takashi Hashimoto, Takashi Hashimoto, Michael Hertl, Kyle T. Amber, Kyle T. Amber   +13 more
doaj   +1 more source

Laminin and Integrin in LAMA2-Related Congenital Muscular Dystrophy: From Disease to Therapeutics

Frontiers in Molecular Neuroscience, 2020
Laminin-α2-related congenital muscular dystrophy (LAMA2-CMD) is a devastating neuromuscular disease caused by mutations in the LAMA2 gene. These mutations result in the complete absence or truncated expression of the laminin-α2 chain.
Pamela Barraza-Flores, Christina R. Bates, Ariany Oliveira-Santos, Dean J. Burkin   +3 more
doaj   +1 more source

Distinct roles for laminin globular domains in laminin alpha1 chain mediated rescue of murine laminin alpha2 chain deficiency. [PDF]

PLoS ONE, 2010
BACKGROUND: Laminin alpha2 chain mutations cause congenital muscular dystrophy with dysmyelination neuropathy (MDC1A). Previously, we demonstrated that laminin alpha1 chain ameliorates the disease in mice.
Kinga I Gawlik, Mikael Akerlund, Virginie Carmignac, Harri Elamaa, Madeleine Durbeej   +4 more
doaj   +1 more source

Laminin‐221 Enhances Therapeutic Effects of Human‐Induced Pluripotent Stem Cell–Derived 3‐Dimensional Engineered Cardiac Tissue Transplantation in a Rat Ischemic Cardiomyopathy Model

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2020
Background Extracellular matrix, especially laminin‐221, may play crucial roles in viability and survival of human‐induced pluripotent stem cell‐derived cardiomyocytes (hiPS‐CMs) after in vivo transplant.
Takaaki Samura, Shigeru Miyagawa, Takuji Kawamura, Satsuki Fukushima, Jun‐ya Yokoyama, Maki Takeda, Akima Harada, Fumiya Ohashi, Ryoko Sato‐Nishiuchi, Toshihiko Toyofuku, Koichi Toda, Kiyotoshi Sekiguchi, Yoshiki Sawa   +12 more
doaj   +1 more source

Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes. [PDF]

PLoS ONE, 2014
We describe the detailed structural investigation of nidogen-1/laminin γ1 complexes using full-length nidogen-1 and a number of laminin γ1 variants. The interactions of nidogen-1 with laminin variants γ1 LEb2-4, γ1 LEb2-4 N836D, γ1 short arm, and γ1 ...
Philip Lössl, Knut Kölbel, Dirk Tänzler, David Nannemann, Christian H Ihling, Manuel V Keller, Marian Schneider, Frank Zaucke, Jens Meiler, Andrea Sinz   +9 more
doaj   +1 more source

Laminin-bound integrin α6β4 promotes non-small cell lung cancer progression via the activation of YAP/TAZ signaling pathway

Frontiers in Oncology, 2022
Laminin is an extracellular matrix multidomain trimeric glycoprotein, that has a potential role in tumor progression. Here, we studied the effects of non-small cell lung cancer (NSCLC) cells interaction on laminin and explored the underlying mechanism of
Xiaopeng Zhao, Chuang Liu, Xu He, Miao Wang, Haoran Zhang, Jingge Cheng, Hongyan Wang   +6 more
doaj   +1 more source

Autoimmunity against laminin 332

Frontiers in Immunology, 2023
Laminin 332 is a heterotrimeric structural protein of the basal membrane zone (BMZ) of the skin and adjacent mucosal tissues. The importance of laminin 332 for the structural integrity of the BMZ is demonstrated by mutations in any of the three genes ...
Sabrina Patzelt, Enno Schmidt, Enno Schmidt   +2 more
doaj   +1 more source

Agrin binds to the nerve-muscle basal lamina via laminin [PDF]

, 1997
Agrin is a heparan sulfate proteoglycan that is required for the formation and maintenance of neuromuscular junctions. During development, agrin is secreted from motor neurons to trigger the local aggregation of acetylcholine receptors (AChRs) and other ...
Altschul, Bowe, Bowe, Bowen, Brancaccio, Brandenberger, Brandenberger, Brubacher, Burden, Burgeson, Campagna, Campanelli, Campbell, Chiu, Cohen, Cohen, Denzer, Denzer, Ferns, Fox, Gautam, Gee, Gesemann, Gesemann, Gluzman, Godfrey, Godfrey, Godfrey, Godfrey, Graham, Hagen, Halfter, Hall, Hunter, Kleinman, Lennon, Lowry, Magill-Solc, Martin, Martin, McMahan, McMahan, Morrissey, Nitkin, Nitkin, Noakes, Ott, Paulsson, Pearson, Perris, Reist, Ries, Ruegg, Ruegg, Ruegg, Rupp, Sanes, Sanes, Sanes, Schuler, Smith, Sugiyama, Timpl, Timpl, Timpl, Tsen, Tsen, Tsim, Wallace, Wallace, Weber, Worton, Yurchenco, Yurchenco   +73 more
core   +3 more sources