Differential Expression of Basement Membrane Components in Lymphatic Tissues

Määttä, Marko; Liakka, Annikki; Salo, Sirpa; Tasanen, Kaisa; Bruckner‐Tuderman, Leena; Autio–Harmainen, Helena

doi:10.1369/jhc.4a6253.2004

Cited by 22 publications

(7 citation statements)

References 34 publications

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“…Therefore, we studied whether the ␣ 3 ␤ 1 -integrin is functional in our cells. Ln-5 is one of the high-affinity ligands for integrin ␣ 3 ␤ 1 (59), and some studies have proposed that this laminin is located to BMs of some capillaries (32,63), suggesting that human microvascular endothelial cells could interact with Ln-5 via this receptor. The results show that the adhesion of HDME Fig.…”

Section: Discussionmentioning

confidence: 99%

Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells

Vainionpää

Kikkawa²,

Lounatmaa³

et al. 2006

American Journal of Physiology-Cell Physiology

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Laminin alpha5-chain, a constituent of laminins-10 and -11, is expressed in endothelial basement membranes. In this study we evaluated the roles of alpha5 laminins and Lutheran blood group glycoproteins (Lu), recently identified receptors of the laminin alpha5-chain, in the adhesion of human dermal microvascular and pulmonary artery endothelial cells. Field emission scanning electron microscopy and immunohistochemistry showed that the endothelial cells spread on laminin-10 and formed fibronectin-positive fibrillar adhesion structures. Immunoprecipitation results suggested that the cells produced fibronectin, which they could use as adhesion substratum, during the adhesion process. When the protein synthesis during the adhesion was inhibited with cycloheximide, the formation of fibrillar adhesions on laminin-10 was abolished, suggesting that laminin-10 does not stimulate the formation of any adhesion structures. Northern and Western blot analyses showed that the cells expressed M(r) 78,000 and 85,000 isoforms of Lu. Quantitative cell adhesion assays showed that in the endothelial cell adhesion to laminin-10, Lu acted in concert with integrins beta(1) and alpha(v)beta(3), whereas in the adhesion to laminin-10/11, Lu and integrin beta(1) were involved. In the cells adhering to the alpha5 laminins, Lu and the integrins showed uniform cell surface distribution. These findings indicate that alpha5 laminins stimulate endothelial cell adhesion but not the formation of fibrillar or focal adhesions. Lu mediates the adhesion of human endothelial cells to alpha5 laminins in collaboration with integrins beta(1) and alpha(v)beta(3).

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Section: Discussionmentioning

confidence: 99%

Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells

Vainionpää

Kikkawa²,

Lounatmaa³

et al. 2006

American Journal of Physiology-Cell Physiology

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“…Precollectors merge into larger collecting vessels, made up of a series of subunits called “lymphangions” (the section between 2 intraluminal valves) . The collecting vessel wall is organized into a layer of continuously adherent LECs (intima), a basement membrane comprising laminin and type IV collagen, and circumferential smooth muscle (media) . Lymphangions act individually and in groups, forming contractile units that propel lymph via intraluminal valves made of connective tissue covered with LECs …”

Section: Lymphatic Structure and Functionmentioning

confidence: 99%

Comparative pathophysiology and management of protein‐losing enteropathy

Craven

Washabau

2019

Veterinary Internal Medicne

116

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Protein‐losing enteropathy, or PLE, is not a disease but a syndrome that develops in numerous disease states of differing etiologies and often involving the lymphatic system, such as lymphangiectasia and lymphangitis in dogs. The pathophysiology of lymphatic disease is incompletely understood, and the disease is challenging to manage. Understanding of PLE mechanisms requires knowledge of lymphatic system structure and function, which are reviewed here. The mechanisms of enteric protein loss in PLE are identical in dogs and people, irrespective of the underlying cause. In people, PLE is usually associated with primary intestinal lymphangiectasia, suspected to arise from genetic susceptibility, or “idiopathic” lymphatic vascular obstruction. In dogs, PLE is most often a feature of inflammatory bowel disease (IBD), and less frequently intestinal lymphangiectasia, although it is not proven which process is the true driving defect. In cats, PLE is relatively rare. Review of the veterinary literature (1977‐2018) reveals that PLE was life‐ending in 54.2% of dogs compared to published disease‐associated deaths in IBD of <20%, implying that PLE is not merely a continuum of IBD spectrum pathophysiology. In people, diet is the cornerstone of management, whereas dogs are often treated with immunosuppression for causes of PLE including lymphangiectasia, lymphangitis, and crypt disease. Currently, however, there is no scientific, extrapolated, or evidence‐based support for an autoimmune or immune‐mediated mechanism. Moreover, people with PLE have disease‐associated loss of immune function, including lymphopenia, severe CD4+ T‐cell depletion, and negative vaccinal titers. Comparison of PLE in people and dogs is undertaken here, and theories in treatment of PLE are presented.

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“…To our knowledge, this is the first report of the characterization of ECM components in swine tonsils. Collagen types I, II, III, IV, VII, and XVIII have been found in human tonsils, as have fibronectin, laminin, vitronectin, tenascin, and thrombospondin (7,8). Maatta et al (7) also detected collagen type XVII in the crypt epithelium of human palatine tonsils, but this type of collagen was not identified in the current study; thrombospondin also was not detected.…”

Section: Discussionmentioning

confidence: 99%

“…The epithelium of the crypts overlays a basement membrane (sometimes fragmented), which in turn is supported by an interstitial extracellular matrix (ECM) of various thickness, depending on the location in the tonsil (3). Despite studies of the ultrastructure and fine structure of the tonsils of swine (1,3) and studies into the ECM components and host cell receptors present in tonsils of other species (6)(7)(8), little has been done to characterize these components in the tonsils of the soft palate of swine.…”

mentioning

confidence: 99%

Attachment of Actinobacillus suis H91-0380 and Its Isogenic Adhesin Mutants to Extracellular Matrix Components of the Tonsils of the Soft Palate of Swine

Bujold

MacInnes

2016

Infect Immun

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Tonsils conduct immune surveillance of antigens entering the upper respiratory tract. Despite their immunological function, they are also sites of persistence and invasion of bacterial pathogens. Actinobacillus suis is a common resident of the tonsils of the soft palate in pigs, but under certain circumstances it can invade, causing septicemia and related sequelae. Twenty-four putative adhesins are predicted in the A. suis genome, but to date, little is known about how they might participate in colonization or invasion. To better understand these processes, swine tonsil lysates were characterized by mass spectrometry. Fifty-nine extracellular matrix (ECM) proteins were identified, including small leucine-rich proteoglycans, integrins, and other cell surface receptors. Additionally, attachment of the wild type and 3 adhesin mutants to 5 ECM components was evaluated. Exponential cultures of wild-type A. suis adhered significantly more than stationary cultures to all ECM components studied except collagen I. During exponential growth, the A. suis ⌬flp1 mutant attached less to collagen IV while the ⌬ompA mutant attached less to all ECMs. The ⌬comE1 strain attached less to collagen IV, fibronectin, and vitronectin during exponential growth and exhibited differential attachment to collagen I over short adherence time points. These results suggest that Flp1, OmpA, and ComE1 are important during early stages of attachment to ECM components found in tonsils, which supports the notion that other adhesins have compensatory effects during later stages of attachment.T onsils are secondary lymphoid organs that are an important part of the host immune response against antigens entering the body through the mouth and nose. Pigs have 5 sets of tonsils located around the oropharyngeal cavity in the so-called Waldeyer's ring, the largest being the tonsils of the soft palate (1), which are thought to be functionally equivalent to the palatine tonsils in humans (2). The tonsils of the soft palate of swine have as many as 200 branching crypts that end blindly within the lymphoid tissue beneath (3). The lumina of the crypts are covered by a layer of nonkeratinized squamous epithelium that is continuous with the epithelium of the oral cavity, while lymphoepithelium lines the deeper areas of the crypts (4). Lymphoepithelium has a thinner epithelial lining interspersed with goblet cells and M cells, the latter of which can be used by some pathogens to invade the tonsil (3, 5). The lymphoepithelium also allows passage of lymphocytes, plasma cells, and macrophages (2). The epithelium of the crypts overlays a basement membrane (sometimes fragmented), which in turn is supported by an interstitial extracellular matrix (ECM) of various thickness, depending on the location in the tonsil (3). Despite studies of the ultrastructure and fine structure of the tonsils of swine (1, 3) and studies into the ECM components and host cell receptors present in tonsils of other species (6-8), little has been done to characterize these components in the tonsi...

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Differential Expression of Basement Membrane Components in Lymphatic Tissues

Cited by 22 publications

References 34 publications

Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells

Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells

Comparative pathophysiology and management of protein‐losing enteropathy

Attachment of Actinobacillus suis H91-0380 and Its Isogenic Adhesin Mutants to Extracellular Matrix Components of the Tonsils of the Soft Palate of Swine

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