Distribution of Laminin Variants and Their Integrin Receptors in Human Secondary Lymphoid Tissue: Colocalization suggests that the α6β4-integrin is a receptor for laminin-5 in lymphoid follicles

Jaspars, L. H.; Melker, Annemieke A. de; Bonnet, Petra; Sonnenberg, Arnoud; Meijer, C. J. L. M.

doi:10.3109/15419069609010771

Cited by 15 publications

(10 citation statements)

References 34 publications

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“…Among the lymphoid vessels, selective staining of the capillaries in the lymphoid follicles by antibodies to ␤3 and ␥2 Lm chains indicated the presence of Lm-332 in this vasculature but not in HEVs. Others [35] have reported similar results. Expression of Lm␣5 by LN blood vessels, including HEV, has been described in mice [47], and broad staining of human LN vasculature, without specifying HEVs, with antibodies to Lm␣3, -␣4, and -␣5 chains has been reported recently [12].…”

Section: Discussionsupporting

confidence: 76%

Laminin isoforms of lymph nodes and predominant role of α5-laminin(s) in adhesion and migration of blood lymphocytes

Gorfu

Virtanen

Hukkanen

et al. 2008

Journal of Leukocyte Biology

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During extravasation and within lymph nodes (LNs), blood lymphocytes interact with laminins (Lms), major components of vascular basement membranes (BMs) and of reticular fibers (RFs), a fibrillar extracellular matrix. However, the identity and role of these laminin isoform(s) are poorly known. By using confocal microscopy examination of human LNs, we show that BMs of high endothelial venules (HEVs) express laminin alpha3, alpha4, alpha5, beta1, beta2, and gamma1 chains and that the same chains, in addition to alpha2, are found in RFs. In functional studies with laminin isoforms covering all Lm alpha chains, alpha5-laminin (Lm-511) was the most adhesion- and migration-promoting isoform for human blood lymphocytes, followed by alpha3- (Lm-332) and alpha4- (Lm-411) laminins, and the lymphocytes used the alpha6beta1 integrin as the primary receptor for the alpha5-laminin. Moreover, Lm-511 strongly co-stimulated T cell proliferation, and blood lymphocytes were able to secrete alpha4- and alpha5-laminins following stimulation. The LN cell number in laminin alpha4-deficient mice compared with wild-type did not differ significantly. This study demonstrates a predominant role for alpha5-laminin(s) in blood lymphocyte biology and identifies LN laminins and their integrin receptors in blood lymphocytes.

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Section: Discussionsupporting

confidence: 76%

Laminin isoforms of lymph nodes and predominant role of α5-laminin(s) in adhesion and migration of blood lymphocytes

Gorfu

Virtanen

Hukkanen

et al. 2008

Journal of Leukocyte Biology

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“…Ln ␣1-chain has been shown to be restricted mainly to the subepithelial glandular BMs and to be absent from the endothelial BMs (Virtanen et al 2000;Määttä et al 2001). However, it has been previously reported in capillaries of the human thymus and follicular capillaries of the lymph node and tonsil (Jaspars et al 1996). Ln 5 is a wellknown component of BMs of squamous epithelia, in which it forms a part of the hemidesmosomal complex and usually has been immunolocalized to the epithelium (Marinkovich et al 1992;Rousselle et al 1997).…”

Section: Discussionmentioning

confidence: 99%

Differential Expression of Basement Membrane Components in Lymphatic Tissues

Määttä¹,

Liakka²,

Salo

et al. 2004

J Histochem Cytochem.

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Peripheral lymphoid tissues act as important organs of immunological defense. Characteristic of their architecture is the rich reticular fiber meshwork composed of various extracellular matrix (ECM) molecules with which the stationary non-lymphatic cells stay in intimate contact and form channels through which the lymphatic cells travel. Here we studied the distribution of various laminin (Ln) chains and different types of collagens in human spleen, lymph node, and tonsil to clarify their chain-specific distribution. The most widely distributed proteins in all these organs were Ln chains alpha5, beta1, gamma1 and collagen types IV and XVIII, which were present in practically all compartments. Conversely, Ln alpha1, alpha2, alpha4, and type VII collagen showed a more restricted expression pattern. A unique feature was that Ln alpha3-, beta3-, and gamma2-chains, which normally are not localized to the vascular wall in non-lymphatic tissues, were present also in capillary basement membranes (BMs) of the follicular structures of lymph node and tonsil and in Ln alpha1-chain and type VII collagen also in the splenic white pulp. We also found that collagen XVII was exclusively present in the ring fibers of the spleen. The results indicate that BMs of lymphatic tissues contain a variety of macromolecules that probably contribute strongly to immunological events. In addition, capillaries of the lymphoid tissue exhibit a specified BM composition resembling that in epithelial BMs of non-lymphoid tissues.

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“…The 4C7 antibody, commercially available under different names, has been much used to study the distribution of laminin ␣1 chain in human, hamster, rat, and guinea pig tissues. The 4C7 antibody described by Engvall et al (15) should not be confused with a more recent, well described laminin antibody recognizing laminin-5 (␣3␤3␥2) also named 4C7 (51). A data base search revealed numerous publications that have used the first described 4C7 antibody to demonstrate a broad tissue distribution of the antigen.…”

Section: Qatgdymgvslrmentioning

confidence: 99%

Presence of Laminin α5 Chain and Lack of Laminin α1 Chain during Human Muscle Development and in Muscular Dystrophies

Tiger

Champliaud

Pedrosa-Domellöf

et al. 1997

Journal of Biological Chemistry

190

153

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There is currently a great interest in identifying laminin isoforms expressed in developing and regenerating skeletal muscle. Laminin ␣1 has been reported to localize to human fetal muscle and to be induced in muscular dystrophies based on immunohistochemistry with the monoclonal antibody 4C7, suggested to recognize the human laminin ␣1 chain. Nevertheless, there seems to be no expression of laminin ␣1 protein or mRNA in developing or dystrophic mouse skeletal muscle fibers. To address the discrepancy between the results obtained in developing and dystrophic human and mouse muscle we expressed the E3 domain of human laminin ␣1 chain as a recombinant protein and made antibodies specific for human laminin ␣1 chain (anti-hLN-␣1G4/G5). We also made antibodies to the human laminin ␣5 chain purified from placenta. In the present report we show that hLN-␣1G4/G5 antibodies react with a 400-kDa laminin ␣1 chain and that 4C7 reacts with a 380-kDa laminin ␣5 chain. Immunohistochemistry with the hLN-␣1G4/G5 antibody and 4C7 revealed that the two antibodies stained human kidney, developing and dystrophic muscle in distinct patterns. Our data indicate that the previously reported expression patterns in developing, adult, and dystrophic human muscle tissues with 4C7 should be re-interpreted as an expression of laminin ␣5 chain. Our data are also consistent with earlier work in mouse, indicating that laminin ␣1 is largely an epithelial laminin chain not present in developing or dystrophic muscle fibers.

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Distribution of Laminin Variants and Their Integrin Receptors in Human Secondary Lymphoid Tissue: Colocalization suggests that the α6β4-integrin is a receptor for laminin-5 in lymphoid follicles

Cited by 15 publications

References 34 publications

Laminin isoforms of lymph nodes and predominant role of α5-laminin(s) in adhesion and migration of blood lymphocytes

Laminin isoforms of lymph nodes and predominant role of α5-laminin(s) in adhesion and migration of blood lymphocytes

Differential Expression of Basement Membrane Components in Lymphatic Tissues

Presence of Laminin α5 Chain and Lack of Laminin α1 Chain during Human Muscle Development and in Muscular Dystrophies

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