Junctional Adhesion Molecules (JAMs) are Differentially Expressed in Fibroblasts and Co-Localize with ZO-1 to Adherens-Like Junctions

Morris, Andrew P.; Tawil, Ahmad; Berkova, Zuzana; Wible, Linda; Smith, C. Wayne; Cunningham, Sonia

doi:10.1080/15419060600877978

Cited by 56 publications

(48 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…30 However, it has been suggested that during leukocyte transendothelial migration, such homophilic interaction of JAM-A may be replaced with heterophilic trans-interactions involving leukocyte integrin counterreceptors. 22,24 In line with this, the integrin LFA-1 (␣ L ␤ 2 , CD11c/CD18) has been identified as a ligand for JAM-A, an interaction that reportedly mediates leukocyte transmigration through cultured endothelial cells and also contributes to their Lymphocyte subsets 27 Maintenance of tight junctions 27,30 Leukocyte transmigration 27,28 Assembly and remodelling of tight junctions Maintenance of endothelial tight junctions 62 Regulation of neutrophil, monocyte and lymphocyte accumulation at sites of inflammation 40,43 Maintenance of adheren-like junctions 100 Neutrophil transepithelial migration 52 Unknown -JAML Neutrophils 21 Transepithelial migration 54 adhesion under conditions where JAM-A is mobilized to the luminal surface of the endothelium. 31 Although more recent studies have confirmed that during leukocyte transmigration JAM-A and intercellular adhesion molecule-1 (ICAM-1) can redistribute on the endothelial cell surface and colocalize with LFA-1 within ring-like clusters on adherent neutrophils, 32 obtaining additional evidence for a direct JAM-A/LFA-1 interaction has proved elusive.…”

Section: Classical Jam Proteinsmentioning

confidence: 99%

JAM Family and Related Proteins in Leukocyte Migration (Vestweber Series)

Bradfield

Nourshargh

Aurrand-Lions

et al. 2007

ATVB

View full text Add to dashboard Cite

Abstract-Exploring the role of junctional adhesion molecules (JAMs) has proven to be varied and controversial. The purpose of this review is to discuss the new and exciting roles of these IgSF molecules and how they have evolved to contribute to diverse functions from development to inflammation. In particular, recent research has focused on JAM subfamily members JAM-A, -B, and -C with newly described roles in leukocyte trafficking during inflammation and angiogenesis. However, research on all JAM family members has demonstrated recurring themes with striking similarities in the many diverse processes they are now known to regulate. (Arterioscler Thromb Vasc Biol. 2007;27:2104-2112.)

show abstract

Section: Classical Jam Proteinsmentioning

confidence: 99%

JAM Family and Related Proteins in Leukocyte Migration (Vestweber Series)

Bradfield

Nourshargh

Aurrand-Lions

et al. 2007

ATVB

View full text Add to dashboard Cite

show abstract

“…[1][2][3][4][5] JAM-B has been previously shown to interact with JAM-C and contributes to leukoendothelial and interendothelial cell-cell adhesion. 6,7 In mice, JAM-B expression is restricted to endothelial cells whereas JAM-C is expressed by various cell types including endothelial, 1,2 fibroblastic, 8 and smooth muscle cells. 9 Moreover, we have recently shown that JAM-C expression in lymph node fibroblastic cells is required for constitutive secretion of several chemokines such as SDF-1␣.…”

Section: Introductionmentioning

confidence: 99%

JAM-B regulates maintenance of hematopoietic stem cells in the bone marrow

Arcangeli

Frontera

Bardin

et al. 2011

Blood

View full text Add to dashboard Cite

IntroductionThe junctional adhesion molecules (JAMs) are a subset of the immunoglobulin (Ig) protein superfamily and are characterized by the presence of both a type V and a type C2 extracellular Ig domain. JAMs and related molecules have been involved in the control of interendothelial junctions and leukocyte transendothelial migration through homotypic and heterotypic interactions. 1-5 JAM-B has been previously shown to interact with JAM-C and contributes to leukoendothelial and interendothelial cell-cell adhesion. 6,7 In mice, JAM-B expression is restricted to endothelial cells whereas JAM-C is expressed by various cell types including endothelial, 1,2 fibroblastic, 8 and smooth muscle cells. 9 Moreover, we have recently shown that JAM-C expression in lymph node fibroblastic cells is required for constitutive secretion of several chemokines such as SDF-1␣. 10 Recently, expression of several JAM family members, such as JAM-A, JAM-C, JAM4, or ESAM, has been reported in hematopoietic stem cells (HSCs), although a function for these proteins in hematopoiesis remains unknown. [11][12][13][14][15][16] In adult mammals, HSCs are rare cells mainly located in the bone marrow (BM) and able to generate all mature blood cells. In mice, HSCs are comprised within the LSK compartment as defined by the Lineage Neg c-kit Hi Sca-1 Hi (LSK) phenotype; the LSK compartment can be further subdivided using additional markers such as CD34, CD150, or CD48. Indeed, CD34 Neg CD135 Neg LSK, or Thy-1 Lo LSK 17,18 and CD150 Pos CD48 Neg LSK cells 19 have been shown to contain, respectively, around 20% and 50% of HSCs with long-term hematopoietic reconstitution potential (LT-HSCs). Because HSCs give rise to mature hematopoietic cells, including immune cells, their replacement must be adjusted to homeostatic or stress conditions such as infections, inflammation, or blood loss, and their expansion must be controlled to avoid exhaustion through inappropriate proliferation and differentiation. This is possible by the coordinated regulation of quiescence, self-renewal, and differentiation of HSCs through appropriate signals delivered by functional microenvironments called niches. [20][21][22] HSCs are restrained in these specialized microenvironments by interactions mediated by adhesion molecules and chemokine receptors expressed by HSCs, such as VLA-4 or CXCR4, with their ligands present within the BM microenvironment. Other signaling pathways controlled by growth factors and their receptors expressed on HSCs, such as angiopoietin-1 and TIE2, SCF and KIT, Thrombopoietin and MPL, have also been involved in HSC maintenance and retention in BM niches. 23,24 Whether the JAM family members expressed on HSCs also contribute to this signaling network has not been addressed so far.When necessary, HSCs enter the cell cycle to maintain BM cellularity and replenish peripheral blood in a process called mobilization, which can be induced using various hematopoietic growth factors, cyclophosphamide in combination with G-CSF (Cy/G-CSF), or intravenous inject...

show abstract

“…In the rodent testis, TJ proteins are found in close spatial association with the basal ectoplasmic specialisation, which is a testis-specific actinbased adherens junction containing the actin-bundling protein espin (Bartles et al 1996, Lee & Cheng 2004, involved in Sertoli-Sertoli and Sertoli-GC adhesion. Claudin and occludin TJ proteins are thought to be classical barrier-forming proteins, while JAM family members have also been associated with cellular adhesion (Morris et al 2006), trans-epithelial cellular migration (Woodfin et al 2007) and cellular polarity (Rehder et al 2006) in other mammalian tissues, with recent evidence suggesting that they may also play a role in spermatogenesis in rodents (Zen et al 2005. JAM family members (JAM-B and JAM-C) have been identified on both Sertoli and GCs in rodents, while claudins and occludin have been localised exclusively to inter-Sertoli cell TJs in this species .…”

Section: Introductionmentioning

confidence: 99%

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Tarulli¹,

Meachem²,

Schlatt³

et al. 2008

Reproduction

View full text Add to dashboard Cite

This study aimed to assess the effect of gonadotrophin suppression and FSH replacement on testicular tight junction dynamics and blood-testis barrier (BTB) organisation in vivo, utilising the seasonal breeding Djungarian hamster. Confocal immunohistology was used to assess the cellular organisation of tight junction proteins and real-time PCR to quantify tight junction mRNA. The effect of tight junction protein organisation on the BTB permeability was also investigated using a biotin-linked tracer. Tight junction protein (claudin-3, junctional adhesion molecule (JAM)-A and occludin) localisation was present but disorganised after gonadotrophin suppression, while mRNA levels (claudin-11, claudin-3 and occludin) were significantly (two-to threefold) increased. By contrast, both protein localisation and mRNA levels for the adaptor protein zona occludens-1 decreased after gonadotrophin suppression. FSH replacement induced a rapid reorganisation of tight junction protein localisation. The functionality of the BTB (as inferred by biotin tracer permeation) was found to be strongly associated with the organisation and localisation of claudin-11. Surprisingly, JAM-A was also recognised on spermatogonia, suggesting an additional novel role for this protein in trans-epithelial migration of germ cells across the BTB. It is concluded that gonadotrophin regulation of tight junction proteins forming the BTB occurs primarily at the level of protein organisation and not gene transcription in this species, and that immunolocalisation of the organised tight junction protein claudin-11 correlates with BTB functionality.

show abstract

Junctional Adhesion Molecules (JAMs) are Differentially Expressed in Fibroblasts and Co-Localize with ZO-1 to Adherens-Like Junctions

Cited by 56 publications

References 52 publications

JAM Family and Related Proteins in Leukocyte Migration (Vestweber Series)

JAM Family and Related Proteins in Leukocyte Migration (Vestweber Series)

JAM-B regulates maintenance of hematopoietic stem cells in the bone marrow

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Contact Info

Product

Resources

About