The inducible blood-brain barrier specific molecule HT7 is a novel immunoglobulin-like cell surface glycoprotein.

Seulberger, Harald; Lottspeich, F.; Risau, Werner

doi:10.1002/j.1460-2075.1990.tb07384.x

Cited by 151 publications

(120 citation statements)

References 47 publications

(56 reference statements)

Supporting

Mentioning

109

Contrasting

Unclassified

Order By: Relevance

“…Exceptional examples are components of the CD3 complex (CD3 d, :, g and z, and CD16) and the Fc:RI complex (Fc:RI a and g), suggesting that a charged residue in the transmembrane domain could be involved in the protein association on the plasma membrane [11,17]. In addition, Seulberger et al noted that three leucines were repeated every seventh amino-acid residue in the Bsg transmembrane domain, which is similar to a motif, named leucine zipper [11]. This motif is implicated in the dimerization of DNA binding proteins, and is also found in a subset of the Ig superfamily, such as CD8, that comprises subunit structures.…”

Section: Discussionmentioning

confidence: 99%

Homo‐oligomer formation by basigin, an immunoglobulin superfamily member, via its N‐terminal immunoglobulin domain

Yoshida¹,

Shibata²,

Yamamoto³

et al. 2000

European Journal of Biochemistry

View full text Add to dashboard Cite

Basigin (Bsg) is a highly glycosylated transmembrane protein with two immunoglobulin (Ig)-like domains. A number of studies, including gene targeting, have demonstrated that Bsg plays pivotal roles in spermatogenesis, implantation, neural network formation and tumor progression. In the present study, to understand the mechanism of action of Bsg, we determined its expression status on the plasma membrane. Cotransfection of Bsg expression vectors with two different tags clarified that Bsg forms homo-oligomers in a cis-dependent manner on the plasma membrane. If the disulfide bond of the more N-terminally located Ig-like domain was destroyed by mutations, Bsg could not form oligomers. In contrast, the mutations of the C-terminal Ig-like domain or N-glycosylation sites did not affect the association. The association of mouse and human Bsgs, which exhibit high homology in the transmembrane and intracellular domains but low homology in the extracellular domain, was very weak as compared with that within the same species, suggesting the importance of the extracellular domain in the association. If the extracellular domain of the human Ret protein was replaced with the N-terminal Ig-like domain of Bsg, the resulting chimera protein was associated with intact wild-type Bsg, but not if the C-terminal Ig-like domain, instead of the N-terminal one, of Bsg was used. No oligomer formation took place between the intact wild-type Ret and Bsg proteins. In conclusion, these data indicate that the N-terminal Ig-like domain is necessary and sufficient for oligomer formation by Bsg on the plasma membrane.Keywords: basigin; EMMPRIN; immunoglobulin superfamily; neurothelin; oligomer.Cell-surface proteins, such as the Ig superfamily, the cadherin superfamily and the integrin superfamily, play important roles in development by regulating cellular differentiation, adhesion and migration [1,2]. Supramolecular structure formation, such as oligomer formation, between these molecules plays crucial roles in exerting their functions. This has been documented by extensive studies of the Ig superfamily. NCAM participates in neural cell adhesion, which is mainly mediated by homophilic binding in a trans-dependent manner through its third Ig-like domain [3,4]. Homodimer formation of ICAM in a cis-dependent manner enhances its binding to a leukocyte b2-integrin [5]. Binding of fibroblast growth factor (FGF) to its receptor (FGFR) leads to dimer formation of FGFR (eventually a complex formation consisting of two FGF, two FGFR and a heparan sulfate chain), which is mediated mainly through homophilic binding at the second Ig-like domain of FGFR [6]. In addition to protein±protein interaction as mentioned above, protein±sugar interaction is also important. P0, a neural adhesion molecule implicated in myelination, harbors an N-glycosylation site, to which the major homophilic binding site is mapped [7]. NCAM and L1, another neural adhesion molecule, associate each other in a cis-dependent manner to reinforce L1 homophilic trans-interaction: in this case...

show abstract

Section: Discussionmentioning

confidence: 99%

Homo‐oligomer formation by basigin, an immunoglobulin superfamily member, via its N‐terminal immunoglobulin domain

Yoshida¹,

Shibata²,

Yamamoto³

et al. 2000

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…This indicates that although the complete functional barrier establishment may not occur until later, morphological changes of endothelial cells in the nervous system may occur as early as E10.5. There are several markers distinguishing endothelial cells at the BBB from other endothelial cells (Dermietzel et al, 1992;Risau, 1991;Risau et al, 1986a;Seulberger et al, 1990). However, none of these markers have been reported to be expressed in endothelial cells of E10.5 brain.…”

Section: Specificity Of the Mdrlul3 Probementioning

confidence: 99%

Mouse multidrug resistance 1a/3 gene is the earliest known endothelial cell differentiation marker during blood‐brain barrier development

Qin

Sato

1995

Developmental Dynamics

View full text Add to dashboard Cite

Molecular mechanisms of endothelial cell differentiation during blood-brain barrier (BBB) development is not well understood due to the lack of specific molecular markers. Here we describe that expression of the mouse multidrug resistance la/3 ( m d r l d 3 ) gene can be detected specifically in subsets of vascular endothelial cells associated with neural tissues at as early as embryonic day 10.5 (E10.5). This onset of mdrl u/3 gene expression coincides with the previously described first appearance of morphologically distinct endothelial cells in neural tissues during BBB development. To our knowledge, the mdrlu/3 gene is the earliest endothelial cell differentiation marker gene during BBB development described thus far. In addition, we have found that neither the level nor pattern of mdrlu/3 gene expression in BBB endothelial cells is affected by aberrant cortical neuronal layers in mutant mouse reeler. o 1995 Wiley-Liss, Inc.

show abstract

“…1,2 Because of its broad distribution, it was expected that basigin plays fundamental roles in various physiologic processes. Molecules identical to basigin were subsequently identified and given different names: M6 3 and EMMPRIN 4 in human; HT7, 5 neurothelin 6 and 5A11 7 in chicken; gp42 8 in mouse; and OX-47 9 and CE9 10 in rat. Of them, EMMPRIN, previously termed TCSF, has been implicated in the induction of MMPs.…”

mentioning

confidence: 99%

Basigin (cd147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts

Kanekura

Chen

Kanzaki

2002

Intl Journal of Cancer

267

210

View full text Add to dashboard Cite

Key words: basigin (CD147); malignant melanoma; invasion; metastasis; matrix metalloproteinaseBasigin (CD147), a transmembrane glycoprotein belonging to the Ig superfamily, was cloned from F9 embryonic carcinoma cells. 1 The Ig domain has strong homology with both the Ig variable domain and the major histocompatibility complex class II ␤ chain. It is expressed in various embryonic and adult tissues. 1,2 Because of its broad distribution, it was expected that basigin plays fundamental roles in various physiologic processes. Molecules identical to basigin were subsequently identified and given different names: M6 3 and EMMPRIN 4 in human; HT7, 5 neurothelin 6 and 5A11 7 in chicken; gp42 8 in mouse; and OX-47 9 and CE9 10 in rat. Of them, EMMPRIN, previously termed TCSF, has been implicated in the induction of MMPs. 4,11 Expression of EMMPRIN is enhanced in a variety of human carcinomas and correlates with tumor progression and invasion by inducing production of MMPs by stromal cells. 4,[11][12][13][14][15][16] It was also shown in vitro that recombinant EMMPRIN purified from Chinese hamster ovary cells transfected with cDNA for human EMMPRIN stimulates cultured human fibroblasts to produce MMP-1, MMP-2 and MMP-3. 17 EMMPRIN not only stimulates the production of interstitial collagenase (MMP-1) but also forms a complex with MMP-1 at the human lung carcinoma cell surface, which would facilitate invasive processes. 18 MMPs are a family of enzymes that degrade different components of the ECM, and a number of studies indicate that they play an important role in tissue remodeling, tumor invasion and metastasis. 19 -24 There are 2 distinct types of MMP, secreted and nonsecreted. Based on their substrate specificities, secreted MMPs are classified into collagenases (MMP-1, MMP-8 and MMP-13), gelatinases (MMP-2 and MMP-9) and stromelysins (MMP-3 and MMP-10). 20 Several nonsecreted MMPs are bound to membranes and designated MT-MMPs. 25 Tumor spread is a multistep process, which requires degradation or breakdown of the ECM and connective tissue and is caused by the concerted effects of these MMPs. 26 In the initial stage of tumor invasion, the gelatinases, particularly MMP-2, degrade components of the basement membrane, including type IV collagen. Although MMP-3, one of the stromelysins, also breaks down type IV collagen of the basement membrane, it degrades a variety of matrix components, including proteoglycans and noncollagenous glycoproteins such as laminin and fibronectin. Local tumor invasion is facilitated by collagenases, particularly MMP-1, which degrades the ECM. 20 MT1-MMP triggers tumor invasion by activating MMP-2. 25,27,28 Cutaneous MM is characterized by a high potential for invasion and metastasis. Previous studies reported the involvement of MMPs in migration, invasion, metastasis and progression of MM. Elevated expression of MMP-1, MMP-2 or MMP-9 was correlated with migration and invasion of cultured human melanoma cells. 21,22,29,30 In human melanoma lesions, positive correlations between tumor progressio...

show abstract

The inducible blood-brain barrier specific molecule HT7 is a novel immunoglobulin-like cell surface glycoprotein.

Cited by 151 publications

References 47 publications

Homo‐oligomer formation by basigin, an immunoglobulin superfamily member, via its N‐terminal immunoglobulin domain

Homo‐oligomer formation by basigin, an immunoglobulin superfamily member, via its N‐terminal immunoglobulin domain

Mouse multidrug resistance 1a/3 gene is the earliest known endothelial cell differentiation marker during blood‐brain barrier development

Basigin (cd147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts

Contact Info

Product

Resources

About