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OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes.

Tiwari-Woodruff SK, Buznikov AG, Vu TQ, Micevych PE, Chen K, Kornblum HI, Bronstein JM - J. Cell Biol. (2001)

Bottom Line: Overexpression of OSP/claudin-11 or OAP-1 induced proliferation in an oligodendrocyte cell line.Anti-OAP-1, anti-OSP/claudin-11, and anti-beta1 integrin antibodies inhibited migration of primary oligodendrocytes, and migration was impaired in OSP/claudin-11-deficient primary oligodendrocytes.These data suggest a role for OSP/claudin-11, OAP-1, and beta1 integrin complex in regulating proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, University of California at Los Angeles School of Medicine, Los Angeles, California 90095, USA.

ABSTRACT
Oligodendrocyte-specific protein (OSP)/claudin-11 is a major component of central nervous system myelin and forms tight junctions (TJs) within myelin sheaths. TJs are essential for forming a paracellular barrier and have been implicated in the regulation of growth and differentiation via signal transduction pathways. We have identified an OSP/claudin-11-associated protein (OAP)1, using a yeast two-hybrid screen. OAP-1 is a novel member of the tetraspanin superfamily, and it is widely expressed in several cell types, including oligodendrocytes. OAP-1, OSP/claudin-11, and beta1 integrin form a complex as indicated by coimmunoprecipitation and confocal immunocytochemistry. Overexpression of OSP/claudin-11 or OAP-1 induced proliferation in an oligodendrocyte cell line. Anti-OAP-1, anti-OSP/claudin-11, and anti-beta1 integrin antibodies inhibited migration of primary oligodendrocytes, and migration was impaired in OSP/claudin-11-deficient primary oligodendrocytes. These data suggest a role for OSP/claudin-11, OAP-1, and beta1 integrin complex in regulating proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.

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OSP/claudin-11 colocalizes with OAP-1 and β1 integrin in oligodendrocytes. (A) Confocal images of primary mouse oligodendrocytes shown in the top row were double labeled for OSP/claudin-11 (Texas red) and OAP-1 (FITC) or β1 integrin (FITC). Fused images are shown at the far right and bottom. Most cells showed striking colocalization of OSP/claudin-11, OAP-1, and β1 integrin. (B) Confocal images of primary mouse oligodendrocytes shown were double labeled for OAP-1 (Texas Red) and OSP/claudin-11 (FITC) in live primary oligodendrocytes. Fused images are showed to the far right. Colocalization of the two proteins was mostly observed in the cell borders. (C) Live primary oligodendrocytes were cultured on slides and immunostained with anti–OAP-1 (top row) and anti–OSP/claudin-11 (bottom row) antibody in the presence and absence of the respective antibody peptides. Background staining is also shown. Bars: (A, top row) 10 μM; (A, bottom row) 25 μM.
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Figure 5: OSP/claudin-11 colocalizes with OAP-1 and β1 integrin in oligodendrocytes. (A) Confocal images of primary mouse oligodendrocytes shown in the top row were double labeled for OSP/claudin-11 (Texas red) and OAP-1 (FITC) or β1 integrin (FITC). Fused images are shown at the far right and bottom. Most cells showed striking colocalization of OSP/claudin-11, OAP-1, and β1 integrin. (B) Confocal images of primary mouse oligodendrocytes shown were double labeled for OAP-1 (Texas Red) and OSP/claudin-11 (FITC) in live primary oligodendrocytes. Fused images are showed to the far right. Colocalization of the two proteins was mostly observed in the cell borders. (C) Live primary oligodendrocytes were cultured on slides and immunostained with anti–OAP-1 (top row) and anti–OSP/claudin-11 (bottom row) antibody in the presence and absence of the respective antibody peptides. Background staining is also shown. Bars: (A, top row) 10 μM; (A, bottom row) 25 μM.

Mentions: Additional confirmation of an association between OSP/claudin-11, OAP-1, and β1 integrin was obtained using double-labeled immunocytochemistry and confocal microscopy (Fig. 5 A). Controls with GFAP showed no colocalization with any of the experimental proteins (data not shown). A striking colocalization of OSP/claudin-11, OAP-1, and β1 integrin was observed in most oligodendrocytes (Fig. 5 A, third panel in rows 1 and 2). A few oligodendrocytes showed only partial colocalization (data not shown), suggesting that complex formation was under dynamic control or that the population of oligodendrocytes was heterogeneous.


OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes.

Tiwari-Woodruff SK, Buznikov AG, Vu TQ, Micevych PE, Chen K, Kornblum HI, Bronstein JM - J. Cell Biol. (2001)

OSP/claudin-11 colocalizes with OAP-1 and β1 integrin in oligodendrocytes. (A) Confocal images of primary mouse oligodendrocytes shown in the top row were double labeled for OSP/claudin-11 (Texas red) and OAP-1 (FITC) or β1 integrin (FITC). Fused images are shown at the far right and bottom. Most cells showed striking colocalization of OSP/claudin-11, OAP-1, and β1 integrin. (B) Confocal images of primary mouse oligodendrocytes shown were double labeled for OAP-1 (Texas Red) and OSP/claudin-11 (FITC) in live primary oligodendrocytes. Fused images are showed to the far right. Colocalization of the two proteins was mostly observed in the cell borders. (C) Live primary oligodendrocytes were cultured on slides and immunostained with anti–OAP-1 (top row) and anti–OSP/claudin-11 (bottom row) antibody in the presence and absence of the respective antibody peptides. Background staining is also shown. Bars: (A, top row) 10 μM; (A, bottom row) 25 μM.
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Related In: Results  -  Collection

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Figure 5: OSP/claudin-11 colocalizes with OAP-1 and β1 integrin in oligodendrocytes. (A) Confocal images of primary mouse oligodendrocytes shown in the top row were double labeled for OSP/claudin-11 (Texas red) and OAP-1 (FITC) or β1 integrin (FITC). Fused images are shown at the far right and bottom. Most cells showed striking colocalization of OSP/claudin-11, OAP-1, and β1 integrin. (B) Confocal images of primary mouse oligodendrocytes shown were double labeled for OAP-1 (Texas Red) and OSP/claudin-11 (FITC) in live primary oligodendrocytes. Fused images are showed to the far right. Colocalization of the two proteins was mostly observed in the cell borders. (C) Live primary oligodendrocytes were cultured on slides and immunostained with anti–OAP-1 (top row) and anti–OSP/claudin-11 (bottom row) antibody in the presence and absence of the respective antibody peptides. Background staining is also shown. Bars: (A, top row) 10 μM; (A, bottom row) 25 μM.
Mentions: Additional confirmation of an association between OSP/claudin-11, OAP-1, and β1 integrin was obtained using double-labeled immunocytochemistry and confocal microscopy (Fig. 5 A). Controls with GFAP showed no colocalization with any of the experimental proteins (data not shown). A striking colocalization of OSP/claudin-11, OAP-1, and β1 integrin was observed in most oligodendrocytes (Fig. 5 A, third panel in rows 1 and 2). A few oligodendrocytes showed only partial colocalization (data not shown), suggesting that complex formation was under dynamic control or that the population of oligodendrocytes was heterogeneous.

Bottom Line: Overexpression of OSP/claudin-11 or OAP-1 induced proliferation in an oligodendrocyte cell line.Anti-OAP-1, anti-OSP/claudin-11, and anti-beta1 integrin antibodies inhibited migration of primary oligodendrocytes, and migration was impaired in OSP/claudin-11-deficient primary oligodendrocytes.These data suggest a role for OSP/claudin-11, OAP-1, and beta1 integrin complex in regulating proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, University of California at Los Angeles School of Medicine, Los Angeles, California 90095, USA.

ABSTRACT
Oligodendrocyte-specific protein (OSP)/claudin-11 is a major component of central nervous system myelin and forms tight junctions (TJs) within myelin sheaths. TJs are essential for forming a paracellular barrier and have been implicated in the regulation of growth and differentiation via signal transduction pathways. We have identified an OSP/claudin-11-associated protein (OAP)1, using a yeast two-hybrid screen. OAP-1 is a novel member of the tetraspanin superfamily, and it is widely expressed in several cell types, including oligodendrocytes. OAP-1, OSP/claudin-11, and beta1 integrin form a complex as indicated by coimmunoprecipitation and confocal immunocytochemistry. Overexpression of OSP/claudin-11 or OAP-1 induced proliferation in an oligodendrocyte cell line. Anti-OAP-1, anti-OSP/claudin-11, and anti-beta1 integrin antibodies inhibited migration of primary oligodendrocytes, and migration was impaired in OSP/claudin-11-deficient primary oligodendrocytes. These data suggest a role for OSP/claudin-11, OAP-1, and beta1 integrin complex in regulating proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.

Show MeSH
Related in: MedlinePlus