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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.

Show MeSH
OAP-1 belongs to the tetraspanin family of proteins. (A) Multiple sequence alignment of OAP-1 with murine tetraspanins (mA15, mCD53, mCD63, mCD82), a rat tetraspanin (rTspan-2), and a human tetraspanin (hTspan-3). Boxed residues denote conservation among TM4SFs. (B) Kyte-Doolittle hydropathy plot of the predicted amino acid sequence of OAP-1, predicting four-transmembrane hydrophobic domains (arrows).
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Figure 1: OAP-1 belongs to the tetraspanin family of proteins. (A) Multiple sequence alignment of OAP-1 with murine tetraspanins (mA15, mCD53, mCD63, mCD82), a rat tetraspanin (rTspan-2), and a human tetraspanin (hTspan-3). Boxed residues denote conservation among TM4SFs. (B) Kyte-Doolittle hydropathy plot of the predicted amino acid sequence of OAP-1, predicting four-transmembrane hydrophobic domains (arrows).

Mentions: Anti–OSP/claudin-11 antibody was made as described previously (Bronstein et al. 1997). Rabbit polyclonal antibodies for OAP-1 were raised against an 18–amino acid peptide (H-YSDWENTDWFKETKNQSV-OH) conjugated to keyhole limpet hemocyanin (Research Genetics). The 18 amino acids (153–170) (see Fig. 1) correspond to a region within the putative second extracellular loop of OAP-1. Antibody specificity was confirmed by Western blot, immunohistochemistry, and peptide competition experiments. Anti-GFAP antibody, peroxidase-conjugated, and horseradish-conjugated goat anti–rabbit antibody were purchased from Zymed Laboratories. Anti–β1 integrin antibody (Chemicon), Texas red–labeled and FITC-labeled goat anti–rabbit antibody, FITC-labeled goat anti–mouse antibody (Vector Laboratories), and anti-GalC antibody (Boehringer) were used in different concentrations for immunohistochemistry and in some cases for Western blots and migration assays.


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)

OAP-1 belongs to the tetraspanin family of proteins. (A) Multiple sequence alignment of OAP-1 with murine tetraspanins (mA15, mCD53, mCD63, mCD82), a rat tetraspanin (rTspan-2), and a human tetraspanin (hTspan-3). Boxed residues denote conservation among TM4SFs. (B) Kyte-Doolittle hydropathy plot of the predicted amino acid sequence of OAP-1, predicting four-transmembrane hydrophobic domains (arrows).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2169454&req=5

Figure 1: OAP-1 belongs to the tetraspanin family of proteins. (A) Multiple sequence alignment of OAP-1 with murine tetraspanins (mA15, mCD53, mCD63, mCD82), a rat tetraspanin (rTspan-2), and a human tetraspanin (hTspan-3). Boxed residues denote conservation among TM4SFs. (B) Kyte-Doolittle hydropathy plot of the predicted amino acid sequence of OAP-1, predicting four-transmembrane hydrophobic domains (arrows).
Mentions: Anti–OSP/claudin-11 antibody was made as described previously (Bronstein et al. 1997). Rabbit polyclonal antibodies for OAP-1 were raised against an 18–amino acid peptide (H-YSDWENTDWFKETKNQSV-OH) conjugated to keyhole limpet hemocyanin (Research Genetics). The 18 amino acids (153–170) (see Fig. 1) correspond to a region within the putative second extracellular loop of OAP-1. Antibody specificity was confirmed by Western blot, immunohistochemistry, and peptide competition experiments. Anti-GFAP antibody, peroxidase-conjugated, and horseradish-conjugated goat anti–rabbit antibody were purchased from Zymed Laboratories. Anti–β1 integrin antibody (Chemicon), Texas red–labeled and FITC-labeled goat anti–rabbit antibody, FITC-labeled goat anti–mouse antibody (Vector Laboratories), and anti-GalC antibody (Boehringer) were used in different concentrations for immunohistochemistry and in some cases for Western blots and migration assays.

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