Expression of hyaluronic acid binding protein (HABP) and CD44 in murine temporomandibular joint synovium.

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Mechanisms regulating the binding activity of CD44 to hyaluronic acid.

CD44 is a cell surface glycoprotein present on many cell types. Many CD44 isoforms have been identified. All CD44 isoforms utilize identical transmembrane and cytoplasmic domains. The hematopoietic form of CD44 (CD44H) is the major CD44 protein present on normal human lymphocytes and monocytes. One of the ligands for CD44 is hyaluronic acid (HA), a polymer consisting of repeat units of disaccha...

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NADPH oxidases regulate CD44 and hyaluronic acid expression

3 The abbreviations used are: ROS, reactive oxygen species; VSMC, vascular smooth muscle cells, HA, hyaluronic acid; DMEM, Dulbecco’s modified Eagle’s medium; FBS, fetal bovine serum; Has2, hyaluronan synthase 2; Hyal3, hyaluronidase 3; LMW-HA, low-molecular-weight HA; HMW-HA, highmolecular-weight HA; DPI, diphenyleneiodonium chloride; DMNQ, 2,3-Dimethoxy-1,4-naphthoquinone; GKT136901 (2-(2-chl...

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CD44 Binding to Hyaluronic Acid Is Redox Regulated by a Labile Disulfide Bond in the Hyaluronic Acid Binding Site

CD44 is the primary leukocyte cell surface receptor for hyaluronic acid (HA), a component of the extracellular matrix. Enzymatic post translational cleavage of labile disulfide bonds is a mechanism by which proteins are structurally regulated by imparting an allosteric change and altering activity. We have identified one such disulfide bond in CD44 formed by Cys77 and Cys97 that stabilises the ...

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DIFFERENTIAL EXPRESSION OF SURFACE MARKERS CD45RB AND CD44 ON MURINE CD8+ CELLS

Considering the emerging importance of phenotypic markers as indicators of cell function and differentiation, we studied patterns ofCD44 and CD45RB expression in CD8+ murine T cells with prior exposure to antigen or staphylococcal enterotoxin B ( SEB ). Following in vivo priming with two purified protein derivatives (one from a virulent WHO strain and the other from an avirulent strain), T ...

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A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid

In the transmembrane domain and cytoplasmic domain of human CD44 protein there are two cysteine residues. These two cysteines are conserved in all known mammalian CD44 proteins. The functions of these cysteine residues are not known. Site-specific mutagenesis was used to create CD44 mutant proteins lacking either one or both of these cysteine residues. Wild-type CD44 and mutant CD44 genes were ...

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ژورنال

عنوان ژورنال: Japanese Journal of Oral & Maxillofacial Surgery

سال: 2002

ISSN: 2186-1579,0021-5163

DOI: 10.5794/jjoms.48.349