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Volumn 30, Issue 1, 2000, Pages 245-253

The role of the CD44 cytoplasmic and transmembrane domains in constitutive and inducible hyaluronan binding

Author keywords

CD44; Cytoplasmic domain; Dimerization; Hyaluronan binding; Transmembrane domain

Indexed keywords

CHIMERIC PROTEIN; HERMES ANTIGEN; HYALURONIC ACID; INTEGRIN; MUTANT PROTEIN;

EID: 0033987011     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/1521-4141(200001)30:1<245::AID-IMMU245>3.0.CO;2-X     Document Type: Article
Times cited : (51)

References (52)
  • 1
    • 0028270665 scopus 로고
    • Hyaluronan binding function of CD44 is transiently activated on T cells during an in vivo immune response
    • Lesley, J., Howes, N., Perschl, A. and Hyman, R., Hyaluronan binding function of CD44 is transiently activated on T cells during an in vivo immune response. J. Exp. Med. 1994. 180: 383-387.
    • (1994) J. Exp. Med. , vol.180 , pp. 383-387
    • Lesley, J.1    Howes, N.2    Perschl, A.3    Hyman, R.4
  • 2
    • 0025245009 scopus 로고
    • IL-5 induces a Pgp-1 (CD44) bright B cell subpopulation that is highly enriched in proliferative and Ig secretory activity and binds to hyaluronate
    • Murakami, S., Miyake, K., June, C. H., Kincade, P. W. and Hodes, R. J., IL-5 induces a Pgp-1 (CD44) bright B cell subpopulation that is highly enriched in proliferative and Ig secretory activity and binds to hyaluronate. J. Immunol. 1990. 145: 3618-3627.
    • (1990) J. Immunol. , vol.145 , pp. 3618-3627
    • Murakami, S.1    Miyake, K.2    June, C.H.3    Kincade, P.W.4    Hodes, R.J.5
  • 4
    • 0027377499 scopus 로고
    • Regulation of human CD44H and CD44E isoform binding to hyaluronan by phorbol myristate acetate and anti-CD44 monoclonal and polyclonal antibodies
    • Liao, H.-X., Levesque, M. C., Patton, K., Bergamo, B., Jones, D., Moody, M. A., Telen, M. J. and Haynes, B. F., Regulation of human CD44H and CD44E isoform binding to hyaluronan by phorbol myristate acetate and anti-CD44 monoclonal and polyclonal antibodies. J. Immunol. 1993. 151: 6490-6499.
    • (1993) J. Immunol. , vol.151 , pp. 6490-6499
    • Liao, H.-X.1    Levesque, M.C.2    Patton, K.3    Bergamo, B.4    Jones, D.5    Moody, M.A.6    Telen, M.J.7    Haynes, B.F.8
  • 5
    • 0029966274 scopus 로고    scopus 로고
    • CD44 and its ligand hyaluronate mediate rolling under physiologic flow: A novel lymphocyte-endothelial cell primary adhesion pathway
    • DeGrendele, H. C., Estess, P., Picker, L. J. and Siegelman, M. H., CD44 and its ligand hyaluronate mediate rolling under physiologic flow: a novel lymphocyte-endothelial cell primary adhesion pathway. J. Exp. Med. 1996. 183: 1119-1130.
    • (1996) J. Exp. Med. , vol.183 , pp. 1119-1130
    • DeGrendele, H.C.1    Estess, P.2    Picker, L.J.3    Siegelman, M.H.4
  • 6
    • 0030690228 scopus 로고    scopus 로고
    • Requirement for CD44 in activated T cell extravasation into an inflammatory site
    • DeGrendele, H. C., Estess, P. and Siegelman, M. H., Requirement for CD44 in activated T cell extravasation into an inflammatory site. Science 1997. 278: 672-675.
    • (1997) Science , vol.278 , pp. 672-675
    • DeGrendele, H.C.1    Estess, P.2    Siegelman, M.H.3
  • 7
    • 0030602171 scopus 로고    scopus 로고
    • Binding of CD44 to hyaluronic acid can be induced by multiple signals and requires the CD44 cytoplasmic domain
    • Liu, D., Zhang, D., Mori, H. and Sy, M.-S., Binding of CD44 to hyaluronic acid can be induced by multiple signals and requires the CD44 cytoplasmic domain. Cell Immunol. 1996. 174: 73-83.
    • (1996) Cell Immunol. , vol.174 , pp. 73-83
    • Liu, D.1    Zhang, D.2    Mori, H.3    Sy, M.-S.4
  • 8
    • 0032582805 scopus 로고    scopus 로고
    • TNF-α induction of CD44-mediated leukocyte adhesion by sulfation
    • Maiti, A., Maki, G. and Johnson, P., TNF-α induction of CD44-mediated leukocyte adhesion by sulfation. Science 1998. 282: 941-943.
    • (1998) Science , vol.282 , pp. 941-943
    • Maiti, A.1    Maki, G.2    Johnson, P.3
  • 9
    • 0026537561 scopus 로고
    • Requirements for hyaluronic acid binding by CD44: A role for the cytoplasmic domain and activation by antibody
    • Lesley, J., He, Q., Miyake, K., Hamann, A., Hyman, R. and Kincade, P., Requirements for hyaluronic acid binding by CD44: A role for the cytoplasmic domain and activation by antibody. J. Exp. Med. 1992. 175: 257-266.
    • (1992) J. Exp. Med. , vol.175 , pp. 257-266
    • Lesley, J.1    He, Q.2    Miyake, K.3    Hamann, A.4    Hyman, R.5    Kincade, P.6
  • 10
    • 0026801075 scopus 로고
    • CD44 can be activated to function as an hyaluronic acid receptor in normal murine T-cells
    • Lesley, J. and Hyman, R., CD44 can be activated to function as an hyaluronic acid receptor in normal murine T-cells. Eur J. Immunol. 1992. 22: 2719-2723.
    • (1992) Eur J. Immunol. , vol.22 , pp. 2719-2723
    • Lesley, J.1    Hyman, R.2
  • 11
    • 0025282411 scopus 로고
    • CD44 is the principal cell surface receptor for hyaluronate
    • Aruffo, A., Stamenkovic, I., Melnick, M., Underbill, C. B. and Seed, B., CD44 is the principal cell surface receptor for hyaluronate. Cell 1990. 61: 1303-1313.
    • (1990) Cell , vol.61 , pp. 1303-1313
    • Aruffo, A.1    Stamenkovic, I.2    Melnick, M.3    Underbill, C.B.4    Seed, B.5
  • 12
    • 0032529429 scopus 로고    scopus 로고
    • Site-specific de-N-glycosylation of CD44 can activate hyaluronan binding and CD44 activation states show distinct threshold densities for hyaluronan binding
    • English, N., Lesley, J. and Hyman, R., Site-specific de-N-glycosylation of CD44 can activate hyaluronan binding and CD44 activation states show distinct threshold densities for hyaluronan binding. Cancer Res. 1998. 58: 3736-3742.
    • (1998) Cancer Res. , vol.58 , pp. 3736-3742
    • English, N.1    Lesley, J.2    Hyman, R.3
  • 14
    • 0028897337 scopus 로고
    • Defective phosphorylation and hyaluronate binding of CD44 with point mutations in the cytoplasmic domain
    • Pure, E., Camp, R., Peritt, D., Panettieri, R., Lazaar, A. and Nayak, S., Defective phosphorylation and hyaluronate binding of CD44 with point mutations in the cytoplasmic domain. J. Exp. Med. 1995. 181: 55-62.
    • (1995) J. Exp. Med. , vol.181 , pp. 55-62
    • Pure, E.1    Camp, R.2    Peritt, D.3    Panettieri, R.4    Lazaar, A.5    Nayak, S.6
  • 15
    • 0027101721 scopus 로고
    • Phosphorylation of CD44 in vivo requires both Ser 323 and Ser 325, but does not regulate membrane localization or cytoskeletal interaction in epithelial cells
    • Neame, S. and Isacke, C., Phosphorylation of CD44 in vivo requires both Ser 323 and Ser 325, but does not regulate membrane localization or cytoskeletal interaction in epithelial cells. EMBO J. 1992. 11: 4733-4738.
    • (1992) EMBO J. , vol.11 , pp. 4733-4738
    • Neame, S.1    Isacke, C.2
  • 16
    • 0032535118 scopus 로고    scopus 로고
    • Identification of two regions in the cytoplasmic domain of CD44 through which PMA, calcium, and forskolin differentially regulate the binding of CD44 to hyaluronic acid
    • Liu, D., Liu, T. and Sy, M. S., Identification of two regions in the cytoplasmic domain of CD44 through which PMA, calcium, and forskolin differentially regulate the binding of CD44 to hyaluronic acid. Cell. Immunol. 1998. 190: 132-140.
    • (1998) Cell. Immunol. , vol.190 , pp. 132-140
    • Liu, D.1    Liu, T.2    Sy, M.S.3
  • 17
    • 0028141591 scopus 로고
    • Ankyrin-binding domain of CD44 (GP85) is required for the expression of hyaluronic acid-mediated adhesion function
    • Lokeshwar, V., Fregien, N. and Bourguignon, L., Ankyrin-binding domain of CD44 (GP85) is required for the expression of hyaluronic acid-mediated adhesion function. J. Cell Biol. 1994. 126: 1099-1109.
    • (1994) J. Cell Biol. , vol.126 , pp. 1099-1109
    • Lokeshwar, V.1    Fregien, N.2    Bourguignon, L.3
  • 18
    • 0029055188 scopus 로고
    • Hyaluronan binding by CD44 is regulated by a phosphorylation-independent mechanism
    • Uff, C., Neame, S. and Isacke, C., Hyaluronan binding by CD44 is regulated by a phosphorylation-independent mechanism. Eur. J. Immunol. 1995. 25: 1883-1887.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1883-1887
    • Uff, C.1    Neame, S.2    Isacke, C.3
  • 19
    • 0032482323 scopus 로고    scopus 로고
    • Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44
    • Legg, J. W. and Isacke, C. M., Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44. Curr. Biol. 1998. 8: 705-708.
    • (1998) Curr. Biol. , vol.8 , pp. 705-708
    • Legg, J.W.1    Isacke, C.M.2
  • 21
    • 0029904110 scopus 로고    scopus 로고
    • A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid
    • Liu, D. and Sy, M.-S., A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid. J. Exp. Med. 1996. 183: 1987-1994.
    • (1996) J. Exp. Med. , vol.183 , pp. 1987-1994
    • Liu, D.1    Sy, M.-S.2
  • 22
    • 0031571729 scopus 로고    scopus 로고
    • Phorbol myristate acetate stimulates the dimerization of CD44 involving a cysteine in the transmembrane domain
    • Liu, D. and Sy, M.-S., Phorbol myristate acetate stimulates the dimerization of CD44 involving a cysteine in the transmembrane domain. J. Immunol. 1997. 159: 2702-2711.
    • (1997) J. Immunol. , vol.159 , pp. 2702-2711
    • Liu, D.1    Sy, M.-S.2
  • 25
    • 0027491845 scopus 로고
    • CD44 and its interaction with extracellular matrix
    • Lesley, J., Hyman, R. and Kincade, P., CD44 and its interaction with extracellular matrix. Adv. Immunol. 1993. 54: 271-335.
    • (1993) Adv. Immunol. , vol.54 , pp. 271-335
    • Lesley, J.1    Hyman, R.2    Kincade, P.3
  • 26
    • 0025308383 scopus 로고
    • Binding of hyaluronic acid to lymphoid cell lines is inhibited by monoclonal antibodies against Pgp-1
    • Lesley, J., Schulte, R. and Hyman, R., Binding of hyaluronic acid to lymphoid cell lines is inhibited by monoclonal antibodies against Pgp-1. Exp. Cell Res. 1990. 187: 224-233.
    • (1990) Exp. Cell Res. , vol.187 , pp. 224-233
    • Lesley, J.1    Schulte, R.2    Hyman, R.3
  • 27
    • 0029946652 scopus 로고    scopus 로고
    • Regulation of leukocyte integrin function: Affinity vs. Avidity
    • Stewart, M. and Hogg, N., Regulation of leukocyte integrin function: Affinity vs. avidity. J. Cell. Biochem. 1996. 61: 554-561.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 554-561
    • Stewart, M.1    Hogg, N.2
  • 28
    • 0025856309 scopus 로고
    • Role of lymphocyte adhesion receptors in transient interactions and cell locomotion
    • Dustin, M. L. and Springer, T. A., Role of lymphocyte adhesion receptors in transient interactions and cell locomotion. Annu. Rev. Immunol. 1991. 9: 27-66.
    • (1991) Annu. Rev. Immunol. , vol.9 , pp. 27-66
    • Dustin, M.L.1    Springer, T.A.2
  • 29
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil, S., Kashiwagi, H. and Pampori, N., Integrin signaling: The platelet paradigm. Blood 1998. 91: 2645-2657.
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.1    Kashiwagi, H.2    Pampori, N.3
  • 30
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni, G. and Hemler, M., Are changes in integrin affinity and conformation overemphasized? Trends Biochem. Sci. 1998. 23: 30-34.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.2
  • 31
    • 0001286055 scopus 로고    scopus 로고
    • CD44 structure and function
    • Lesley, J. and Hyman, R., CD44 Structure and Function. Front. Biosci. 1998. 3: 616-630.
    • (1998) Front. Biosci. , vol.3 , pp. 616-630
    • Lesley, J.1    Hyman, R.2
  • 32
    • 0028922840 scopus 로고
    • Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts
    • Perschl, A., Lesley, J., English, N., Hyman, R. and Trowbridge, I., Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts. J. Cell Sci. 1995. 108: 1033-1041.
    • (1995) J. Cell Sci. , vol.108 , pp. 1033-1041
    • Perschl, A.1    Lesley, J.2    English, N.3    Hyman, R.4    Trowbridge, I.5
  • 33
    • 0032555935 scopus 로고    scopus 로고
    • The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity
    • Ozawa, M. and Kemler, R., The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity. J. Cell Biol. 1998. 142: 1605-1613.
    • (1998) J. Cell Biol. , vol.142 , pp. 1605-1613
    • Ozawa, M.1    Kemler, R.2
  • 34
    • 0029913643 scopus 로고    scopus 로고
    • Adhesion-activating phorbol ester increases the mobility of leukocyte intgrin LFA-1 in cultured lymphocytes
    • Kucik, D., Dustin, M., Miller, J. and Brown, E., Adhesion-activating phorbol ester increases the mobility of leukocyte intgrin LFA-1 in cultured lymphocytes. J. Clin. Invest. 1996. 97: 2139-2144.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2139-2144
    • Kucik, D.1    Dustin, M.2    Miller, J.3    Brown, E.4
  • 35
    • 0027197441 scopus 로고
    • Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody
    • Lesley, J., Kincade, P. and Hyman, R., Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody. Eur. J. Immunol. 1993. 23: 1902-1909.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1902-1909
    • Lesley, J.1    Kincade, P.2    Hyman, R.3
  • 36
    • 0029095821 scopus 로고
    • Glycosylation of CD44 negatively regulates its recognition of hyaluronan
    • Katoh, S., Zheng, Z., Oritani, K., Shimozato, T. and Kincade, P., Glycosylation of CD44 negatively regulates its recognition of hyaluronan. J. Exp. Med. 1995. 182: 419-429.
    • (1995) J. Exp. Med. , vol.182 , pp. 419-429
    • Katoh, S.1    Zheng, Z.2    Oritani, K.3    Shimozato, T.4    Kincade, P.5
  • 37
    • 0027144466 scopus 로고
    • CD44 expression on activated B cells. Differential capacity for CD44-dependent binding to hyaluronic acid
    • Hathcock, K. S., Hirano, H., Murakami, S. and Hodes, R. J., CD44 expression on activated B cells. Differential capacity for CD44-dependent binding to hyaluronic acid. J. Immunol. 1993. 151: 6712-6722.
    • (1993) J. Immunol. , vol.151 , pp. 6712-6722
    • Hathcock, K.S.1    Hirano, H.2    Murakami, S.3    Hodes, R.J.4
  • 39
    • 0029094899 scopus 로고
    • Variant cell lines selected for alterations in the function of the hyaluronan receptor CD44 show differences in glycosylation
    • Lesley, J., English, N., Perschl, A., Gregoroff, J. and Hyman, R., Variant cell lines selected for alterations in the function of the hyaluronan receptor CD44 show differences in glycosylation. J. Exp. Med. 1995. 182: 431-437.
    • (1995) J. Exp. Med. , vol.182 , pp. 431-437
    • Lesley, J.1    English, N.2    Perschl, A.3    Gregoroff, J.4    Hyman, R.5
  • 40
    • 0030567971 scopus 로고    scopus 로고
    • O-linked glycosylation modifies CD44 adhesion to hyaluronate in colon carcinoma cells
    • Dasgupta, A., Takahashi, K., Cutler, M. and Tanabe, K. K., O-linked glycosylation modifies CD44 adhesion to hyaluronate in colon carcinoma cells. Biochem. Biophys. Res. Commun. 1996. 227: 110-117.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 110-117
    • Dasgupta, A.1    Takahashi, K.2    Cutler, M.3    Tanabe, K.K.4
  • 41
    • 0029928193 scopus 로고    scopus 로고
    • Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan
    • Bartolazzi, A., Nocks, A., Aruffo, A., Spring, F. and Stamenkovic, I., Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan. J. Cell Biol. 1996. 132: 1199-1208.
    • (1996) J. Cell Biol. , vol.132 , pp. 1199-1208
    • Bartolazzi, A.1    Nocks, A.2    Aruffo, A.3    Spring, F.4    Stamenkovic, I.5
  • 42
  • 43
    • 0030930218 scopus 로고    scopus 로고
    • Growth as a solid tumor or reduced glucose concentrations in culture reversibly induce CD44-mediated hyaluronan recognition by Chinese hamster ovary cells
    • Zheng, Z., Cummings, R., Pummill, P. and Kincade, P., Growth as a solid tumor or reduced glucose concentrations in culture reversibly induce CD44-mediated hyaluronan recognition by Chinese hamster ovary cells. J. Clin. Invest. 1997. 100: 1217-1229.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1217-1229
    • Zheng, Z.1    Cummings, R.2    Pummill, P.3    Kincade, P.4
  • 44
    • 0031956737 scopus 로고    scopus 로고
    • Analysis of CD44 interactions with hyaluronan in murine L cell fibroblasts deficient in glycosaminoglycan synthesis: A role for chondroitin sulfate
    • Esford, L. E., Maiti, A., Bader, S. A., Tufaro, F. and Johnson, P., Analysis of CD44 interactions with hyaluronan in murine L cell fibroblasts deficient in glycosaminoglycan synthesis: a role for chondroitin sulfate. J. Cell Sci. 1998. 111: 1021-1029.
    • (1998) J. Cell Sci. , vol.111 , pp. 1021-1029
    • Esford, L.E.1    Maiti, A.2    Bader, S.A.3    Tufaro, F.4    Johnson, P.5
  • 45
    • 0032567715 scopus 로고    scopus 로고
    • Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan
    • Skelton, T. P., Zeng, C., Nocks, A. and Stamenkovic, I., Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan. J. Cell Biol. 1998. 140: 431-446.
    • (1998) J. Cell Biol. , vol.140 , pp. 431-446
    • Skelton, T.P.1    Zeng, C.2    Nocks, A.3    Stamenkovic, I.4
  • 46
    • 0027930281 scopus 로고
    • The role of the cytoplasmic domain in regulating CD44 function
    • Isacke, C., The role of the cytoplasmic domain in regulating CD44 function. J. Cell Sci. 1994. 107: 2353-2359.
    • (1994) J. Cell Sci. , vol.107 , pp. 2353-2359
    • Isacke, C.1
  • 48
    • 0020067501 scopus 로고
    • Biochemical characterization and cellular distribution of a polymorphic, murine cell-surface glycoprotein expressed on lymphoid tissues
    • Trowbridge, I. S., Lesley, J., Schulte, R., Hyman, R. and Trotter, J., Biochemical characterization and cellular distribution of a polymorphic, murine cell-surface glycoprotein expressed on lymphoid tissues. Immunogenetics 1982. 15: 299-312.
    • (1982) Immunogenetics , vol.15 , pp. 299-312
    • Trowbridge, I.S.1    Lesley, J.2    Schulte, R.3    Hyman, R.4    Trotter, J.5
  • 49
    • 0031425531 scopus 로고    scopus 로고
    • The 3'-end of the human β-actin gene enhances activity of the β-actin expression vector system: Construction of improved vectors
    • Qin, H. and Gunning, P., The 3'-end of the human β-actin gene enhances activity of the β-actin expression vector system: construction of improved vectors. J. Biochem. Biophys. Methods 1997. 36: 63-72.
    • (1997) J. Biochem. Biophys. Methods , vol.36 , pp. 63-72
    • Qin, H.1    Gunning, P.2
  • 50
    • 0027048901 scopus 로고
    • Molecular isoforms of murine CD44 and evidence that the membrane proximal domain is not critical for hyaluronate recognition
    • He, Q., Lesley, J., Hyman, R., Ishihara, K. and Kincade, P., Molecular isoforms of murine CD44 and evidence that the membrane proximal domain is not critical for hyaluronate recognition. J. Cell. Biol. 1992. 119: 1711-1719.
    • (1992) J. Cell. Biol. , vol.119 , pp. 1711-1719
    • He, Q.1    Lesley, J.2    Hyman, R.3    Ishihara, K.4    Kincade, P.5
  • 51
    • 0019989719 scopus 로고
    • Transformation of mammalian cells to antibiotic resistence with a bacterial gene under control of the SV40 early region promoter
    • Southern, P. J. and Berg, P., Transformation of mammalian cells to antibiotic resistence with a bacterial gene under control of the SV40 early region promoter. J. Appl. Mol. Genet. 1982. 1: 327-341.
    • (1982) J. Appl. Mol. Genet. , vol.1 , pp. 327-341
    • Southern, P.J.1    Berg, P.2
  • 52
    • 0024560984 scopus 로고
    • A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family
    • Stamenkovic, I., Amiot, M., Pesando, J. M. and Seed, B., A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family. Cell 1989. 56: 1057-1062.
    • (1989) Cell , vol.56 , pp. 1057-1062
    • Stamenkovic, I.1    Amiot, M.2    Pesando, J.M.3    Seed, B.4


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