Search results for: Donald A. Withers

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A sphingosine-dependent protein kinase that specifically phosphorylates 14-3-3 (SDK1) is identified as the kinase domain of PKCδ: a preliminary note

Akikazu Hamaguchi, Erika Suzuki, Kimie Murayama, Tsutomu Fujimura, more

Biochemical and Biophysical Research Communications > 2003 > 307 > 3 > 589-594

A specific protein kinase that phosphorylates Ser60, Ser59, or Ser58 of 14-3-3β, η, or ζ, respectively, only in the presence of sphingosine (Sph) or N,N-dimethyl-Sph (DMS), was termed ''sphingosine-dependent protein kinase-1'' (SDK1) [J. Biol. Chem. 273(34) (1998) 21834]. We have now identified SDK1 as a protein having the same amino acid sequence as in the C-terminal-half kinase domain of PKCδ, with...

article

Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: possible role of disialogangliosides in tumor progression

Akihiro Ito, Kazuko Handa, Donald A. Withers, Makoto Satoh, more

FEBS Letters > 2001 > 504 > 1-2 > 82-86

Previous studies indicate that expression of higher gangliosides in renal cell carcinoma (RCC) is correlated with metastatic potential, particularly in the lung. Out of five major gangliosides in RCC, three disialogangliosides (disialogalactosylgloboside, IV³NeuAcIII⁶NeuAcLc₄, and IV⁴GalNAcIV³NeuAcIII⁶NeuAcLc₄) bind strongly to siglec7, which is expressed highly in monocytes and natural killer cells...

article

Erratum to: Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: possible role of disialogangliosides in tumor progression (FEBS 24901)

Akihiro Ito, Kazuko Handa, Donald A. Withers, Makoto Satoh, more

FEBS Letters > 2001 > 504 > 1-2 > 81

article

Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: possible role of disialogangliosides in tumor progression

Akihiro Ito, Kazuko Handa, Donald A. Withers, Makoto Satoh, more

FEBS Letters > 2001 > 498 > 1 > 116-120

Previous studies indicate that expression of higher gangliosides in renal cell carcinoma (RCC) is correlated with metastatic potential, particularly in the lung. Out of five major gangliosides in RCC, three disialogangliosides (disialogalactosylgloboside, IV ³ NeuAcIII ⁶ NeuAcLc ₄ , and IV ⁴ GalNAcIV ³ NeuAcIII ⁶ NeuAcLc ₄ ) bind strongly to...

article

GM3 Ganglioside Inhibits CD9-Facilitated Haptotactic Cell Motility: Coexpression of GM3 and CD9 Is Essential in the Downregulation of Tumor Cell Motility and Malignancy ^†

Masaya Ono, Kazuko Handa, Sandro Sonnino, Donald A. Withers, more

Biochemistry > 2001 > 40 > 21 > 6414 - 6421

article

Glycosylation Effect on Membrane Domain (GEM) Involved in Cell Adhesion and Motility: A Preliminary Note on Functional α3, α5-CD82 Glycosylation Complex in ldlD 14 Cells

Masaya Ono, Kazuko Handa, Donald A. Withers, Sen-itiroh Hakomori

Biochemical and Biophysical Research Communications > 2000 > 279 > 3 > 744-750

Laminin (LN)- or fibronectin (FN)-dependent adhesion in Krieger's ldlD 14 (D14) cells is enhanced significantly in the presence vs absence, of galactose (Gal), whereas LN- or FN-induced haptotactic cell motility is barely affected unless cells express CD82 by its gene transfection (cells termed D14/CD82). The effect of CD82 on LN- or FN-induced motility is based on its ability to associate with α3...

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Deletion of A-antigen in a human cancer cell line is associated with reduced promoter activity of CBF/NF-Y binding region, and possibly with enhanced DNA methylation of A transferase promoter

Sadahiko Iwamoto, Donald A. Withers, Kazuko Handa, Sen-itiroh Hakomori

Glycoconjugate Journal > 1999 > 16 > 10 > 659-666

Employing blood group A⁻ and A⁺ clones derived from the same parental colonic cancer cell lines, we studied the molecular mechanism of deletion/ reduction vs. continuous expression of A antigen in A tumors, a crucial determinant of human tumor malignancy. A⁻ transferase mRNA level in one of the A⁻ clones (A⁻ SW480) was undetectable, while that in A⁺ SW480 was strongly detectable by semiquantitative...

article

The α1 -> 3 Fucosylation at the Penultimate GlcNAc Catalyzed by Fucosyltransferase VII Is Blocked by Internally Fucosylated Residue in Sialosyl Long-Chain Poly-LacNAc: Enzymatic Basis for Expression of Physiological E-Selectin Epitope

Kazuko Handa, Donald A. Withers, Sen-itiroh Hakomori

Biochemical and Biophysical Research Communications > 1998 > 243 > 1 > 199-204

Sialosyl-fucosyl poly-LacNAc without sialosyl-Le ^x epitope in myeloid cell line HL60 was shown to be the ligand for E-selectin-dependent adhesion, particularly under dynamic flow conditions, in our previous study (Handa K, Stroud MR, Hakomori S,Biochemistry36, 12412-12420, 1997). HL60 cells express only fucosyltransferase (FT) IV and VII. X ³ NeuAcVII ³ FucnLc ₁ ₀ ...

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