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Articles by K Sakaguchi
Total Records ( 3 ) for K Sakaguchi
  X Xu , Y Horibata , M Inagaki , Y Hama , K Sakaguchi , H. M Goda and M. Ito
 

Endoglycoceramidase (EGCase; EC 3.2.1.123) is a glycohydrolase that hydrolyzes the glycosidic linkage between the oligosaccharide and ceramide of various glycosphingolipids. We previously reported that hydra produced EGCase to digest glycosphingolipids of brine shrimp (Artemia salina), a type of aquatic crustacean used as a diet for the culture of hydra (Horibata Y, Sakaguchi K, Okino N, Iida H, Inagaki M, Fujisawa T, Hama Y, Ito M. 2004. J Biol Chem. 279:33379-33389). We report here that a major glycosphingolipid of brine shrimp is unique in structure and highly sensitive to EGCase. The glycosphingolipid was extracted from freshly hatched brine shrimp by Folch's partition, followed by mild alkaline hydrolysis and purification with a Sep-Pak plus silica cartridge. The structure of brine shrimp glycosphingolipid was determined by gas chromatography, gas chromatography-mass spectrometry, fast-atom bombardment mass spectrometry, and 1H-NMR spectrometry to be GlcNAc1-2Fuc1-3Manβ1-4Glcβ1-1'Cer. Two major molecular species of the glycosphingolipid were identified; the sugar and sphingoid base of each were the same but the major fatty acid was C22:0 and 2-hydroxy C22:0, respectively. This is the first report describing the glycosphingolipid that has an internal fucosyl residue substituted with 1-2 N-acetylglucosaminyl residue. This study also suggests the biological relevance of the glycosphingolipid as a dietary source of hydra which possesses EGCase as a digestion enzyme.

  Y Tachibana , K Sakaguchi , T Goto , H Oda , K Yamazaki and S. Iida
  Background

Although several devices for meniscal repairs have become available, a successful outcome is ultimately due to a healed meniscus on the clinical findings. The authors assessed the repair integrity after meniscal repair with the FasT-Fix device using second-look arthroscopy.

Hypothesis

Meniscal repair with the FasT-Fix will lead to arthroscopically evident healing, but some menisci will show incomplete healing even in clinically successful cases and have newly formed injuries on the meniscal substance resulting from the path of the implant.

Study Design

Case series; Level of evidence, 4.

Methods

Sixty-five consecutive patients were studied, in whom 84 menisci were subjected to all-inside meniscal repair with the FasT-Fix device in conjunction with anterior cruciate ligament reconstruction. Repair was only performed on longitudinal or double longitudinal tears within the red-red or red-white zone. The repaired menisci were evaluated by second-look arthroscopy at the time of staged hardware removal after anterior cruciate ligament reconstruction.

Results

Sixty-two meniscal tears in 46 patients were available for this study. Eight patients were found to be symptomatic and considered to be clinical failures. The clinical success rate was 83%. At second-look arthroscopy, 46 tears (74%) were healed, 9 (15%) were healed incompletely, and 7 (11%) had failed. In the failed menisci, 1 had meniscal symptoms, while the other 6 were asymptomatic. In the 9 menisci with incomplete healing, 3 were associated with nonspecific knee pain but none showed meniscal symptoms. Newly formed injuries, which occurred in an area different from the original repair site, were confirmed on the surface of 19 menisci (35%) among the healed and incompletely healed menisci. Thirty menisci (48%) displayed successful and complete healing of the original tear site without newly formed tears.

Conclusion

Meniscal repair with the FasT-Fix in conjunction with anterior cruciate ligament reconstruction resulted in complete healing in 74% of cases. Eighty-three percent of menisci were symptom-free regardless of meniscal integrity. Even when the menisci repaired are asymptomatic and considered to be a clinical success, however, there may be newly formed injuries.

  M Kiyohara , K Sakaguchi , K Yamaguchi , T Araki and M. Ito
 

β-1,3-Xylanase from Vibrio sp. strain AX-4 (XYL4) is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules (CBMs) belonging to family 31 in the C-terminal region. To investigate the functions of these three modules, five deletion mutants lacking individual modules were constructed. The binding assay of these mutants showed that a repeating unit of the CBM was a non-catalytic β-1,3-xylan-binding module, while the catalytic module per se was not likely to contribute to the binding activity when insoluble β-1,3-xylan was used for the assay. The repeating CBMs were found to specifically bind to insoluble β-1,3-xylan, but not to β-1,4-xylan, Avicel, β-1,4-mannan, curdlan, chitin or soluble glycol-β-1,3-xylan. Both the enzyme and the binding activities for insoluble β-1,3-xylan but not soluble glycol-β-1,3-xylan were enhanced by NaCl in a concentration-dependent manner, indicating that the CBMs of XYL4 bound to β-1,3-xylan through hydrophobic interaction. This property of the CBMs was successfully applied to the purification of a recombinant XYL4 from the cell extracts of Escherichia coli transformed with the xyl4 gene and the detection of β-1,3-xylan-binding proteins including β-1,3-xylanase from the extract of a turban shell, Turbo cornutus.

 
 
 
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