Difference of hyaluronidase produced by human tumor cell lines with hyaluronidase present in human serum as revealed by zymography.

Abstract:

:Human carcinoma cells cultured in serum free medium produced an enzyme present as two different isoforms of 62 and 59 kDa which was found to degrade hyaluronan and chondroitin sulfate, with optimum activity at pH 4.0 and 0.03 M NaCl. The activity was suppressed by treatment with 250 mM apigenin and 1 mM DTT. The one-dimensional and two-dimensional gel patterns of tumor hyaluronidase differed from those of human serum hyaluronidase. Deglycosylation of tumor hyaluronidase caused nearly complete elimination of activity, suggesting the importance of sugar chains in enzymatic function. The results of treatment with neuraminidase, in addition to the findings for the enzyme mentioned above, suggest hyaluronidase from carcinoma cells and serum hyaluronidase to differ in sugar chains and/or the core protein. Tumor hyaluronidase was shown to be endo-beta-N-acetyl-D-hexosaminidase and tetrasaccharide was identified as the major product, thus indicating the tumor hyaluronidase to be a testis-type hyaluronidase.

authors

Podyma KA,Yamagata S,Sakata K,Yamagata T

doi

10.1006/bbrc.1997.7829

subject

Has Abstract

pub_date

1997-12-18 00:00:00

pages

446-52

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97829-3

journal_volume

241

pub_type

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