Hyaluronate depolymerization activity induced by progesterone in cultured fibroblasts derived from human uterine cervix.

Abstract:

:High-molecular-weight [14C]hyaluronate was incubated with cultured fibroblasts from human uterine cervix and skin, and then the depolymerization of the hyaluronate was investigated. [14C]Hyaluronate in the medium of skin fibroblasts was depolymerized into a constant molecular weight (M(r) about 40,000), whereas that of cervix fibroblasts was not depolymerized, irrespective of incubation period. However, when progesterone was added to the medium of cervix fibroblasts, hyaluronate was depolymerized to the same extent as that in skin fibroblasts. The reducing terminal sugar of the depolymerized hyaluronate was N-acetylglucosamine. These results suggest that a hyaluronate-depolymerizing enzyme, endo-beta-N-acetylglucosaminidase, was induced by progesterone in cultured fibroblasts derived from human uterine cervix.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Tanaka K,Nakamura T,Ikeya H,Higuchi T,Tanaka A,Morikawa A,Saito Y,Takagaki K,Endo M

doi

10.1016/0014-5793(94)00517-6

subject

Has Abstract

pub_date

1994-06-20 00:00:00

pages

95-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)00517-6

journal_volume

347

pub_type

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