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Characterization of a 54 kDa, α 1 Antitrypsin‐like Protein Isolated from Ascitic Fluid of an Endometrial Cancer Patient
Author(s) -
Tanaka Naotake,
Sekiya Souei,
Takamizawa Hiroyoshi,
Kato Noriko,
Moriyama Yoichi,
Fujimura Shinji
Publication year - 1991
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.1991.tb01905.x
Subject(s) - endometrial cancer , ascitic fluid , cancer , endometrium , medicine , pathology , gastroenterology , cancer research , ascites
A protein factor which stimulated [ 3 H]thymidine uptake into free hepatocytes prepared from normal mouse liver was detected in the ascitic fluid of gynecological cancer patients. The factor was subsequently further purified from the ascitic fluid of an endometrial cancer patient by DEAE‐Sephacel, Sephadex G‐150 and Phenyl‐Sepharose CL‐4B column chromatographies, and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed a single protein band of 54,000 Da, designated tentatively as 54K ascitic protein (54K‐AP). 54K‐AP was similar to human Qt‐antitrypsin (α 1 ‐AT) in terms of SDS‐PAGE and immunological behavior, but was slightly different in terms of amino acid sequence and isoelectric point. Although 54K‐AP inhibited the activities of bovine trypsin and a‐chymotrypsin as did human α 1 ‐AT, 54K‐AP inhibited the plasminogen activator released from human endometrial cancer Ishikawa cells more efficiently than α 1 ‐AT. Because, in contrast to normal serum, the serum from the endometrial cancer patients stimulated [ 3 H]thymidine uptake into hepatocytes, the possibility arises that 54K‐AP could he produced hy the cancer host as a defence mechanism against the cancer.

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