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Lectin‐based electrophoretic analysis of the expression of the 35 kDa inter‐α‐trypsin inhibitor heavy chain H4 fragment in sera of patients with five different malignancies
Author(s) -
Mohamed Emida,
AbdulRahman Puteri Shafinaz,
Doustjalali Saeid Reza,
Chen Yeng,
Lim BoonKiong,
Omar Siti Zawiah,
Bustam Anita Zarina,
Singh Vivek Ajit,
MohdTaib Nur Aishah,
Yip ChengHar,
Hashim Onn Haji
Publication year - 2008
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200700828
Subject(s) - lectin , trypsin , glycoprotein , chemistry , cancer research , carcinoma , microbiology and biotechnology , biology , biochemistry , enzyme , genetics
A 35 kDa glycoprotein whose abundance was previously demonstrated to be enhanced in sera of patients with endometrial adenocarcinoma ( n = 12), was isolated from pooled sera of three of the cancer patients using champedak galactose‐binding lectin affinity chromatography in the present study. Subjecting it to 2‐DE and MS/MS, the glycoprotein was identified as the O ‐glycosylated fragment of inter‐α‐trypsin inhibitor heavy chain H4 (ITIH4). When compared to control sera ( n = 17), expression of the 35 kDa ITIH4 cleavage fragment was demonstrated to be significantly enhanced in sera of patients with breast carcinoma ( n = 10), epithelial ovarian carcinoma ( n = 10), and germ cell ovarian carcinoma ( n = 10) but not in patients with nasopharyngeal carcinoma ( n = 13) and osteosarcoma ( n = 7). The lectin‐based electrophoretic bioanalytical method adopted in the present study may be used to assess the physiological relevance of ITIH4 fragmentation and its correlation with different malignancies, their stages and progression.