Properties of α₁‐antitrypsin secreted by human adenocarcinoma cell lines

Abstract

~,-Antit~psin; (a,-AT) produced by various human carcinoma (non-hepatoma) cell lines were analyzed. Ftve out of eight ceil lines secreted detectable amounts of a,-AT into the ~onditloned media. All were aden~arcinoma cell lines. The tumor cell-derived a,-ATs had higher molecular weights (MW) than the normal plasma form. Most of this difference was an overall reflection of altered ~-~ycosylation. As judged by binding of iectins, the glycosyiation had shifted towards higher levels of triantennary oligosaccharides and higher levels of fucosylation. The condittoned media also contained lower MW

Reverse‐zymographic analysis of protease nexin‐II/amyloid β protein precursor of human carcinoma cell lines, with special reference to the grade of differentiation and metastatic phenotype

“…These HMTI are immunologically related to APP and thus considered to be PN-IIIAPP. The slightly higher MW of PN-II/APP in the colorectal carcinoma cell lines may reflect heavier glycosylation of the protein (Weidemann et a/., 1989), similar to that of a,-AT produced by carcinoma cell lines, as previously reported (Kataoka et a/., 1993). With RT-PCR study, PN-II/APP isoforms with exon 7 which encodes Kunitztype serine proteinase inhibitor domain were the main molecular species of APP for carcinoma cell lines.…”

“…Three kinds of HMTI can be seen: (i) 180 to 200-kDa HMTI which is seen in RCM-3 and very weakly in CoCM-1; (ii) 130 to 140-kDa HMTI seen in RCM-1, RCM-3, CoCM-1 and Colo 205, which are all colorectal carcinomas; (iii) 110 to 130-kDa HMTI seen in MKN-28, MKN-45, SUIT-2, LC-Uad, T-24, LC-l/sq. In addition, a 60-kDa inhibitor is noted in LC-2iad which might be al-AT because LC-2/ad produced a large amount of al-AT in vitro (Kataoka et al, 1993). SUIT-2 has an additional 43-kDa trypsin inhibitory activity.…”

Identification of Differentially Secreted Biomarkers Using LC-MS/MS in Isogenic Cell Lines Representing a Progression of Breast Cancer

“…Both proteins are serine proteinase inhibitors produced by various tumor cells. While AAT is primarily secreted by the liver [23], it is also secreted by monocytes and certain types of tumors [24][25][26], and is associated with inflammation, infection and other malignant diseases. Its C-terminal fragment can potentiate proliferation, invasiveness and NF-κB (nuclear factor kappa B) activity in breast cancer cells [27].…”

Secretion of α1‐antitrypsin by alveolar epithelial cells

“…Instead of producing A A T tha: contains one tri-and two bi-antennary side chains (as occurs in the liver), A549 processing of A A T m a y result in tri-and/or tetra-antennary sialylated side chains, which suggests a specific glycosyltransferase action. Such high:y branched chains have already been observed in A,~t" isolated from h u m a n hepatoma cell lines [3,4] and from various adenocarcinoma ceil iines [24].…”