Oestrogen-induced pS2 protein is similar to pancreatic spasmolytic polypeptide and the kringle domain
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منابع مشابه
Oestrogen-induced pS2 protein is similar to pancreatic spasmolytic polypeptide and the kringle domain.
are oestrogen-dependent (Katzenellenbogen, 1980; McGuire, 1980). The MCF-7 cell line (Lippman & Bolan, 1975), a human breast cancer cell line, has been especially useful for understanding the mechanism of action of oestrogen. The pS2 protein (Mr 6500) is an abundant oestrogen-induced protein secreted by MCF-7 cells and found in breast tumour tissue (Masiokowski et al., 1982; Jakowlew et al., 19...
متن کاملExpression of trefoil peptides pS2 and human spasmolytic polypeptide in gastric metaplasia at the margin of duodenal ulcers.
Duodenal ulcers are associated with gastric metaplasia in the duodenum, both at the ulcer margin and at more distant sites in the duodenal bulb. pS2 and human spasmolytic polypeptide (hSP) are secretory peptides expressed in gastric epithelial cells and in gastric metaplasia. As these peptides may be important in ulcer healing, this study investigated the possibility that the expression of pS2 ...
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The human pS2 gene, whose expression is restricted to breast cancer cells, and whose transcription is induced by oestrogen in the human breast cancer cell line MCF-7, has been cloned from both placental and MCF-7 cell DNA. The exon-intron organization has been established by electron microscopy using genomic DNA-cDNA or -mRNA hybrid duplexes and by sequencing the exons and exon-intron junctions...
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1. The process by which the egg-yolk protein precursor vitellogenin is biosynthesized, assembled and secreted by Xenopus laevis (South African clawed toad) liver was studied. It was previously shown in other laboratories that vitellogenin contains the two egg-yolk proteins lipovitellin (mol.wt. 140000) and phosvitin (mol.wt. 35000). 2. Evidence is presented which shows that Xenopus liver micros...
متن کاملNMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
NMR spectroscopy measurements have been used to obtain structural information about the pNR-2/pS2 single-domain trefoil peptide. NMR data from 2D (two dimensional) double-quantum-filtered correlation spectroscopy (DQF-COSY), total correlation spectroscopy (TOCSY), NOE spectroscopy (NOESY), rotating frame NOE spectroscopy (ROESY) and 2D 13C-1H heteronuclear single-quantum coherence (HSQC) and 13...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1988
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2530307