dynorphins and Carcinoma--Small-Cell

dynorphins has been researched along with Carcinoma--Small-Cell* in 2 studies

Other Studies

2 other study(ies) available for dynorphins and Carcinoma--Small-Cell

Article	Year
A novel soluble protein factor with non-opioid dynorphin A-binding activity. Biochemical and biophysical research communications, 2004, Aug-13, Volume: 321, Issue:1 A novel soluble non-opioid dynorphin A-binding factor (DABF) was identified and characterized in neuronal cell lines, rat spinal cord, and brain. DABF binds dynorphin A(1-17), dynorphin A(2-17), and the 32 amino acid prodynorphin fragment big dynorphin consisting of dynorphin A and B, but not other opioid and non-opioid peptides, opiates, and benzomorphans. The IC50 for dynorphin A(1-17), dynorphin A(2-17), and big dynorphin is in the 5-10 nM range. Using dynorphin A and big dynorphin fragments a binding epitope was mapped to dynorphin A(6-13). DABF has a molecular mass of about 70 kDa. SH-groups are apparently involved in the binding of dynorphin A since p-hydroxy-mercuribenzoic acid inhibited this process. Upon interaction with DABF dynorphin A was converted into Leu-enkephalin, which remained bound to the protein. These data suggest that DABF functions as an oligopeptidase that forms stable and specific complexes with dynorphin A. The presence of DABF in brain structures and other tissues with low level of prodynorphin expression suggests that DABF as an oligopeptidase may degrade other peptides. Dynorphin A at the sites of its release in the CNS may attenuate this degradation as a competitor when it specifically binds to the enzyme. Topics: Animals; Brain; Carcinoma, Small Cell; Carrier Proteins; Cell Line; Cell Line, Tumor; Choriocarcinoma; DDT; Dynorphins; Humans; Hydroxymercuribenzoates; Kinetics; Lung Neoplasms; Mice; Mice, Inbred Strains; Nerve Tissue Proteins; Neuroblastoma; Neurons; Protease Inhibitors	2004
Expression of preprodynorphin in human small cell lung carcinoma cell lines. Regulatory peptides, 1991, Jul-09, Volume: 34, Issue:3 The expression of preprodynorphin has been studied using the Northern blot technique. Ten human cell lines, six small cell lung carcinoma (SCLC), one large cell carcinoma (LCC), two neuroblastoma and one lymphoblast-like cell line, were screened with a preprodynorphin cRNA-probe. Tryptic digestion followed by radioimmunoassay for Leu-enkephalin-Arg6 was used to detect possible translation of the preprodynorphin transcript. Of the ten cell lines investigated we found that all expressed preprodynorphin-mRNA to various degrees, and that this transcript is also translated. Two of the cell lines, neuroblastoma SK-N-MC and SCLC H69, also expressed preproenkephalin-mRNA. This set of cell lines provides a useful model of human origin in which the regulation of the preprodynorphin gene and the posttranslational processing of its products can be studied and compared. Topics: Blotting, Northern; Carcinoma, Small Cell; Dynorphins; Enkephalins; Humans; Protein Precursors; RNA, Messenger; Tumor Cells, Cultured	1991

Article

Year

A novel soluble protein factor with non-opioid dynorphin A-binding activity.

Biochemical and biophysical research communications, 2004, Aug-13, Volume: 321, Issue:1

A novel soluble non-opioid dynorphin A-binding factor (DABF) was identified and characterized in neuronal cell lines, rat spinal cord, and brain. DABF binds dynorphin A(1-17), dynorphin A(2-17), and the 32 amino acid prodynorphin fragment big dynorphin consisting of dynorphin A and B, but not other opioid and non-opioid peptides, opiates, and benzomorphans. The IC50 for dynorphin A(1-17), dynorphin A(2-17), and big dynorphin is in the 5-10 nM range. Using dynorphin A and big dynorphin fragments a binding epitope was mapped to dynorphin A(6-13). DABF has a molecular mass of about 70 kDa. SH-groups are apparently involved in the binding of dynorphin A since p-hydroxy-mercuribenzoic acid inhibited this process. Upon interaction with DABF dynorphin A was converted into Leu-enkephalin, which remained bound to the protein. These data suggest that DABF functions as an oligopeptidase that forms stable and specific complexes with dynorphin A. The presence of DABF in brain structures and other tissues with low level of prodynorphin expression suggests that DABF as an oligopeptidase may degrade other peptides. Dynorphin A at the sites of its release in the CNS may attenuate this degradation as a competitor when it specifically binds to the enzyme.

Topics: Animals; Brain; Carcinoma, Small Cell; Carrier Proteins; Cell Line; Cell Line, Tumor; Choriocarcinoma; DDT; Dynorphins; Humans; Hydroxymercuribenzoates; Kinetics; Lung Neoplasms; Mice; Mice, Inbred Strains; Nerve Tissue Proteins; Neuroblastoma; Neurons; Protease Inhibitors

2004

Expression of preprodynorphin in human small cell lung carcinoma cell lines.

Regulatory peptides, 1991, Jul-09, Volume: 34, Issue:3

The expression of preprodynorphin has been studied using the Northern blot technique. Ten human cell lines, six small cell lung carcinoma (SCLC), one large cell carcinoma (LCC), two neuroblastoma and one lymphoblast-like cell line, were screened with a preprodynorphin cRNA-probe. Tryptic digestion followed by radioimmunoassay for Leu-enkephalin-Arg6 was used to detect possible translation of the preprodynorphin transcript. Of the ten cell lines investigated we found that all expressed preprodynorphin-mRNA to various degrees, and that this transcript is also translated. Two of the cell lines, neuroblastoma SK-N-MC and SCLC H69, also expressed preproenkephalin-mRNA. This set of cell lines provides a useful model of human origin in which the regulation of the preprodynorphin gene and the posttranslational processing of its products can be studied and compared.

Topics: Blotting, Northern; Carcinoma, Small Cell; Dynorphins; Enkephalins; Humans; Protein Precursors; RNA, Messenger; Tumor Cells, Cultured

1991