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- Ulvsbäck, M., et al.
(author)
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Gene structure of semenogelin I and II. The predominant proteins in human semen are encoded by two homologous genes on chromosome 20
- 1992
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In: Journal of Biological Chemistry. - 0021-9258. ; 267:25, s. 4-18080
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Journal article (peer-reviewed)abstract
- The genes for semenogelin I and II, the major protein constituents of the human seminal fluid, have been characterized by three overlapping clones in bacteriophage lambda, encompassing 31.5 kilobases (kb) of genomic DNA. The two genes are located 11.5 kb apart in the region q12-q13.1 on chromosome 20. Both genes are relatively compact, spanning only 2.7 and 3.1 kb, respectively. The transcription units are composed of three exons, of which the first encodes the signal peptide, the second encodes the secreted protein, while the third solely contains 3'-noncoding nucleotides. The nucleotide sequences exhibit a similarity of close to 90% in the exons and exceeding 80% in the introns and flanking nucleotides.
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- Rascon, Ana, et al.
(author)
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Identification of the phosphorylation site in vitro for cAMP-dependent protein kinase on the rat adipocyte cGMP-inhibited cAMP phosphodiesterase
- 1994
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In: Journal of Biological Chemistry. - 1083-351X. ; 269:16, s. 11962-11966
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Journal article (peer-reviewed)abstract
- Rat adipocyte cGMP-inhibited cAMP phosphodiesterase (cGI-PDE) appears to be dually regulated in intact cells by serine phosphorylations induced by isoprenaline and insulin, respectively (Degerman, E., Smith, C. J., Tornqvist, H., Vasta, V., Belfrage, P., and Manganiello, V. C. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 533-537; Smith, C. J., Vasta, V., Degerman, E., Belfrage, P., and Manganiello, V. C. (1991) J. Biol. Chem. 266, 13385-13390). Since cAMP-dependent protein kinase (cAMP-PK) catalyzes the beta-adrenergic effects, the site in the isolated cGI-PDE phosphorylated by this kinase was explored. A peptide, LRRSSGASGLLTSEHHSR (P18), corresponding to the amino acid sequence Leu423-Arg440 in the putative regulatory domain of the rat adipocyte cGI-PDE was synthesized. It contains a consensus substrate sequence -RRXS- for cAMP-PK within two tryptic cleavage sites and was readily phosphorylated by cAMP-PK. Two phosphopeptides, identified as RS-[32P]SGASGLLTSEHHSR and S-[32P]SGASGLLTSEHHSR, were obtained after stoichiometric phosphorylation and trypsinization of the peptide. These two peptides and the two main tryptic phosphopeptides obtained from immunoisolated [32P]cGI-PDE phosphorylated with cAMP-PK in a solubilized crude adipocyte membrane fraction were immuno-precipitated by an affinity-purified polyclonal antibody raised against P18 and exhibited the same chromatographic and electrophoretic profiles in three different separation systems. Similar radiosequencing profiles indicated that the second most N-terminal serine, corresponding to Ser-427 in the intact cGI-PDE, was phosphorylated by cAMP-PK in both P18 and authentic cGI-PDE. It is concluded that serine 427 is the target for cAMP-PK phosphorylation of the rat adipocyte cGI-PDE in vitro.
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