[A Solitary PSA-Negative Late Metastasis of Prostate Cancer on the Penis]. / Solitäre PSA-negative Spätmetastase eines Prostatakarzinoms in der Glans penis.

Metastatic involvement of the penis is rare. Secondary lesions generally originate from pelvic tumours. Bladder and prostate are the most common primary tumours. Commonly, penile metastases occur in cases of disseminated cancer disease. We present the case of a prostatic mucinous adenocarcinoma with a solitary, PSA-negative, asymptomatic metastasis to the glans 6 years after radical prostatectomy, which was successfully treated by local excision.

Tetrahydrobiopterin responsiveness in a large series of phenylketonuria patients.

In a group of 87 consecutive patients with hyperphenylalaninaemia born since 1990, only 3 patients showed a (temporary) decrease of serum phenylalanine levels after tetrahydrobiopterin (BH4) loading in usual doses (20 mg/kg body weight).

Phosphorylation of PS II polypeptides inhibits D1 protein-degradation and increases PS II stability.

To study the significance of Photosystem (PS) II phosphorylation for the turnover of the D1 protein, phosphorylation was compared with the synthesis and content of the D1 protein in intact chloroplasts. As shown by radioactive labelling with [(32)Pi] phosphorylation of PS II polypeptides was saturated at light intensities of 125 mol m(-2) s(-1). Under steady state conditions, in intact chloroplasts D1 protein, once it was phosphorylated, was neither dephosphorylated nor degraded in the light. D1 protein-synthesis was measured as incorporation of [(14)C] leucine. As shown by non-denaturing gel-electrophoresis followed by SDS-PAGE newly synthesised D1 protein was assembled to intact PS II-centres and no free D1 protein could be detected. D1 protein-synthesis was saturated at light intensities of 500 mol m(-2) s(-1). The content of D1 protein stayed stable even after illumination with 5000 µmol m(-2) s(-1) showing that D1 protein-degradation was saturated at the same light intensities. The difference in the light saturation points of phosphorylation and of D1 protein-turnover indicates a complex regulation of D1 protein-turnover by phosphorylation. Separation of the phosphorylated and dephosphorylated D1 protein by LiDS-gelelectrophoresis combined with radioactive pulse-labelling with [(14)C] leucine and [(32)Pi] revealed that D1 protein, synthesised under steady state conditions in the light, did not become phosphorylated but instead was rapidly degraded whereas the phosphorylated form of the D1 protein was not a good substrate for degradation. According to these observations phosphorylation of the D1 protein creates a pool of PS II centres which is not involved in D1 to these observations phosphorylation of the D1 protein creates a pool of PS II centres which is not involved in D1 protein-turnover. Fractionation of thylakoid membranes confirms that the phosphorylated, non-turning over pool of PS II-centres was located in the central regions of the grana, whereas PS II-centres involved in D1 protein-turnover were found exclusively in the stroma-lamellae and in the grana-margins.