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Psychological distress following cancer diagnosis may lead to mental health complications including depression and anxiety. Non-Hodgkin lymphomas (NHLs) include indolent and aggressive subtypes for which treatment and prognosis differ widely. Incident use of psychotropic drugs (PDs - antidepressants, antipsychotics, and anxiolytics) and its correlation to lymphoma types can give insights into the psychological distress these patients endure. In this prospective matched cohort study, we used nationwide population-based registries to investigate the cumulative risk of PD use in NHL patients compared to a sex- and age-matched cohort from the Danish background population. In addition, contact patterns to psychiatric departments and incident intentional self-harm or completed suicide were explored. In total, 8,750 NHL patients and 43,750 matched comparators were included (median age 68; male:female ratio 1.6). Median follow-up was 7.1 years. Two-year cumulative risk of PD use was higher in NHL patients (16.4%) as compared to the matched comparators (5.1%, p

The crustacean pigment-translocating hormones, the red pigment-concentrating hormone (RPCH), an octapeptide, and the light-adapting distal retinal pigment hormone (DRPH), an octadecapeptide, are the first invertebrate neurohormones to be fully characterized. Studies with both purified and synthetic hormones show that, in certain decapods, RPCH is a general pigment-concentrating hormone (PCH), affecting the pigments of all kinds of chromatophores (erythrophores, xanthophores, leucophores and melanophores); the DRPH seems to serve not only light-adapting function, but also act as a general chromatophore pigment-dispersing hormone (PDH). The two hormones thus function as antagonists when regulating the color-adaptation of the decapod crustaceans. PCH activity is widely distributed within the arthropod endocrine systems. The first characterized insect neurohormones, the locust adipokinetic hormones (AKH I and AKH II), show close structural similarities to the crustacean hormone, indicating a common evolution of some of the arthropod neurohormones. Physiological studies of the three hormones (RPCH, AKH I, and AKH II) and their synthetic analogs show that they crossreact, i.e., they all exhibit pigment-concentrating activity when tested on decapod crustaceans, adipokinetic activity when tested on locusts, and hyperglycemic activity when tested on cockroaches, although each of the hormones is more potent in its own system. Structure-function studies show, however, that quite different binding-site requirements exist for the hormones in activating their receptors on the various target tissues. The physiological specificity in their action therefore seems to depend on a differential evolution of the hormone receptors.

Antibodies were raised in rabbits against glycylleucine dipeptidase (EC 3.4.13.2) and proline dipeptidase (EC 3.4.13.9) purified from the pig. IgG fractions were isolated and purified by affinity chromatography on Sepharose (dipeptidase) columns and then used in histological studies on the small intestine and the liver from pig, using the double layer immunofluorescence-staining technique. In the small intestine the dipeptidases were predominantly localized in the cytoplasm of the enterocytes. A reaction was also seen in the leukocyte cytoplasm in the stroma of the small intestine. The dipeptidases were present in the villi but not in the crypts. In the liver the dipeptidases were localized, in the cytoplasm of the hepatocyte, but strong fluorescence was also obtained in the epithelium of the bile ducts. Glycylleucine dipeptidase and proline dipeptidase have been isolated from liver tissue and they were shown to be immunologically identical with the purified intestinal dipeptidases.

1. Red pigment concentrating hormone-like activity (RPCA) has been demonstrated and quantified in the head or cephalic neuroendocrine system of several insects. Schistocerca gregaria adults contained the highest levels of RPCA.2. RPCA was found in all post-embryonic life cycle stages of S. gregaria, and seems to be present in equal quantities in both males and females. Adult locusts contain significantly more RPCA than do immature animals.3. RPCA is concentrated in the locust CC glandular lobe hut is also present in the CC storage lobe, brain and hemolymph of both mature and immature animals. Significant variations in CC RPCA content have been demonstrated in both mature and immature stages.4. Synthetic red pigment concentrating hormone (RPCH) is adipokinetic in both intact and neck-ligatured S. gregaria adults and in intact immature animals. Doses of about 6 ng and 50 ng, respectively, result in minimal and maximal adipokinetic responses. RPCH selectively elevates hemolymph 1.2-diglycerides.5. RPCH in la...

The blanching hormone of the prawn, Pandalus borealis, is pGlu-Leu-Asn-Phe-Ser-Pro-Gly-Trp-NH(2). Its structure was settled by a combination of mass spectrometry and Edman-dansyl analysis of a thermolysin fragment. Confirmation of the structure was obtained by chemical synthesis from amino acids. This neurosecreted hormone is active in picogram amounts when tested in shrimps.

INVESTIGATIONS of intestinal mucosal dipeptidases have been hampered in the past by the lack of suitable assay methods. The methods in use at present1 require relatively large amounts of substrate and are inadequate for the examination of dipeptidase activities in crude tissue extracts or partially purified preparations. The new assay method described here has a wide application and is simple and rapid. It is convenient even when a large number of determinations is required.

DURING the past three decades, investigations of neuro-secretory eye-stalk hormones among crustaceans have revealed a variety of physiological effects produced by eye-stalk ablation as well as by replacement experiments involving injection of extracts of eye-stalk tissue1,2. Resolution of the number of hormones involved in such physiological responses cannot be readily made with the crude extracts so far used. Progress along this line of crustacean endocrinology will evidently depend on isolation and purification of the different hormones, determination of their chemical nature and structure, and testing such purified preparations for the specificity of their physiological effects. Some attempt in this direction with the pigmentary effector hormones indicates that they may be peptide in nature3–5. On the basis of physiological6 and specificity tests7, the light-adapting retinal pigment hormone and the hormone which concentrates pigment in erythrophores appear to be different entities; less-complete separation of retinal pigment hormone and erythrophore-dispersing substance by paper electrophoresis has also been reported8.

KNOWLEDGE about the various types of RNA involved in the biosynthesis of proteins has increased greatly over the past few years. Little is known, however, about the part played by the various ribonucleases (RNases) known to be present in most cells, in the metabolism of the RNA. There has been much speculation on this topic, but few attempts have been made to investigate the physiological action of these substances. This is largely because few of the many RNases identified have been isolated and purified sufficiently to allow them to be characterized. The purification of RNase has great interest at present because of its possible use in the structural analysis of RNA molecules.

IN the course of a study of the N,O-acyl shift at the hydroxyamino-acid residues of proteins (N,O-peptidyl shift) we observed that under certain conditions lysozyme was reversibly inactivated in a way suggestive of a direct dependence on the reversible N,O-peptidyl shift. In earlier work1 on this rearrangement in proteins, concentrated mineral acids were employed, and concomitant, irreversible processes then make it difficult to observe any connexion between the N,O-peptidyl shift and the biological activity. However, a search for milder conditions has revealed that the reaction also takes place in formic acid at ordinary temperature, and apparently without other changes2.