The timing of prehensile movements in subjects with cerebral palsy.

In this study, a paradigm is presented for the assessment of manual dexterity in subjects with cerebral palsy (CP) that divides the prehensile action into a 'time-to-contact' phase and a 'time-in-contact' phase. Two experiments were performed that determined the effect of object weight on the timing of both phases for the impaired hand and non-impaired hand of subjects with spastic hemiparesis (N = 14). In the first experiment, subjects had to reach for and lift a tube at their own preferred speed. The results showed that the prehensile deficit of the impaired limb is to a large degree manifested by a longer time spent in contact with the object before it was lifted. The time-in-contact phase was decreased after repeated lifts, suggesting that subjects with CP can control and modify force output in advance based on weight information from preceding lifts. In the second experiment speed of movement execution was stressed to examine whether the observed timing pattern of the first experiment is characteristic of prehensile movements of the paretic arm or represents a movement strategy adapted to the disorder. The results of the second experiment showed that subjects could comply with the instruction by reducing the absolute duration of both phases of the prehensile movement. Furthermore, the anticipation effects were eliminated to a large degree. In both experiments the time-in-contact phase was longer for the impaired limb. These results indicate a pathological constant in the time-in-contact phase for the impaired limb. This assumption is discussed in relation to the application of grip and lift forces during this phase. It is concluded that the paradigm is well suited for use in a practical setting as a simple and broad clinical test to assess the prehensile decrements of subjects with CP.

Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13.

In this report, the identification and molecular characterization of a novel gene, designated TM7SF2, is reported. This gene was found in the FAU neighboring area (FAUNA) to which other genes have been mapped previously. The FAUNA gene cluster is located at chromosome 11q13 between landmarks H4B and D11S2196E. The TM7SF2 gene contains eight coding exons, and their splice site consensus sequences are consistent with AG/GT rule. Northern blot analysis with a cDNA probe corresponding to TM7SF2 revealed varying expression levels of a 1.7-kb transcript in adult human heart, brain, pancreas, lung, liver, skeletal muscle, kidney, ovary, prostate, and testis, but no detectable expression in placenta, spleen, thymus, small intestine, colon (mucosal lining), or peripheral blood leukocytes. The open reading frame in the cDNA sequence codes for a protein of 590 amino acids that is rich in glycine (23%) and arginine (17%) residues in its amino-terminal half and contains seven transmembrane domains in its carboxy-terminal half. The transmembrane region of the putative TM7SF2 protein shows amino acid sequence similarity to those of the lamin B receptor and the C14/C24 sterol reductase.

Menin interacts directly with the homeobox-containing protein Pem.

The tumour suppressor gene causing multiple endocrine neoplasia type 1 (MEN1) encodes a 610 amino acid protein, menin. In order to identify menin-interacting proteins we used a yeast two-hybrid assay to screen a 12.5-dpc mouse embryo library with partial menin encompassing amino acids 278 to 476. This identified a homeobox containing protein encoded by a placenta and embryonic expression gene, referred to as Pem. GST-pull-down and coimmunoprecipitation experiments confirmed the interaction. Both proteins colocalised predominantly in the nucleus but were occasionally also found in the cytoplasm. Furthermore, in situ hybridisation studies revealed similarities in their expression patterns in mouse embryos and adult tissues. In adult mice both Men1 and Pem yielded strong signals in testis, Sertoli cells and particularly in seminiferous tubules. Thus, our study has identified that menin interacts with Pem, and the high expression of these proteins in the testis suggests a role in spermatogenesis.