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Biomedical subjects

D M Cowan

Publications and source records attributed to D M Cowan.

7 recordsLinked to original sources

A transputer-based physiological signal processing system. Part 1--System design.

This paper, the first of two, details the design and in-vitro testing of a transputer-based physiological signal processing system. The heart of the system is a transputer-based digital signal processing (DSP) board which can act as a stand-alone spectrum analyser, designed to operate in the audio-frequency band up to 25 kHz. The board comprises a T800 processor, two A100 transversal filters, 12 bit A-D circuitry capable of sampling up to 48 kHz, memory and address mapper. The initial application of the system is for the detection of early arterial disease. For this the DSP board is harnessed to the front end of a multigate pulsed Doppler ultrasound scanner operating at 4.8 MHz insonation frequency and incorporating a vessel wall tracking unit. The complete system performs a Fourier transform on the backscattered signals, providing spectral information on discrete areas of flow (0.6 mm3) across the vessel lumen in real time. This first paper describes the hardware, and the second describes the performance testing of the system on the bench and an assessment of its ability to detect low grade stenoses during steady flow.

Arteries

Structure and expression of a rat agrin.

Agrin is a component of the basal lamina that causes the aggregation of acetylcholine receptors on cultured muscle fibers. An agrin cDNA clone isolated from electromotor neurons of a marine ray was used to characterize the corresponding cDNAs from a rat embryonic spinal cord library. Analysis of a set of clones predicts a 1940 amino acid protein containing 141 cysteine residues. The predicted protein has nine domains homologous to protease inhibitors, a region similar to domain III of laminin, and four epidermal growth factor repeats. The agrin gene is expressed in rat embryonic nervous system and muscle. The rat agrin protein is concentrated at synapses, where it may play a role in development and regeneration.

Agrin

VAMP-1: a synaptic vesicle-associated integral membrane protein.

Several proteins are associated with, or are integral components of, the lipid bilayer that forms the delineating membrane of neuronal synaptic vesicles. To characterize these molecules, we used a polyclonal antiserum raised against purified cholinergic synaptic vesicles from Torpedo to screen a cDNA expression library constructed from mRNA of the electromotor nucleus. One clone encodes VAMP-1 (vesicle-associated membrane protein 1), a nervous-system-specific protein of 120 amino acids whose primary sequence can be divided into three domains: a proline-rich amino terminus, a highly charged internal region, and a hydrophobic carboxyl-terminal domain that is predicted to comprise a membrane anchor. Tryptic digestion of intact and lysed vesicles suggests that the protein faces the cytoplasm, where it may play a role in packaging, transport, or release of neurotransmitters.

Amino Acid Sequence

The production of mammary carcinomas in rats by 9,10-dimethyl-1,2-benzanthracene and its relationship to the oestrous cycle.

Sprague-Dawley rats aged 50 days were given single oral doses of the carcinogen, DMBA.Rats receiving the carcinogen at the same stage of the oestrous cycle were grouped together and mammary tumour production was compared between these groups.When the carcinogen was given during di-oestrus the mean number of tumours per animal was significantly greater than when it was given at other stages in the oestrous cycle. There was considerable variation in total tumour yield from one batch of animals to another.

Animals