By K. Tatemoto (auth.), Professor Martin C. Michel (eds.)
After a bit greater than twenty years because the unique discovery of neuropeptide Y (NPY) through Tatemoto and co-workers, the sector of NPY study has made extraordinary growth and is coming of age.The current quantity addresses all significant subject matters in reference to NPY and similar peptides via proven leaders of their respective parts. skilled NPY-aficionados will surely locate new and necessary more information during this quantity and novices to the sector will confidently notice how a lot intriguing examine this nonetheless has to offer.
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1992 Human Takiyyuddin et al. 1994 GABA, Gamma-aminobutyric acid; VIp, vasointestinal peptide; ANp, atrial natriuretic peptide; CGRp, calcitonin gene-related peptide. 2 Small Vesicles In addition to the storage in LDCV, some members of the NPY family are also stored in smaller vesicles. With a diameter between 30 and 50 nm the so-called synaptic vesicles (SV) are the smallest known membrane-bound organelles (Dannies 1999). 2 Posttranslational Modification As mentioned above, peptides of the NPY family are not synthesized in their final biologically active form.
Pp, PYY and NPY: Synthesis, Storage, Release and Degradation 27 Table 1 Mediators and hormones that are costored with NPY Mediator Cell type/tissue Species References Norepinephrine Sympathetic neurons, vas deferens Cattle, rat de Potter et al. 1998; Fried et al. 1985 GABA Spinal cord, brain Fish, frog Parker et al. 1998; deRijk et al. 1992 VIP Submucos neurons, perivascular nerves Rat, cattle,pig Cox et al. 1994; Majewski et al. 1995 Substance P Submucos neurons, adrenal medulla Guinea pig, cattle Masuku et al.
The aim of thi s chapter is to sum marize key findings about synthesis, storage, relea se and localizati on of NPY famil y peptides, and discu ss recent findings on their degradation by spec ific enzymes . 26 S. von Htirsten et al. 1 Subcellular Storage in Vesicles Polarized cells such as neurons and epithelial cells maintain separate plasma membrane domains, each with a distinct protein and lipid composition and intracellular sorting mechanisms that recognize classes of proteins which ensure that specific vesicles are transported to the correct surface domain (Nillson 1992).
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