Measuring the peptides in individual organelles with mass spectrometry

• Published in: Nature biotechnology Vol. 18; no. 2; pp. 172 - 175
• Main Authors: Sweedler, Jonathan V, Rubakhin, Stanislav S, Garden, Rebecca W, Fuller, Robert R
• Format: Journal Article
• Language: English
• Published: New York, NY Nature 01.02.2000; Nature Publishing Group
• Subjects: Animals; Aplysia - chemistry; Aplysia californica; atrial gland; Biological and medical sciences; Biotechnology; Cytoplasmic Granules - chemistry; Diverse techniques; Electron microscopes; Exocrine Glands - chemistry; Fundamental and applied biological sciences. Psychology; Genes; Invertebrate Hormones - analysis; Lasers; Marine; Mass spectrometry; Microscopy; Molecular and cellular biology; Organelles - chemistry; Peptides; Peptides - analysis; Scientific imaging; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods; Matrix isolation; Cell organelle; Aplysia californica; Peptides; Photoionization; Gastropoda; Measurement method; Invertebrata; Mollusca; Mass spectrometry; Laser desorption
• ISSN: 1087-0156; 1546-1696
• DOI: 10.1038/72622

New sampling protocols combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) allow the assay of single dense core vesicles. Understanding the packaging of vesicles is important as vesicles are the quanta of information for intercellular communication. Using vesicles from the exocrine atrial gland of Aplysia californica as the model, a wide range of bioactive peptides are detected within each vesicle. Although the expression of the egg-laying hormone gene family of type 1 atrial gland cells has been previously examined, chemical characterization of individual 1-2 microm diameter vesicles demonstrates that products from several genes are colocalized. The mass sensitivity of MALDI MS can be further improved to enable the analysis of even smaller subcellular organelles.