The N-terminal domain of chromogranin A (CgA1-40) interacts with monolayers of membrane lipids of fungal and mammalian compositions

Annals of the New York Academy of Sciences

Volumn 971, Issue , 2002, Pages 352-354

  Maget Dana, R ^a   Metz Boutigue, M H ^b   Helle, K B ^c  

^a CENTRE DE BIOPHYSIQUE MOLÉCULAIRE   (France)

^b INSERM   (France)

^c UNIVERSITY OF BERGEN   (Norway)

Author keywords

CgA1 40; CgA7 40; Chromogranin A; Monolayers; Phospholipid

Indexed keywords

CHROMOGRANIN A; MEMBRANE LIPID;

AMINO TERMINAL SEQUENCE; CONFERENCE PAPER; FUNGUS; LIPID COMPOSITION; MAMMAL; MEMBRANE BINDING; NONHUMAN; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION;

FUNGI; MAMMALIA;

EID: 0037024562     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2002.tb04494.x     Document Type: Conference Paper

References (4)

1. Russel, J. et al. 1994. Inhibition of parathyroid hormone secretion by amino-terminal chromogranin peptides. Endocrinology 135: 337-342.
2. Angeletti, R.H. et al. 1994. Vasoinhibiting activity of the synthetic peptides from the amino terminus of the adrenomedullary chromogranin A. Acta Physiol. Scand. 152: 11-19.
3. Lugardon, K. et al. 2000. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. J. Biol. Chem. 275: 10745-10753.
4. Maget-Dana, R. 1999. The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interaction with lipid membranes. Biochim. Biophys. Acta 1462: 109-140.